195 results on '"Collagen solubility"'
Search Results
2. Effects of Dietary Energy Density in a Fermented Total Mixed Ration Formulated with Different Ratios of Rice Straw and Cassava Pulp on 2- or 14-Day-Aged Meat Quality, Collagen, Fatty Acids, and Ribonucleotides of Native Thai Cattle Longissimus Muscle.
- Author
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Chaosap, Chanporn, Lukkananukool, Achara, Polyorach, Sineenart, Sommart, Kritapon, Sivapirunthep, Panneepa, and Limsupavanich, Rutcharin
- Subjects
CASSAVA ,RICE straw ,ENERGY density ,RIBONUCLEOTIDES ,MEAT quality ,FATTY acids ,MEAT aging - Abstract
This study investigated the effects of dietary energy density in rice straw and cassava pulp fermented total mixed ration on pH, cooking loss, Warner–Bratzler shear force (WBSF), and collagen content of 2- or 14-d-aged native Thai cattle (NTC) Longissimus thoracic (LT) muscles and fatty acids and ribonucleotides of 2-d-aged LT. Eighteen yearling NTC (Bos indicus) were randomly divided into three dietary treatments (T1 = 8.9, T2 = 9.7, and T3 = 10.5 MJ ME/kg), with six bulls per treatment. The results showed that T1 had the highest WBSF (p < 0.05). However, T2 had similar WBSF to T3 (p > 0.05). With aging, cooking loss increased (p < 0.01), while WBSF decreased (p < 0.01). Insoluble and total collagen decreased with aging (p < 0.05). Dietary energy density had no effect (p > 0.05) on collagen content, ribonucleotides and most fatty acids. However, T1 had more (p < 0.05) decanoic (C10:0), vaccenic (C18:1n9t), trans-linolelaidic (C18:2n6t), eicosatrienoic (C20:3n6), and docosadienoic (C22:2) acids than T2 and T3. In terms of lowest feed cost with comparable tenderness to T2 and highest energy density, T3 may be well suited for feeding NTC. Aging for 14 days improves LT tenderness, but its cooking loss may affect yield and juiciness. [ABSTRACT FROM AUTHOR]
- Published
- 2022
- Full Text
- View/download PDF
3. Assessment of gelatinolytic proteinases in chilled grass carp (Ctenopharyngodon idellus) fillets: characterization and contribution to texture softening.
- Author
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Shen, Jiandong, Jiang, Qixing, Zhang, Wei, Xu, Yanshun, and Xia, Wenshui
- Subjects
- *
CTENOPHARYNGODON idella , *FISH fillets , *PROTEINASES , *SERINE proteinases , *METALLOPROTEINASES , *CHEMICAL industry - Abstract
BACKGROUND Texture softening is always a problem during chilling of grass carp fillets. To solve this problem and provide for better quality of flesh, understanding the mechanism of softening is necessary. Gelatinolytic proteinases are suspected to play an essential role in the disintegration of collagen in softening of fish flesh. In the present study, the types and contribution of gelatinolytic proteinases in chilled fillets were investigated. RESULTS: Four active bands (G1, 250 kDa; G2, 68 kDa; G3, 66 kDa; G4, 29 kDa) of gelatinolytic proteinases were identified in grass carp fillets by gelatin zymography. The effect of inhibitors and metal ions revealed that G1 was possibly a serine proteinase, G2 and G3 were calcium‐dependent metalloproteinases and G4 was a cysteine proteinase. The effect of the inhibitors phenylmethanesulfonyl fluoride (PMSF), l‐3‐carboxy‐trans‐2,3‐epoxy‐propionyl‐l‐leucine‐4‐guanidinobutylamide (E‐64) and 1,10‐phenanthroline (Phen) on chilled fillets revealed that gelatinolytic proteinase activities were significantly suppressed. Collagen solubility indicated that metalloproteinase and serine proteinase played critical roles in collagen breakdown during the first 3 days, and cysteine proteinase revealed its effect after 3 days. Meanwhile, during chilled storage for 11 days, the final values of shear force increased 19.68% and 24.33% in PMSF and E‐64 treatments when compared to control fillets respectively, whereas the increase after Phen treatment was 49.89%. CONCLUSION: Our study concluded that the disintegration of collagen in post‐mortem softening of grass carp fillets was mainly mediated by metalloproteinase and to a lesser extent by serine proteinase and cysteine proteinase. © 2021 Society of Chemical Industry. [ABSTRACT FROM AUTHOR]
- Published
- 2022
- Full Text
- View/download PDF
4. Major Optical Clearing Mechanisms
- Author
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Oliveira, Luís Manuel Couto, Tuchin, Valery Victorovich, Ananthanarayan, Balasubramanian, Series Editor, Babaev, Egor, Series Editor, Bremer, Malcolm, Series Editor, Calmet, Xavier, Series Editor, Di Lodovico, Francesca, Series Editor, Esquinazi, Pablo D., Series Editor, Hoogerland, Maarten, Series Editor, Le Ru, Eric, Series Editor, Lewerenz, Hans-Joachim, Series Editor, Narducci, Dario, Series Editor, Overduin, James, Series Editor, Petkov, Vesselin, Series Editor, Theisen, Stefan, Series Editor, Wang, Charles H.-T., Series Editor, Wells, James D., Series Editor, Whitaker, Andrew, Series Editor, Oliveira, Luís Manuel Couto, and Tuchin, Valery Victorovich
- Published
- 2019
- Full Text
- View/download PDF
5. Investigation of the solubility and dispersion degree of calf skin collagen in ionic liquids
- Author
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Sicong Liu, Qian Li, and Guoying Li
- Subjects
Ionic liquids concentrations ,Collagen solubility ,Structural integrity ,Dispersion degree ,Aggregation state ,Chemical technology ,TP1-1185 - Abstract
Abstract The dissolution of collagen in ionic liquids (ILs) was highly dependent on the polarity of ILs, which was influenced by their sorts and concentrations. Herein, the solubility and dispersion degree of collagen in two sorts of ILs, namely 1-ethyl-methylimidazolium tetrafluoroborate ([EMIM][BF4]) with low polarity and 1-ethyl-3-methylimidazolium acetate ([EMIM][Ac]) with high polarity in a concentration range from 10% to 70% at 10 °C were investigated. When 150 mg of collagen was added to 30 mg of ILs, the minimum soluble collagen concentration was 0.02 mg/mL in 70% [EMIM][BF4] with lowest polarity and the maximum was 3.57 mg/mL in 70% [EMIM][Ac] with highest polarity, which indicates that soluble collagen and insoluble collagen fibers were both present. For insoluble collagens, differential scanning calorimetry showed that the thermal-stability was weakened when increasing the ILs concentration and polarity, and the fiber arrangement was looser with a more uniform lyophilized structure, observed by atomic force microscopy and scanning electron microscopy. For soluble collagens, electrophoresis patterns and Fourier transform infrared spectroscopy showed that no polypeptide chain degradation occurred during dissolution, but the thermal denaturation temperature decreased by 0.26 °C~ 7.63 °C with the increase of ILs concentrations, measured by ultra-sensitive differential scanning calorimetry. Moreover, the aggregation of collagen molecules was reduced when ILs polarity was increased as determined by fluorescence measurements and dynamic light scattering, which resulted in an increased loose fiber arrangement observed by atomic force microscopy. If the structural integrity of collagen needs to be retained, then the ILs sorts and concentrations should be considered. Graphical abstract
- Published
- 2019
- Full Text
- View/download PDF
6. Effects of Dietary Energy Density in a Fermented Total Mixed Ration Formulated with Different Ratios of Rice Straw and Cassava Pulp on 2- or 14-Day-Aged Meat Quality, Collagen, Fatty Acids, and Ribonucleotides of Native Thai Cattle Longissimus Muscle
- Author
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Chanporn Chaosap, Achara Lukkananukool, Sineenart Polyorach, Kritapon Sommart, Panneepa Sivapirunthep, and Rutcharin Limsupavanich
- Subjects
beef ,aging ,collagen solubility ,inosine monophosphate ,meat flavor ,Chemical technology ,TP1-1185 - Abstract
This study investigated the effects of dietary energy density in rice straw and cassava pulp fermented total mixed ration on pH, cooking loss, Warner–Bratzler shear force (WBSF), and collagen content of 2- or 14-d-aged native Thai cattle (NTC) Longissimus thoracic (LT) muscles and fatty acids and ribonucleotides of 2-d-aged LT. Eighteen yearling NTC (Bos indicus) were randomly divided into three dietary treatments (T1 = 8.9, T2 = 9.7, and T3 = 10.5 MJ ME/kg), with six bulls per treatment. The results showed that T1 had the highest WBSF (p < 0.05). However, T2 had similar WBSF to T3 (p > 0.05). With aging, cooking loss increased (p < 0.01), while WBSF decreased (p < 0.01). Insoluble and total collagen decreased with aging (p < 0.05). Dietary energy density had no effect (p > 0.05) on collagen content, ribonucleotides and most fatty acids. However, T1 had more (p < 0.05) decanoic (C10:0), vaccenic (C18:1n9t), trans-linolelaidic (C18:2n6t), eicosatrienoic (C20:3n6), and docosadienoic (C22:2) acids than T2 and T3. In terms of lowest feed cost with comparable tenderness to T2 and highest energy density, T3 may be well suited for feeding NTC. Aging for 14 days improves LT tenderness, but its cooking loss may affect yield and juiciness.
- Published
- 2022
- Full Text
- View/download PDF
7. Relevance of collagen solubility and gelatinolytic proteinase activity for texture softening in chilled grass carp (Ctenopharyngodon idellus) fillets.
- Author
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Shen, Jiandong, Yu, Dawei, Gao, Pei, Xu, Yanshun, Jiang, Qixing, and Xia, Wenshui
- Subjects
- *
CTENOPHARYNGODON idella , *COLLAGEN , *SOLUBILITY , *SHEARING force , *FOOD texture - Abstract
Summary: The aim of the present study was to investigate the underlying mechanisms of softening texture in chilled grass carp filletsunderpinning collagen solubility, gelatinolytic proteinase activity and physicochemical parameters. Acid‐soluble collagen (ASC) and heat soluble collagen (HSC) increased markedly, while a significant decline was detected in total collagen and insoluble collagen (ISC) during the first 3 days of storage, coinciding with a loss of shear force and water‐holding capacity (WHC) (P < 0.05). Moreover, the activity of gelatinolytic proteinases was gradually activated and reached the peak at day 3 (P < 0.05). Pearson coefficient analysis showed that gelatinolytic proteinase activity revealed a significant correlation with collagen solubility. Total collagen, ASC, ISC and HSC were significantly correlated with shear force and WHC. Our study clarified that the increase of collagen solubility by gelatinolytic proteinases played an important role for texture softening in the early stage of chilled grass carp fillets. [ABSTRACT FROM AUTHOR]
- Published
- 2021
- Full Text
- View/download PDF
8. Investigation of the solubility and dispersion degree of calf skin collagen in ionic liquids.
- Author
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Liu, Sicong, Li, Qian, and Li, Guoying
- Subjects
TETRAFLUOROBORATES ,SCANNING force microscopy ,COLLAGEN ,FOURIER transform infrared spectroscopy ,IONIC liquids ,ATOMIC force microscopy ,NEAR infrared spectroscopy - Abstract
The dissolution of collagen in ionic liquids (ILs) was highly dependent on the polarity of ILs, which was influenced by their sorts and concentrations. Herein, the solubility and dispersion degree of collagen in two sorts of ILs, namely 1-ethyl-methylimidazolium tetrafluoroborate ([EMIM][BF
4 ]) with low polarity and 1-ethyl-3-methylimidazolium acetate ([EMIM][Ac]) with high polarity in a concentration range from 10% to 70% at 10 °C were investigated. When 150 mg of collagen was added to 30 mg of ILs, the minimum soluble collagen concentration was 0.02 mg/mL in 70% [EMIM][BF4 ] with lowest polarity and the maximum was 3.57 mg/mL in 70% [EMIM][Ac] with highest polarity, which indicates that soluble collagen and insoluble collagen fibers were both present. For insoluble collagens, differential scanning calorimetry showed that the thermal-stability was weakened when increasing the ILs concentration and polarity, and the fiber arrangement was looser with a more uniform lyophilized structure, observed by atomic force microscopy and scanning electron microscopy. For soluble collagens, electrophoresis patterns and Fourier transform infrared spectroscopy showed that no polypeptide chain degradation occurred during dissolution, but the thermal denaturation temperature decreased by 0.26 °C~ 7.63 °C with the increase of ILs concentrations, measured by ultra-sensitive differential scanning calorimetry. Moreover, the aggregation of collagen molecules was reduced when ILs polarity was increased as determined by fluorescence measurements and dynamic light scattering, which resulted in an increased loose fiber arrangement observed by atomic force microscopy. If the structural integrity of collagen needs to be retained, then the ILs sorts and concentrations should be considered. [ABSTRACT FROM AUTHOR]- Published
- 2019
- Full Text
- View/download PDF
9. Revisiting optical clearing with dimethyl sulfoxide (DMSO)
- Author
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Bui, Albert K, McClure, R Anthony, Chang, Jennell, Stoianovici, Charles, Hirshburg, Jason, Yeh, Alvin T, and Choi, Bernard
- Subjects
Biomedical and Clinical Sciences ,Clinical Sciences ,Dimethyl Sulfoxide ,Humans ,In Vitro Techniques ,Skin ,glycerol ,hyperosmotic agents ,collagen dissociation ,collagen solubility ,integrating spheres ,Dermatology & Venereal Diseases ,Clinical sciences ,Dentistry - Abstract
Functional optical characterization of disease progression and response to therapy suffers from loss of spatial resolution and imaging depth due to scattering. Here we report on the ability of dimethyl sulfoxide (DMSO) alone to reduce the optical scattering of skin. We observed a threefold reduction in the scattering of skin with topical DMSO application. With an in vivo window chamber model, we observed a threefold increase in light transmittance through the preparation and enhanced visualization of subsurface microvasculature. Collectively, our data demonstrate the potential of DMSO alone to mitigate effects of scattering, which we expect will improve molecular imaging studies.
- Published
- 2009
10. Effect of Different Temperature and Time Combinations on Quality Characteristics of Sous-vide Cooked Goat Gluteus Medius and Biceps Femoris.
- Author
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Ismail, Ishamri, Hwang, Young-Hwa, and Joo, Seon-Tea
- Subjects
- *
BICEPS femoris , *TEMPERATURE effect , *GLUTEAL muscles , *SHEARING force , *HEAT treatment , *COLORS - Abstract
The combination of proper temperature and time duration in sous-vide cooking could provide good water-holding capacity, color parameters, and tender cooked meat. In this study, goat muscles gluteus medius (GM) and biceps femoris (BF) treated with single-stage sous-vide (cooked at 60 °C, 65 °C, 70 °C) and two-stage sous-vide (cooked at 45 and 60 °C, 45 and 65 °C, 45 and 70 °C) methods for 6 h and 12 h were compared. Cooking loss decreased by 5–10% for GM and 10–13% for BF after 6 h of heat treatment with two-stage sous-vide likely due to high sarcoplasmic solubility. Cooking time and temperature combination in two-stage sous-vide contributed to better a* values for both GM and BF, with higher values recorded for 6 h at 45 and 60 °C. Significant reduction of toughness was successfully achieved using stepped cooking temperatures compared with sous-vide cooking at a single temperature. The lowest shear force values were achieved at a combined temperature of 45 and 60 °C with only 6 h of cooking duration (GM 28 N; BF 40 N) likely from desmin degradation. However, the tenderness effect of single-stage sous-vide was seen after collagen solubility was maximized in prolonged cooking at 70 °C, but other quality features such as redness values and water content had recorded the lowest values. [ABSTRACT FROM AUTHOR]
- Published
- 2019
- Full Text
- View/download PDF
11. MEAT SCIENCE AND MUSCLE BIOLOGY SYMPOSIUM: BIOLOGICAL INFLUENCERS OF MEAT PALATABILITY: Production factors affecting the contribution of collagen to beef toughness,.
- Author
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Bruce, Heather L and Roy, Bimol C
- Subjects
- *
BEEF , *MEAT , *BEEF quality , *COLLAGEN , *PYRIDINOLINE , *MEAT science - Abstract
Intramuscular collagen may affect the value of meat by limiting its tenderness and cooking convenience. Production factors such as age of animal at slaughter, the use of steroids and beta-adrenergic agonists as growth promotants, and cattle breed may affect the contribution of collagen to beef quality. Recent research has indicated that concentrations of the mature collagen cross-link pyridinoline (PYR) are positively correlated with Warner-Bratzler shear force (WBSF) and animal age at slaughter, while contribution of the concentration of a second mature collagen cross-link Ehrlich's Chromogen (EC) to beef toughness declines with cattle age. Cattle breed influences total collagen content of muscle due to differing rates of maturation among breeds. Growth promoting technologies do not appear to affect collagen solubility, but do influence PYR and EC densities and concentrations in some beef muscles. Concentrations of PYR and EC do not account for all the variation in collagen heat solubility in beef muscles, nor do advanced glycation end products given the relative immaturity of cattle at slaughter. In light of this, other collagen cross-links such as heat-stable divalent cross-links may warrant reconsideration with regard to their contribution to cooked beef toughness. [ABSTRACT FROM AUTHOR]
- Published
- 2019
- Full Text
- View/download PDF
12. MEAT SCIENCE AND MUSCLE BIOLOGY SYMPOSIUM: BIOLOGICAL INFLUENCERS OF MEAT PALATABILITY: Production factors affecting the contribution of collagen to beef toughness,.
- Author
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Bruce, Heather L and Roy, Bimol C
- Subjects
BEEF ,MEAT ,BEEF quality ,COLLAGEN ,PYRIDINOLINE ,MEAT science - Abstract
Intramuscular collagen may affect the value of meat by limiting its tenderness and cooking convenience. Production factors such as age of animal at slaughter, the use of steroids and beta-adrenergic agonists as growth promotants, and cattle breed may affect the contribution of collagen to beef quality. Recent research has indicated that concentrations of the mature collagen cross-link pyridinoline (PYR) are positively correlated with Warner-Bratzler shear force (WBSF) and animal age at slaughter, while contribution of the concentration of a second mature collagen cross-link Ehrlich's Chromogen (EC) to beef toughness declines with cattle age. Cattle breed influences total collagen content of muscle due to differing rates of maturation among breeds. Growth promoting technologies do not appear to affect collagen solubility, but do influence PYR and EC densities and concentrations in some beef muscles. Concentrations of PYR and EC do not account for all the variation in collagen heat solubility in beef muscles, nor do advanced glycation end products given the relative immaturity of cattle at slaughter. In light of this, other collagen cross-links such as heat-stable divalent cross-links may warrant reconsideration with regard to their contribution to cooked beef toughness. [ABSTRACT FROM AUTHOR]
- Published
- 2019
- Full Text
- View/download PDF
13. THE EFFECT OF WATER VAPOR PRESSURE ON MUSCLE COLLAGEN SOLUBILITY AND SELECTED CHARACTERISTICS OF THE LONGISSIMUS LUMBORUM MUSCLE IN CROSSBRED CATTLE.
- Author
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Głowińska, Beata, Młynek, Krzysztof, Dzido, Alicja, and Salomończyk, Ewa
- Subjects
- *
WATER vapor , *COLLAGEN , *ERECTOR spinae muscles , *BEEF industry , *AMINO acids - Abstract
Most scientific studies are dedicated to the possibility of preparing beef for consumption under industrial conditions. Few publications are devoted to the issue of collagen thermohydrolysis in conditions available to the consumer. This study has analyzed the effect of small values of water vapor pressure on major culinary indices and chemical components of the longissimus lumborum muscle obtained from bulls with different growth rates. The experiment involved 48 animals. On the basis of the gain during the fattening time, the animals were divided into a low growth intensity group, with a daily body weight gain of =900 g, and a high growth intensity group with a daily gain of >900 g/day. A part of the samples of the longissimus lumborum muscle (control) was thermally treated in a water bath at 75°C. Another part was heat treated in a pressure-pot at 150°C, at a pressure of 0.1 MPa. The next part of samples was subjected to the same temperature, but the pressure was 0.2 MPa. The obtained results indicate that the values of the studied indices were largely affected by thermal processing parameters rather than the animals' growth rate. The highest contents of total protein and water-soluble collagen were obtained in the case of a temperature of 150°C and the highest pressure (0.2 MPa). Water vapor with increased temperature and pressure also created favorable conditions for obtaining better meat tenderness and more favorable values of the water holding capacity. The latter characteristic appeared to be strongly connected with an increasing amount of water-soluble collagen, which was confirmed by relatively high values of the correlation coefficient between these characteristics. A strong positive correlation was also shown between thermal drip and the total collagen content in meat. [ABSTRACT FROM AUTHOR]
- Published
- 2018
- Full Text
- View/download PDF
14. Relevance of collagen solubility and gelatinolytic proteinase activity for texture softening in chilled grass carp ( Ctenopharyngodon idellus ) fillets
- Author
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Yanshun Xu, Wenshui Xia, Qixing Jiang, Jiandong Shen, Pei Gao, and Dawei Yu
- Subjects
Collagen solubility ,Ctenopharyngodon idellus ,biology ,Chemistry ,Proteinase activity ,Food science ,Texture (crystalline) ,biology.organism_classification ,Softening ,Industrial and Manufacturing Engineering ,Food Science ,Grass carp - Published
- 2020
15. Effect of visual marbling levels in pork loins on meat quality and Thai consumer acceptance and purchase intent
- Author
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Chanporn Chaosap, Suntaree Suwonsichon, Sawankamol Noidad, and Rutcharin Limsupavanich
- Subjects
Marbled meat ,lcsh:Animal biochemistry ,Increased ph ,Loin ,intramuscular fat ,Article ,Collagen solubility ,Animal science ,purchase intent ,Animal Products ,medicine ,Palatability ,lcsh:QP501-801 ,Longissimus dorsi ,lcsh:SF1-1100 ,Mathematics ,pork loin quality ,0402 animal and dairy science ,04 agricultural and veterinary sciences ,040201 dairy & animal science ,visual marbling level ,Tenderness ,Animal Science and Zoology ,lcsh:Animal culture ,Intramuscular fat ,medicine.symptom ,meat physicochemical traits ,consumer palatability responses ,Food Science - Abstract
Objective We investigated visual marbling level (VML) influence on pork loin physicochemical traits, consumer palatability responses, VML liking, purchase intent, and their relationships. Methods For each of five slaughtering dates, at 24-h postmortem, nine paired Duroc castrated male boneless Longissimus dorsi (LD) muscles were categorized into low (LM, score 1 to 2, n = 3), medium (MM, score 3 to 4, n = 3), and high (HM, score 5 to 6, n = 3) VML. Meat physicochemical quality traits and consumer responses (n = 389) on palatability and VML liking, and purchase intent were evaluated. The experiment was in randomized complete block design. Analysis of variance, Duncan’s multiple mean comparisons, and correlation coefficients were determined. Results VML correspond to crude fat (r = 0.91, p0.05). Compared to the others, HM had lower collagen solubility percentage (p0.05) Warner-Bratzler shear force (WBSF). No differences (p>0.05) were found in juiciness, overall flavor, oiliness, and overall acceptability, but HM was more tender (p0.05). Corresponding to VML preference (r = 0.45, p
- Published
- 2019
16. Improving the physico-chemical and sensory characteristics of camel meat burger patties using ginger extract and papain.
- Author
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Abdel-Naeem, Heba H.S. and Mohamed, Hussein M.H.
- Subjects
- *
CAMEL meat , *GINGER , *PLANT extracts , *MYOFIBRILS , *FOOD production , *COOKING - Abstract
The objective of the current study was to include tenderizing agents in the formulation of camel meat burger patties to improve the physico-chemical and sensory characteristics of the product. Camel meat burger patties were processed with addition of ginger extract (7%), papain (0.01%) and mixture of ginger extract (5%) and papain (0.005%) in addition to control. Addition of ginger, papain and their mixture resulted in significant ( P < 0.05) increase of the collagen solubility and sensory scores (juiciness, tenderness and overall acceptability) with significant ( P < 0.05) reduction of the shear force values. Ginger extract resulted in extensive fragmentation of myofibrils; however, papain extract caused noticeable destructive effect on connective tissue. Moreover, ginger and papain resulted in improvement of the lipid stability of treated burger patties during storage. Therefore, addition of ginger extract and papain powder during formulation of camel burger patties can improve their physico-chemical and sensory properties. [ABSTRACT FROM AUTHOR]
- Published
- 2016
- Full Text
- View/download PDF
17. Effect of Collagen Crosslinking on Collagen-Water Interaction
- Author
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Bonnet, Madeleine, Kopp, J., Renou, J. P., Vasilescu, D., editor, Jaz, J., editor, Packer, L., editor, and Pullman, B., editor
- Published
- 1990
- Full Text
- View/download PDF
18. Profiling of Catfish Swim Bladder Collagen (Pangasius sp.) Through Enzymatic Proses
- Author
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Uju Uju, Wini Trilaksani, and Gevbry Ranti Ramadhani Simamora
- Subjects
lcsh:SH1-691 ,chemistry.chemical_classification ,Chromatography ,Chemistry ,alkaline, papain enzyme, fungsional group, pretreatment ,lcsh:Aquaculture. Fisheries. Angling ,Collagen solubility ,Papain ,chemistry.chemical_compound ,Pangasius sp ,Enzyme ,Swim bladder ,Potential source ,Catfish - Abstract
Swim bladder is a marine byproduct and a potential source of collagen needed by food, cosmetical, biomedical and pharmaceutical industry. This study evaluated the effectiveness of alkaline pretreatment and papain enzyme on the characteristics of collagen from the catfish swim bladders. TThree concentrations of alkaline (0.05; 0.1 and 0.15 M) with were used to pretreat the swim bladders for 2; 4; 6; 8; 10 and 12 hours. The collagen was also treated by papain enzyme with concentrations of 0; 5,000; 10,000; 15,000 and 20,000 U/mg for 24 and 48 hours. The result showed that pretreatment using NaOH 0.05 M for 6 hours effectively reduced the noncollagen protein (p
- Published
- 2019
19. The Use of Syrian Sumac (Rhus coriaria) as a Meat Tenderizer: Effect on Fat, Protein and Collagen Profiles on Pectoralis superficialis Cut
- Author
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Sami El Khatib and Khaula Sakhr
- Subjects
collagen ,0106 biological sciences ,fat content ,business.product_category ,syrian sumac ,Fat content ,three-phase partitioning ,01 natural sciences ,Meat tenderizer ,lcsh:Agriculture ,Protein content ,Collagen solubility ,Meat tenderness ,0404 agricultural biotechnology ,meat tenderness ,010608 biotechnology ,Food science ,lcsh:Agriculture (General) ,Lipase ,biology ,Chemistry ,lcsh:S ,food and beverages ,04 agricultural and veterinary sciences ,General Medicine ,biology.organism_classification ,lcsh:S1-972 ,040401 food science ,Rhus coriaria ,biology.protein ,business - Abstract
The Syrian Sumac (Rhus coriaria) is a widely used spice in the Arab world of attractive economic importance in food, cosmetic and pharmaceutical industries. Meat tenderness is one of the very most important factors for customers‘ acceptability. The global objective of this study was to add an additional value to Sumac by evaluating its meat tenderizing effect. Crude sumac fruits were used to create three different extracts (aqueous, ethanolic and purified enzymatic extract). Pectoralis superficialis cuts were treated with the extracts and studied for their shear stress, pH, protein and fat contents and collagen. The hypothesis that Sumac could have a meat tenderizing effect was supported by our results showing a significant decrease in shear stress and protein content with increase in collagen solubility. Moreover, an effect on decreasing meat fat was detected, where the aqueous sumac extract decreased significantly the fat percentage in meat. The active enzymes in Sumac were shown to be variate in nature, lipase and protease, with a significant effect on collagen, thus proving Sumac‘s possibility to be potentially used as a meat tenderizer.
- Published
- 2019
20. Effects of Alkaline Pretreatment on the Characteristics of Collagen from Mangrove Conch (Telescopium telescopium)
- Author
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Riyan Triono and Sri Purwaningsih
- Subjects
lcsh:SH1-691 ,biology ,amino acids, gastropod, proline, yield ,Telescopium telescopium ,Snail ,biology.organism_classification ,lcsh:Aquaculture. Fisheries. Angling ,Conch ,Acetic acid ,chemistry.chemical_compound ,Collagen solubility ,chemistry ,biology.animal ,medicine ,Food science ,Proline ,Swelling ,medicine.symptom ,Mangrove - Abstract
The horn snail (Telescopium telescopium) is a gastropod living in mangrove forests and is considered as a pond pest. This study was aimed to determine the effects of alkaline and acetic acid pretreatment on the characteristics of collagen from the horn snail meat. The immersion of the meat in NaOH 0.20% for 10 hours gave a significant reduction in non-collagen protein content (α = 0.05). Further immersion with acetic acid 0.05% for 6 hours also significantly affected (α = 0.05) the swelling degree and the collagen solubility. The extraction yield was 1.08±0.21%, with 72.23% of brightness, and the viscosity was 16.34 cP. The proline content of the collagen was 9.21%.
- Published
- 2019
21. Effect of Different Temperature and Time Combinations on Quality Characteristics of Sous-vide Cooked Goat Gluteus Medius and Biceps Femoris
- Author
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Seon-Tea Joo, Young-Hwa Hwang, and Ishamri Ismail
- Subjects
0106 biological sciences ,biology ,Chemistry ,Process Chemistry and Technology ,Sous vide ,food and beverages ,04 agricultural and veterinary sciences ,Time duration ,biology.organism_classification ,040401 food science ,01 natural sciences ,Biceps ,Industrial and Manufacturing Engineering ,Tenderness ,Medius ,Collagen solubility ,0404 agricultural biotechnology ,010608 biotechnology ,medicine ,Cooked meat ,Food science ,medicine.symptom ,Safety, Risk, Reliability and Quality ,Quality characteristics ,Food Science - Abstract
The combination of proper temperature and time duration in sous-vide cooking could provide good water-holding capacity, color parameters, and tender cooked meat. In this study, goat muscles gluteus medius (GM) and biceps femoris (BF) treated with single-stage sous-vide (cooked at 60 °C, 65 °C, 70 °C) and two-stage sous-vide (cooked at 45 and 60 °C, 45 and 65 °C, 45 and 70 °C) methods for 6 h and 12 h were compared. Cooking loss decreased by 5–10% for GM and 10–13% for BF after 6 h of heat treatment with two-stage sous-vide likely due to high sarcoplasmic solubility. Cooking time and temperature combination in two-stage sous-vide contributed to better a* values for both GM and BF, with higher values recorded for 6 h at 45 and 60 °C. Significant reduction of toughness was successfully achieved using stepped cooking temperatures compared with sous-vide cooking at a single temperature. The lowest shear force values were achieved at a combined temperature of 45 and 60 °C with only 6 h of cooking duration (GM 28 N; BF 40 N) likely from desmin degradation. However, the tenderness effect of single-stage sous-vide was seen after collagen solubility was maximized in prolonged cooking at 70 °C, but other quality features such as redness values and water content had recorded the lowest values.
- Published
- 2019
22. Quality and Safety Considerations of Incorporating Post-PEF Ageing into the Pulsed Electric Fields and Sous Vide Processing Chain
- Author
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Patrick Silcock, Indrawati Oey, Amali U. Alahakoon, and Phil Bremer
- Subjects
0106 biological sciences ,Chemistry ,Process Chemistry and Technology ,Sous vide ,04 agricultural and veterinary sciences ,040401 food science ,01 natural sciences ,Industrial and Manufacturing Engineering ,Tenderness ,Collagen solubility ,0404 agricultural biotechnology ,Lipid oxidation ,Ageing ,010608 biotechnology ,Electric field ,medicine ,Food science ,medicine.symptom ,Safety, Risk, Reliability and Quality ,Food quality ,Food Science - Abstract
The effect of pulsed electric fields (0.7 and 1.5 kV/cm, specific energy 90–100 kJ/kg) processing followed by post–pulsed electric field (PEF) ageing ( 0, 3, 7, 14 days) on the safety and quality attributes of sous vide–processed (60 °C/12 or 24 h) beef briskets was assessed. Ageing did not significantly reduce the hardness of sous vide–processed meat except for those PEF treated either at 0.7 kV/cm followed by sous vide processing for 12 h or at 1.5 kV/cm followed by sous vide processing for 24 h. Post-PEF ageing time had no effect on the collagen solubility of sous vide–processed meat. The effect of PEF treatment on hardness was much greater than the effect of ageing time, and sous vide processing time. Sous vide processing (12 or 24 h) for all treatments reduced both aerobic and lactic acid bacteria numbers to below the detection limit. Initial peptide concentrations during in vitro peptic digestibility were significantly (P 0.05) differences were observed in digestion rates between any treatment. Ageing of PEF-treated meat for a few days prior to sous vide processing may improve tenderness; however, these gains in quality may be offset by a greater total water loss and an increase in lipid oxidation.
- Published
- 2019
23. The alternative approach of low temperature-long time cooking on bovine semitendinosus meat quality
- Author
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Ismail, Ishamri, Hwang, Young-Hwa, Bakhsh, Allah, and Joo, Seon-Tea
- Subjects
Chemistry ,Semitendinosus ,Sous vide ,0402 animal and dairy science ,Thermal effect ,food and beverages ,Hanwoo Beef ,04 agricultural and veterinary sciences ,040201 dairy & animal science ,Article ,Low Temperature-long Time ,Tenderness ,Collagen solubility ,Animal Products ,Sous Vide ,Shear Force ,medicine ,Animal Science and Zoology ,Food science ,medicine.symptom ,Semitendinosus muscle ,Protein solubility ,Water content ,Low temperature long time ,Food Science - Abstract
Objective This study aimed to elucidate whether innovative sous vide treatment has a significant influence on the beef semitendinosus muscle as compared to common sous vide treatment and traditional cooking. Methods The innovative sous vide treatments were cooked at 45°C and 65°C for 6 h (SV45–65), common sous vide treatment at 45°C and 65°C for 3 h (SV45 and SV65) and traditional cooking at 75°C for 30 min (CON75). Water loss and cooking loss, as well as the physical properties (color and shear force) and chemical properties (protein and collagen solubility) of the treated meat, were investigated. Results The results obtained indicated that the innovative sous vide with double thermal treatment (SV45–65) and cooked with air presence (CON75) resulted to lower a* and higher b* values, respectively. The water loss and cooking loss increased when temperature increased from 45°C to 65°C, and lower water loss was recorded in SV45 and CON75. These samples presented higher water content and revealed strong correlation to protein solubility. Warner-Bratzler shear force (SF) analysis showed the marked interaction between cooking temperature and time. Sample cooked at a high temperature (CON75) and a long period (SV45–65) showed a significantly lower value of SF than sample SV65 (p
- Published
- 2019
24. Effect of radiation processing on meat tenderisation.
- Author
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Kanatt, Sweetie R., Chawla, S.P., and Sharma, Arun
- Subjects
- *
IRRADIATED meat , *EFFECT of radiation on food , *SHEAR strength , *FOOD consumption , *RADIATION doses , *PROTEIN solubility - Abstract
The effect of radiation processing (0, 2.5, 5 and 10 kGy) on the tenderness of three types of popularly consumed meat in India namely chicken, lamb and buffalo was investigated. In irradiated meat samples dose dependant reduction in water holding capacity, cooking yield and shear force was observed. Reduction in shear force upon radiation processing was more pronounced in buffalo meat. Protein and collagen solubility as well as TCA soluble protein content increased on irradiation. Radiation processing of meat samples resulted in some change in colour of meat. Results suggested that irradiation leads to dose dependant tenderization of meat. Radiation processing of meat at a dose of 2.5 kGy improved its texture and had acceptable odour. [ABSTRACT FROM AUTHOR]
- Published
- 2015
- Full Text
- View/download PDF
25. Effect of ammonium hydroxide on textural and ultrastructural properties of spent hen meat.
- Author
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Kiran, M., Naveena, B. M., Sudhakar Reddy, K., Kondal Reddy, K., and Madhav Rao, T.
- Subjects
AMMONIUM hydroxide ,ULTRASTRUCTURE (Biology) ,MEAT texture ,HYDROGEN-ion concentration ,COLLAGEN ,PROTEIN solubility ,TRANSMISSION electron microscopy - Abstract
Beneficial effects of ammonium hydroxide was studied, to optimize the ammonium hydroxide concentration for effective tenderization of spent henmeat. Spent henmeat chunks were subjected to ammonium hydroxide treatment (AHT) at different concentrations (0%, 0.1%, 0.5% and 1.0% v/w) and evaluated for different quality parameters after 24 hours. The results indicated a significant increase in pH, water holding capacity, total and myofibrillar protein solubility, collagen solubility in 0.5% and 1.0% AHT samples relative to control with significant reduction in Warner-Bratzler shear force (WBSF) for all AHT meat chunks. The SDS-PAGE photographs also revealed a reduction in the band colour intensity in all AHT samples compared to control indicating breakdown of proteins. Transmission electron microscopy (TEM) also confirms the proteolysis and breakdown of muscle fibres in AHT samples. These results clearly suggest the tenderizing effects of ammonium hydroxide in spent hen meat. There was no significant improvement in tenderness at 1% level compared to 0.5% level, therefore ammonium hydroxide at 0.5% was suggested as the optimal for the spent hen chicken tenderization. [ABSTRACT FROM AUTHOR]
- Published
- 2014
26. The effect of extended post-mortem ageing on the Warner–Brazler shear force of longissimus thoracis from beef heifers from two sire breeds, slaughtered at 20 or 25 mo of age
- Author
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Brigitte Picard, Aidan P. Moloney, Lara Morán, Teagasc - The Agriculture and Food Development Authority (Teagasc), Unité Mixte de Recherche sur les Herbivores - UMR 1213 (UMRH), VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), University of the Basque Country/Euskal Herriko Unibertsitatea (UPV/EHU), and European CommissionFOOD-CT-2006-36241
- Subjects
breed ,animal diseases ,Longissimus Thoracis ,wet ageing ,Biology ,instrumental texture ,Collagen solubility ,0404 agricultural biotechnology ,Animal science ,medicine ,2. Zero hunger ,Ecology ,Sire ,0402 animal and dairy science ,food and beverages ,04 agricultural and veterinary sciences ,040401 food science ,040201 dairy & animal science ,Breed ,Tenderness ,Ageing ,Belgian Blue ,Animal Science and Zoology ,Intramuscular fat ,medicine.symptom ,Beef ,Agronomy and Crop Science ,[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition ,Food Science - Abstract
The effects on tenderness of extended ageing of longissimus thoracis (LT, striploin) muscle that differed in structure and composition were examined. Spring-born Angus × Holstein-Friesian heifers (n = 48) and Belgian Blue × Holstein-Friesian heifers (n = 48) were slaughtered, within sire breed, at 20 or 25 mo of age. Approximately 48 h post-mortem, LT steaks (2.5 cm) were removed, and either stored at −20°C for chemical analysis or vacuum-packed, stored at 2°C for 7, 14 or 28 d post-mortem and then at −20°C pending Warner–Bratzler shear force (WBSF) analysis. Muscle from Angus-sired heifers had higher (P < 0.001) intramuscular fat (IMF) concentration, lower (P < 0.001) proportion of type IIX muscle fibres and higher (P < 0.001) proportion of type IIA and type I muscle fibres compared to muscle from Belgian Blue-sired heifers. Collagen characteristics did not differ between sire breeds. Later slaughter increased (P < 0.001) IMF concentration and decreased (P < 0.001) total and insoluble concentrations and collagen solubility. There were no interactions between the main effects for WBSF and no difference between sire breeds. Later slaughter and increasing the duration of ageing decreased (P < 0.05) WBSF. Based on threshold WBSF values in the literature, all samples would be considered tender (
- Published
- 2020
27. Evaluating the effect of cooking temperature and time on collagen characteristics and the texture of hog maw
- Author
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Juan-Juan Wang, Chang-Yu Zhou, Chunbao Li, Chong Wang, Guanghong Zhou, Daming Ding, and Yan-Yan Zheng
- Subjects
Meat ,Chemistry ,Swine ,technology, industry, and agriculture ,Temperature ,food and beverages ,Pharmaceutical Science ,Immunofluorescence staining ,Collagen solubility ,Hardness ,Chewiness ,Texture profile analysis ,otorhinolaryngologic diseases ,Food science ,Texture (crystalline) ,Collagen ,Cooking ,Raw meat ,Water baths ,Type I collagen ,Food Science - Abstract
This study evaluated the texture of hog maw and the degradation of Types I and III collagen in the intramuscular connective tissue (IMCT) of hog maw at different cooking temperatures (75-95°C) and times (50-130 min). The cooking loss, shear force, collagen content, collagen solubility, and IMCT strength of hog maw cooked in water baths were measured. The instrumental texture profile analysis showed that the brittleness, springiness, chewiness and hardness of the cooked hog maw significantly increased with the increase of cooking temperature, while the hardness, springiness and chewiness increased first and then decreased with increasing cooking time. Cooking loss exhibited a 38% increase between the raw meat and meat cooked at 95°C. The collagen solubility significantly increased from 5.5 mg/g for raw meat to 8.6 mg/g for meat cooked at 95°C, accompanied by decreases in the shear force and IMCT strength associated with the increase in cooking temperature and time. These results show that the texture and collagen characteristics of hog maw are dramatically affected by the cooking temperature and time. Sodium dodecyl sulfate electrophoresis and immunofluorescence staining further showed that collagen degradation occurred after cooking, and the degradation of Type I collagen was higher than that of Type III collagen. These results indicated that the degradation of Type I collagen was mainly responsible for the sensory and textural improvements of the cooked hog maw.
- Published
- 2020
28. Review for 'Relevance of collagen solubility and gelatinolytic proteinase activity for texture softening in chilled grass carp ( Ctenopharyngodon idellus ) fillets'
- Author
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Yu Ermeng
- Subjects
Collagen solubility ,Ctenopharyngodon idellus ,biology ,Chemistry ,Proteinase activity ,Food science ,Texture (crystalline) ,biology.organism_classification ,Softening ,Grass carp - Published
- 2020
29. Review for 'Relevance of collagen solubility and gelatinolytic proteinase activity for texture softening in chilled grass carp ( Ctenopharyngodon idellus ) fillets'
- Author
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Bung-Orn Hemung
- Subjects
Collagen solubility ,Ctenopharyngodon idellus ,biology ,Chemistry ,Proteinase activity ,Food science ,Texture (crystalline) ,biology.organism_classification ,Softening ,Grass carp - Published
- 2020
30. Review for 'Relevance of collagen solubility and gelatinolytic proteinase activity for texture softening in chilled grass carp ( Ctenopharyngodon idellus ) fillets'
- Author
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B A. Shamasundar
- Subjects
Collagen solubility ,Ctenopharyngodon idellus ,biology ,Chemistry ,Proteinase activity ,Food science ,Texture (crystalline) ,biology.organism_classification ,Softening ,Grass carp - Published
- 2020
31. Review for 'Relevance of collagen solubility and gelatinolytic proteinase activity for texture softening in chilled grass carp ( Ctenopharyngodon idellus ) fillets'
- Author
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Wenzheng Shi
- Subjects
Collagen solubility ,biology ,Ctenopharyngodon idellus ,Chemistry ,Proteinase activity ,Texture (crystalline) ,Food science ,biology.organism_classification ,Softening ,Grass carp - Published
- 2020
32. Intramuscular collagen characteristics and expression of related genes in skeletal muscle of cull cows receiving a high-energy diet
- Author
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Pedro Veiga Rodrigues Paulino, Marcio de Souza Duarte, Nick V. L. Serão, Fabyano Fonseca e Silva, Marta M.S. Fontes, Lorena Silva Carneiro, Thaís C Costa, Mario Luiz Chizzotti, M. M. Lopes, and Ranyeri Souza
- Subjects
medicine.medical_specialty ,animal structures ,MMP2 ,animal diseases ,Longissimus Thoracis ,Gene Expression ,Protein-Lysine 6-Oxidase ,Collagen solubility ,0404 agricultural biotechnology ,Internal medicine ,medicine ,Animals ,RNA, Messenger ,Muscle, Skeletal ,Gene ,TIMP1 ,Chemistry ,0402 animal and dairy science ,food and beverages ,Skeletal muscle ,04 agricultural and veterinary sciences ,Metabolism ,040401 food science ,040201 dairy & animal science ,Animal Feed ,Diet ,Tenderness ,Red Meat ,medicine.anatomical_structure ,Endocrinology ,Solubility ,Cattle ,Female ,Collagen ,medicine.symptom ,Shear Strength ,Food Science - Abstract
We aimed to investigate differences in the synthesis and metabolism of intramuscular collagen in the Longissimus thoracis (LT) muscle between heifers and cull-cows fed high-energy diet. Ten cull-cows, (74.9 ± 3.2 months age, weighing 536 ± 14.55 kg) and ten heifers (18.4 ± 3.2 months age, weighting 310.5 ± 14.5 kg) were fed with high-energy diets for 150 days. The total collagen content did not differ between treatments. Greater collagen solubility was observed in heifers than cull-cows, although no differences in lysyl oxidase activity were observed between treatments. No differences were observed for mRNA expression of CO1A1, MMP2, MMP9 and TIMP2 between treatments. However, cull-cows presented greater mRNA expression of COL3A1, TIMP1 and TIMP3 than heifers. Our data give no indication that feeding a high-energy diet to cull-cows decreases the concentration of intramuscular collagen in the LT muscle or increases its solubility in respect to the collagen solubility in LT muscles from heifers on the same diet.
- Published
- 2020
33. Post-Harvest Strategies to Improve Tenderness of Underutilized Mature Beef: A Review.
- Author
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Tuell JR, Nondorf MJ, and Brad Kim YH
- Abstract
Beef muscles from mature cows and bulls, especially those originating from the extremities of the carcass, are considered as underutilized due to unsatisfactory palatability. However, beef from culled animals comprises a substantial proportion of the total slaughter in the US and globally. Modern consumers typically favor cuts suitable for fast, dry-heat cookery, thereby creating challenges for the industry to market inherently tough muscles. In general, cull cow beef would be categorized as having a lower extent of postmortem proteolysis compared to youthful carcasses, coupled with a high amount of background toughness. The extent of cross-linking and resulting insolubility of intramuscular connective tissues typically serves as the limiting factor for tenderness development of mature beef. Thus, numerous post-harvest strategies have been developed to improve the quality and palatability attributes, often aimed at overcoming deficiencies in tenderness through enhancing the degradation of myofibrillar and stromal proteins or physically disrupting the tissue structure. The aim of this review is to highlight existing and recent innovations in the field that have been demonstrated as effective to enhance the tenderness and palatability traits of mature beef during the chilling and postmortem aging processes, as well as the use of physical interventions and enhancement., Competing Interests: The authors declare no potential conflicts of interest., (© Korean Society for Food Science of Animal Resources.)
- Published
- 2022
- Full Text
- View/download PDF
34. Optimisation of Sous Vide Processing Parameters for Pulsed Electric Fields Treated Beef Briskets
- Author
-
Amali U. Alahakoon, Patrick Silcock, Indrawati Oey, and Phil Bremer
- Subjects
Materials science ,Scanning electron microscope ,Process Chemistry and Technology ,Sous vide ,Shear force ,04 agricultural and veterinary sciences ,040401 food science ,Industrial and Manufacturing Engineering ,Tenderness ,Meat tenderness ,Collagen solubility ,0404 agricultural biotechnology ,Electric field ,medicine ,Specific energy ,Food science ,medicine.symptom ,Safety, Risk, Reliability and Quality ,Food Science - Abstract
The goal of this research was to optimise sous vide processing parameters for beef briskets, previously treated with pulsed electric fields (PEF), to enhance meat tenderness while maintaining other quality attributes such as water holding capacity, colour, and collagen solubility. PEF-treated briskets (electric field strength 1.5 kV/cm; specific energy of 90–100 kJ/kg) were subjected to various sous vide temperature and time combinations for the process optimisation using response surface methodology. Sous vide temperature was found to significantly reduce the shear force of PEF-treated meat while time significantly reduced its hardness. In addition, beef briskets processed by PEF prior to sous vide processing showed less variation owing to a reduction in the effect of biological variation on the parameters tested. According to the response optimiser prediction, sous vide processing at 60 °C for 24 h resulted in optimal quality and tenderness. Scanning electron microscopy (SEM) revealed that PEF-treated meat showed evidence of pore formation in connective tissue and polarised-sensitive optical coherence topography (PS-OCT) revealed that the collagen matrix of PEF-treated meat had a reduced birefringence capacity compared to non-PEF-treated meat, which indicated a breakdown of the collagen.
- Published
- 2018
35. Palatability and Biochemical Factors of Beef from Mature Cattle Finished on a Concentrate Diet Prior to Harvest
- Author
-
Jerrad F. Legako, D.A. Gredell, J. Chance Brooks, Travis G. O’Quinn, and Markus F. Miller
- Subjects
010405 organic chemistry ,Marbled meat ,food and beverages ,lcsh:TX341-641 ,04 agricultural and veterinary sciences ,Beef cattle ,Biology ,040401 food science ,01 natural sciences ,0104 chemical sciences ,Cattle feeding ,Tenderness ,Collagen solubility ,0404 agricultural biotechnology ,Animal science ,medicine ,Palatability ,lcsh:Animal culture ,medicine.symptom ,Carcass composition ,lcsh:Nutrition. Foods and food supply ,Flavor ,lcsh:SF1-1100 - Abstract
The objective of this study was to investigate the influence of grain-finishing on mature beef palatability. Beef strip loins (n = 15 per treatment) from 2 marbling score groups [Slight (SL) and Traces/Practically Devoid (TR/PD)] and 3 carcass types [young fed (YF), mature fed (MF), and mature unfed (MU)] were collected. Young fed and MF cattle were grain-finished prior to harvest, whereas, beef from MU cattle were not identified as being grain-finished prior to harvest. Consumer and trained sensory panels evaluated steaks for palatability characteristics. Additionally, Warner-Bratzler shear force (WBSF), collagen solubility, sarcomere length, and volatile compounds were evaluated. Consumer ratings were not influenced (P > 0.05) by an interaction of main effects. Slight samples were greater (P < 0.05) than TR/PD samples for tenderness, juiciness, flavor, and overall like. Trained panelists rated SL samples more tender (P < 0.01) than TR/PD samples. Additionally, YF and MU steaks were the most and least tender (P < 0.01), respectively. No differences (P > 0.05) were observed among SL samples for beef flavor, beef flavor intensity, or off-flavor intensity due to carcass type. However, TR/PD-MF and MU steaks had more intense (P < 0.01) off-flavors. Steaks from YF and MF carcasses had lower (P < 0.01) WBSF values than steaks from MU carcasses. Percentage of heat soluble collagen was greatest (P < 0.01) in YF carcasses. Among SL treatments, sarcomere length was not affected (P > 0.05) by carcass type; however, MF and MU carcasses with TR/PD marbling scores had shorter (P < 0.05) sarcomeres than YF carcasses. Various volatile compounds were influenced (P < 0.05) by treatment and showed relationships with sensory ratings. Improvements in palatability were observed due to grain-finishing mature cattle, suggesting an adequate degree of marbling could offset negative palatability traits typically associated with beef from mature cattle.
- Published
- 2018
36. Effect of castration and carcass suspension method on the quality and fatty acid profile of beef from male dairy cattle
- Author
-
Joseph P. Kerry, Yingqun Nian, Sabine M. Harrison, and Paul Allen
- Subjects
chemistry.chemical_classification ,Nutrition and Dietetics ,animal diseases ,0402 animal and dairy science ,food and beverages ,Fatty acid ,04 agricultural and veterinary sciences ,040401 food science ,040201 dairy & animal science ,Tenderness ,chemistry.chemical_compound ,Collagen solubility ,0404 agricultural biotechnology ,Castration ,Animal science ,chemistry ,Ageing ,medicine ,Intramuscular fat ,medicine.symptom ,Agronomy and Crop Science ,Dairy cattle ,Food Science ,Biotechnology ,Polyunsaturated fatty acid - Abstract
The use of bulls rather than steers for beef production offers some considerable advantages; however, the eating quality of bull beef is an issue of marketing concern. This study assessed the physicochemical characteristics of young Holstein-Friesian (HF) bull and steer beef. Steer carcasses were suspended by the Achilles tendon (AS) and by pelvic suspension (PS).; Results: HF steer beef had higher redness, yellowness and chroma values, whereas bulls had higher ultimate pH and darker muscle. Warner-Bratzler shear force, cook loss at different ageing times, moisture, and insoluble and total collagen were higher for HF bull beef, whereas intramuscular fat, soluble collagen and collagen solubility were higher for steer beef. HF steer beef had a higher proportion of saturated fatty acids (SFA) and monounsaturated fatty acids (MUFA), whereas bull beef had higher proportions of polyunsaturated fatty acids (PUFA), PUFA/SFA and n-6/n-3 PUFA ratios. In comparison to AS, PS increased redness and chroma after 24 h blooming; PS improved tenderness up to 7 days of ageing and accelerated the ageing process.; Conclusion: For young dairy cattle, steer beef would likely have superior eating quality but a relatively less favourable nutritional fatty acid profile to bull beef. Suspension method affected the tenderness and colour intensity of dairy steer beef at different ageing times. © 2018 Society of Chemical Industry.; © 2018 Society of Chemical Industry.
- Published
- 2018
37. The effect of water vapor pressure on muscle collagen solubility and selected characteristics of the longissimus lumborum muscle in crossbred cattle
- Author
-
Alicja Dzido, Krzysztof Młynek, Ewa Salomończyk, and Beata Głowińska
- Subjects
Vapor pressure ,Chemistry ,Vapour pressure of water ,0402 animal and dairy science ,04 agricultural and veterinary sciences ,Anatomy ,Crossbred cattle ,040401 food science ,040201 dairy & animal science ,Tenderness ,Collagen solubility ,0404 agricultural biotechnology ,Animal science ,Correlation analysis ,medicine ,Statistical analysis ,medicine.symptom ,Longissimus Lumborum - Abstract
Most scientific studies are dedicated to the possibility of preparing beef for consumption under industrial conditions. Few publications are devoted to the issue of collagen thermohydrolysis in conditions available to the consumer. This study has analyzed the effect of small values of water vapor pressure on major culinary indices and chemical components of the longissimus lumborum muscle obtained from bulls with different growth rates. The experiment involved 48 animals. On the basis of the gain during the fattening time, the animals were divided into a low growth intensity group, with a daily body weight gain of ≤900 g, and a high growth intensity group with a daily gain of >900 g/day. A part of the samples of the longissimus lumborum muscle (control) was thermally treated in a water bath at 75°C. Another part was heat treated in a pressure-pot at 150°C, at a pressure of 0.1 MPa. The next part of samples was subjected to the same temperature, but the pressure was 0.2 MPa. The obtained results indicate that the values of the studied indices were largely affected by thermal processing parameters rather than the animals’ growth rate. The highest contents of total protein and water-soluble collagen were obtained in the case of a temperature of 150°C and the highest pressure (0.2 MPa). Water vapor with increased temperature and pressure also created favorable conditions for obtaining better meat tenderness and more favorable values of the water holding capacity. The latter characteristic appeared to be strongly connected with an increasing amount of water-soluble collagen, which was confirmed by relatively high values of the correlation coefficient between these characteristics. A strong positive correlation was also shown between thermal drip and the total collagen content in meat.
- Published
- 2018
38. Effect of age and cut on tenderness of South African beef
- Author
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Schönfeldt, H.C. and Strydom, P.E.
- Subjects
- *
SENSORY evaluation of beef , *AGE , *ANIMALS , *COLLAGEN , *CATTLE carcasses , *MEAT cuts , *DISCRIMINANT analysis - Abstract
Abstract: The tenderness characteristics of 15 primal cuts of beef of three different age groups were assessed, and the most reliable cut to predict carcass tenderness was determined. Fifteen wholesale cuts from each age group, representing the full variation in fatness, were aged, cooked and underwent sensory evaluation, shear force resistance and proximate analysis. Collagen content and solubility was determined. Percentage fat was used as a covariant during statistical analyses. Tenderness, residue and collagen solubility of all cuts decreased significantly with animal age. Collagen solubility was the largest discriminant between the three age groups, while animal age had no significant effect on collagen content. Tenderness of primal cuts from the same carcass varied considerably, with collagen content and shear force resistance as the largest discriminants between the cuts. Cuts most representative of total carcass tenderness were M. vastus lateralis, M. semimembranosus, M. gluteobiceps, M. semitendinosus and M. triceps brachii caput longum. [ABSTRACT FROM AUTHOR]
- Published
- 2011
- Full Text
- View/download PDF
39. Effect of sous vide cooking and ageing on tenderness and water-holding capacity of low-value beef muscles from young and older animals
- Author
-
Peter C. Thomson, Robyn D. Warner, Michael Friend, Michael Campbell, Minh Ha, David McGill, and Zahra Naqvi
- Subjects
Food Handling ,Sous vide ,Meat tenderness ,Collagen solubility ,0404 agricultural biotechnology ,Animal science ,otorhinolaryngologic diseases ,medicine ,Animals ,Water holding capacity ,Cooking ,Muscle, Skeletal ,M. semitendinosus ,Chemistry ,Age Factors ,technology, industry, and agriculture ,0402 animal and dairy science ,Water ,food and beverages ,04 agricultural and veterinary sciences ,040401 food science ,040201 dairy & animal science ,Tenderness ,Red Meat ,Ageing ,Red meat ,Cattle ,Collagen ,medicine.symptom ,Shear Strength ,Food Science - Abstract
This study investigated the effect of the age of the animal, sous vide cooking and ageing on tenderness and water-holding capacity of bovine biceps femoris (BF) and semitendinosus (ST). Samples of each muscle from young (
- Published
- 2021
40. Collagen solubility testing, a quality assurance step for reproducible electro-spun nano-fibre fabrication. A technical note.
- Author
-
Zeugolis, D. I., Li, B., Lareu, R. R., Chan, C. K., and Raghunath, M.
- Subjects
- *
COLLAGEN , *EXTRACELLULAR matrix proteins , *BIOPOLYMERS , *TISSUE engineering , *ELECTROPHORESIS - Abstract
Collagen is the main component of the extra-cellular matrix and has been utilised for numerous clinical applications in many forms and products. However, since collagen remains a natural animal-derived biopolymer, variation between batches should be addressed and minimised to ensure reproducibility of the fabrication process. Recently, electro-spinning of collagen has been introduced as a leading technique for the production of bio-mimetic nano-scale scaffolds for tissue-engineering applications. However, no protocols are available that would allow comparisons of the quality of different collagen raw materials prior to the electro-spinning process. In order to bridge this gap we assessed the solubility of various freeze-dried collagens in 0.5 M acetic acid and analysed the solved collagen by gel electrophoresis. We show that raw material of limited solubility in acetic acid will not render high quality electro-spun nano-fibres using hexafluoropropanol. In particular, insoluble collagen directly failed to produce nano-fibres, collagen of reduced solubility produced fused nano-fibres with limited inter-nano-fibre space, whilst purified type-I collagen of high solubility produced smooth, reproducible nano-fibres. Gel electrophoresis confirmed the amount of solubility, as well as qualitative differences in terms of collagen cross-links and collagen types. We recommend this simple and fast step to save costs and to enhance control over the electro-spinning process of collagen. Furthermore, we believe that the solubility test should be introduced prior to any collagenous matrix preparation in order to ensure reproducibility and accuracy. [ABSTRACT FROM AUTHOR]
- Published
- 2008
- Full Text
- View/download PDF
41. Thermal stability of connective tissue from porcine muscles
- Author
-
Voutila, L., Mullen, A.M., Ruusunen, M., Troy, D., and Puolanne, E.
- Subjects
- *
CONNECTIVE tissues , *MUSCULOSKELETAL system , *VIRUS diseases in swine , *SYNDROMES in animals - Abstract
Abstract: Connective tissue of three porcine muscles (M. infraspinatus, IS; M. longissimus dorsi, LD; M. semimembranosus, SM) from 27 animals [populations A (n =13, reared in Ireland) and B (n =14, reared in Finland)] was studied by measuring the collagen content, collagen solubility and thermal shrinkage temperature of the connective tissue. Colour and pH were also determined. Collagen solubility was highest in IS (p <0.05) and lowest in SM (p <0.05) although no difference between LD and SM was found in population B. The onset and peak temperatures of thermal shrinkage (T o and T p) were highest in IS (p <0.05). The lowest T o and T p were found in SM from population B whereas no differences were seen between LD and SM muscles in population A. It was concluded that the thermal stability of the connective tissue in the three porcine muscles differ. IS, as a dark muscle has high thermal shrinkage temperatures and high collagen solubilities in comparison to the lighter LD and SM muscles which have lower thermal shrinkage temperatures and collagen solubilities. Collagen contents were highest in IS and lowest in LD. [Copyright &y& Elsevier]
- Published
- 2007
- Full Text
- View/download PDF
42. Effect of cooking temperature and time on the physico-chemical, histological and sensory properties of female carabeef (buffalo) meat
- Author
-
Vasanthi, C., Venkataramanujam, V., and Dushyanthan, K.
- Subjects
- *
BUFFALO meat , *TEMPERATURE effect , *COOKING , *COLLAGEN - Abstract
Abstract: The effect of cooking temperature (80–100°C) and time (30–60min) on collagen solubility of Semimembranosus muscle in carabeef were investigated. The pH, cooking loss, shear force value, collagen content, collagen solubility, sensory evaluation and histological observations of water bath cooked and pressure cooked Semimembranosus meat samples were measured. Increase in pH, cooking loss, collagen solubility and tenderness scores with decrease in shear force value and collagen content was observed with increases in cooking temperature and time. However, no statistical difference was observed for shear force values, collagen solubility values and tenderness scores in pressure cooked meat and meat cooked in a water bath at 100°C for 45min, inferring that cooking of buffalo meat at 100°C for 45min improved collagen solubility and tenderness to the same extent as that due to pressure cooking. [Copyright &y& Elsevier]
- Published
- 2007
- Full Text
- View/download PDF
43. Assessment of physico-chemical traits related to eating quality of young dairy bull beef at different ageing times using Raman spectroscopy and chemometrics
- Author
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Yingqun Nian, Ming Zhao, Colm P. O'Donnell, Gerard Downey, Paul Allen, Joseph P. Kerry, and Teagasc Walsh Fellowship Programme
- Subjects
Male ,Food Handling ,Physico-chemical traits ,Analytical chemistry ,Eating quality ,Spectrum Analysis, Raman ,Post-mortem ageing ,Time ,Chemometrics ,Protein content ,symbols.namesake ,Collagen solubility ,0404 agricultural biotechnology ,Partial least squares regression ,Food Quality ,Animals ,Food science ,Least-Squares Analysis ,Chemistry ,Age Factors ,0402 animal and dairy science ,Discriminant Analysis ,04 agricultural and veterinary sciences ,040401 food science ,040201 dairy & animal science ,Red Meat ,Chemical quality ,Raman spectroscopy ,symbols ,Cattle ,Collagen ,Dietary Proteins ,Intramuscular fat ,Shear Strength ,Beef ,Dairy bull ,Food Science - Abstract
peer-reviewed Raman spectroscopy and chemometrics were investigated for the prediction of eating quality related physico-chemical traits of Holstein-Friesian bull beef. Raman spectra were collected on the 3rd, 7th and 14th days post-mortem. A frequency range of 1300–2800 cm− 1 was used for partial least squares (PLS) modelling. PLS regression (PLSR) models for the prediction of WBSF and cook loss achieved an R2CV of 0.75 with RMSECV of 6.82 N and an R2CV of 0.77 with RMSECV of 0.97%w/w respectively. For the prediction of intramuscular fat, moisture and crude protein content, R2CV values were 0.85, 0.91 and 0.70 with RMSECV of 0.52%w/w, 0.39%w/w and 0.38%w/w respectively. An R2CV of 0.79 was achieved for the prediction of both total collagen and hydroxyproline content, while for collagen solubility the R2CV was 0.88. All samples (100%) from 15- and 19-month old bulls were correctly classified using PLS discriminant analysis (PLS-DA), while 86.7% of samples from different muscles (longissimus thoracis, semitendinosus and gluteus medius) were correctly classified. In general, PLSR models using Raman spectra on the 3rd day post-mortem had better prediction performance than those on the 7th and 14th days. Raman spectroscopy and chemometrics have potential to assess several beef physical and chemical quality traits.
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- 2017
44. Biochemical and organoleptic characteristics of muscle from early and late maturing bulls in different production systems
- Author
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G.B. Mezgebo, Mark McGee, Brigitte Picard, R. I. Richardson, Edward G. O'Riordan, Frank J. Monahan, A.P. Moloney, School of Agriculture and Food Science, University College Dublin [Dublin] ( UCD ), Animal and Grassland Research and Innovation Centre, Irish Agriculture and Food Development Authority, Unité Mixte de Recherches sur les Herbivores ( UMR 1213 Herbivores ), VetAgro Sup ( VAS ) -AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Institut National de la Recherche Agronomique ( INRA ), School of Veterinary Science, Faculty of Health Science, University of Bristol, Teagasc Walsh Fellowship, University College Dublin [Dublin] (UCD), Unité Mixte de Recherches sur les Herbivores - UMR 1213 (UMRH), VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Institut National de la Recherche Agronomique (INRA), University of Bristol [Bristol], Unité Mixte de Recherche sur les Herbivores - UMR 1213 (UMRH), and VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Institut National de la Recherche Agronomique (INRA)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement
- Subjects
Male ,muscle ,[SDV]Life Sciences [q-bio] ,animal diseases ,Organoleptic ,sensory ,Collagen solubility ,chemistry.chemical_compound ,Isocitrate dehydrogenase activity ,Food science ,caractérisation biochimique ,2. Zero hunger ,Silage ,04 agricultural and veterinary sciences ,beef ,Isocitrate Dehydrogenase ,Breed ,Animal culture ,Tenderness ,régime alimentaire ,Adipose Tissue ,Taste ,taureau ,Intramuscular fat ,medicine.symptom ,qualité sensorielle ,Sensation ,Biology ,Poaceae ,SF1-1100 ,intramuscular fat ,Animal science ,Lactate dehydrogenase ,medicine ,Animals ,Muscle, Skeletal ,[ SDV ] Life Sciences [q-bio] ,L-Lactate Dehydrogenase ,Myosin Heavy Chains ,système de production ,0402 animal and dairy science ,040201 dairy & animal science ,graisse intramusculaire ,Diet ,Red Meat ,breed type ,Phosphofructokinases ,chemistry ,040103 agronomy & agriculture ,0401 agriculture, forestry, and fisheries ,Cattle ,Animal Science and Zoology ,diet - Abstract
In grass-based beef production systems (PS), early maturing (EM) breed types may be preferable to late maturing (LM) breed types in achieving adequate fat cover. Biochemical and organoleptic characteristics of muscle from suckler bulls were investigated in EM and LM (n = 28/breed) assigned to one of two PS (ad libitum concentrates and grass silage to slaughter (C) or ad libitum silage plus 2 kg concentrate daily during winter followed by 99 days at pasture and then an indoor finishing period on C (GSPC)) in a breed type × 2 PS factorial arrangement of treatments. Bulls were managed to have a common target carcass weight of 380 kg. Intramuscular fat (IMF) content was higher ( P
- Published
- 2017
45. Effects of pre-slaughter nutritional condition on intramuscular collagen solubility, pyridinoline cross-links and meat tenderness in aged goats.
- Author
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Shiba, Nobuya, Matsuzaki, Masatoshi, and Tsuneishi, Eisaku
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COLLAGEN , *GOAT meat , *GOATS , *ANIMAL nutrition , *BODY weight - Abstract
Effects of preslaughter nutritional condition on intramuscular collagen characteristics were studied, in order to clarify the potential of intensive feeding to aged animals in improving meat tenderness. Ten castrated male goats were assigned into one of two groups: one group was allowed ad libitum access to a concentrate diet (total digestible nutrients 70%, crude protein 15%) and Italian ryegrass hay (ADLIB-group), and the other group was fed a restricted amount of their diet (concentrate diet 0.5% of bodyweight/day; hay 1.5% of bodyweight/day) to maintain their bodyweight (MAIN-group). After 3 months of the experimental period, goats were slaughtered and meat samples were obtained immediately. Goats in ADLIB-group had lower total and insoluble collagen concentrations, higher fat concentrations and collagen solubility than those in MAIN-group, but soluble collagen concentrations of muscles were similar for both groups. Goats in ADLIB-group had lower pyridinoline concentrations than those in MAIN-group, in all muscles, but the differences of pyridinoline concentration between the groups were not statistically significant. Warner-Bratzler shear force values of Longissimus and Biceps femoris muscles were lower in ADLIB-group than in MAIN-group. The increase of meat tenderness by preslaughter intensive feeding seemed to be associated with the increase in intramuscular fat deposition and high collagen solubility, and pyridinoline cross-link appeared to be one of the factors related to collagen solubility. [ABSTRACT FROM AUTHOR]
- Published
- 2004
- Full Text
- View/download PDF
46. The influence of post-mortem ageing and roasting on the microstructure, texture and collagen solubility of bovine semitendinosus muscle
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Palka, Krystyna
- Subjects
- *
SCANNING electron microscopes , *MICROSTRUCTURE - Abstract
Bovine semitendinosus (ST) muscles aged for 5 and 12 days at 4 °C were roasted at 170 °C to internal temperatures of 50, 60, 70, 80 and 90 °C. Microstructural changes in meat were evaluated using a scanning electron microscope (SEM). Texture profile analysis (TPA) and measurements of the shear force values of samples were conducted using a texture analyser. The cooking losses and quantity of total and soluble collagen were also estimated. The structure of intramuscular connective tissue and myofibrillar structure of meat after 5 days of ageing was very regular. In 12-day-aged samples fibrous and myofibrillar structures were less distinct, damages of endomysium tubes appeared and fibres of perimysium were swelled. Ageing of ST muscle for 12 days caused a two-fold increase in the quantity of soluble collagen and a two-fold decrease in the value of TPA parameters—hardness and chewiness, as compared to 5-day-aged samples. The decrease in fibre diameter and sarcomere length during roasting started at 60 °C in 5-day-aged meat and at 50 °C in 12-day-aged samples. The shear force values measured after roasting were lower for 12-day-aged meat than for 5-day-aged samples. The quantity of soluble collagen in roasted meat increased at an internal temperature of 80 °C. At a higher temperature of meat this variable depended on the degree of meat ageing. The cooking losses during roasting of meat were about 3% lower for 12-day-aged than for 5-day-aged samples. In the examined range of internal temperature of meat the cooking losses and the sarcomere length were negatively correlated. [Copyright &y& Elsevier]
- Published
- 2003
- Full Text
- View/download PDF
47. Characterization of meat from three Indian native cattle breeds and cross-bred cows
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S. Prajwal, C. Sunanda, V. N. Vasudevan, P. Gunasekaran, T. Sathu, P. Poobal, A. Irshad, and Kuleswan Pame
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Meat tenderness ,Collagen solubility ,Animal science ,General Veterinary ,Score plot ,Fat content ,Principal component analysis ,food and beverages ,Animal Science and Zoology ,Biology ,Total variability - Abstract
The current study was undertaken to evaluate various quality attributes of meat from three Indian native cattle breeds and cross-bred cows using Principal Component Analysis. Three muscles each from eight Vechur, Kasargod Dwarf, Gir and cross-bred cows of 10 years of age were utilized and analyzed for 13 variables such as physico-chemical and compositional attributes. The coefficients of variation of each parameter were in the range from 1.04 to 42.54 per cent. PCA transformed the variables into five principal components (PC), which explained about 75 per cent of total variability. PC1 was comprised of Warner-Bratzler shear force, collagen content, collagen solubility and sarcomere length. PC2 was characterized by a*, b*, cooking loss and fat content. Loading plots of the first two PCs revealed high correlation for objective measures of meat tenderness. In score plot, meat samples from cross-breds and native cattle breeds were organized into two distinct groups.
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- 2019
48. Production factors affecting the contribution of collagen to beef toughness
- Author
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Heather L. Bruce and Bimol C. Roy
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0303 health sciences ,Growth promoting ,Pyridinoline ,0402 animal and dairy science ,food and beverages ,04 agricultural and veterinary sciences ,General Medicine ,Biology ,040201 dairy & animal science ,Breed ,Tenderness ,03 medical and health sciences ,Collagen solubility ,chemistry.chemical_compound ,chemistry ,Glycation ,Genetics ,medicine ,Animal Science and Zoology ,Food science ,Palatability ,medicine.symptom ,Meat science ,030304 developmental biology ,Food Science - Abstract
Intramuscular collagen may affect the value of meat by limiting its tenderness and cooking convenience. Production factors such as age of animal at slaughter, the use of steroids and beta-adrenergic agonists as growth promotants, and cattle breed may affect the contribution of collagen to beef quality. Recent research has indicated that concentrations of the mature collagen cross-link pyridinoline (PYR) are positively correlated with Warner-Bratzler shear force (WBSF) and animal age at slaughter, while contribution of the concentration of a second mature collagen cross-link Ehrlich's Chromogen (EC) to beef toughness declines with cattle age. Cattle breed influences total collagen content of muscle due to differing rates of maturation among breeds. Growth promoting technologies do not appear to affect collagen solubility, but do influence PYR and EC densities and concentrations in some beef muscles. Concentrations of PYR and EC do not account for all the variation in collagen heat solubility in beef muscles, nor do advanced glycation end products given the relative immaturity of cattle at slaughter. In light of this, other collagen cross-links such as heat-stable divalent cross-links may warrant reconsideration with regard to their contribution to cooked beef toughness.
- Published
- 2019
49. An analysis of the influence of various tenderising treatments on the tenderness of meat from Polish Holstein-Friesian bulls and the course of changes in collagen
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Beata Mikołajczak, Edward Pospiech, Magdalena Montowska, Anita Spychaj, B. Danyluk, B. Grześ, Ryszard Żywica, Ewa Iwańska, and Joanna K. Banach
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Male ,Food Handling ,animal diseases ,Longissimus Thoracis ,Collagen solubility ,0404 agricultural biotechnology ,medicine ,Animals ,Food science ,Muscle, Skeletal ,Type III collagen ,Chemistry ,0402 animal and dairy science ,Temperature ,food and beverages ,04 agricultural and veterinary sciences ,040401 food science ,040201 dairy & animal science ,Electric Stimulation ,Tenderness ,Red Meat ,Cattle ,Collagen ,medicine.symptom ,Shear Strength ,Type I collagen ,Food Science - Abstract
The aim of the study was to analyse the influence of tenderising treatments applied to the carcasses of Polish Holstein-Friesian (PHF) bulls of Black-and-White variety on the process of meat tenderisation and to assess the role of collagen in this process. The research was carried out on m. longissimus thoracis et lumborum. The carcasses were subjected to high-voltage electrical stimulation (ES), conditioning (CD), and both treatments together (ES + CD). The carcasses which were only refrigerated were the control group. The content of collagen in meat, its solubility, the share of the polypeptide subunits α1(I)CB7 and α1(I)CB8 of type I collagen and α1(III)CB5 of type III collagen were also analysed. ES with and without CD significantly accelerated the meat tenderisation and increased collagen solubility. CD always caused the degradation of type I collagen subunits, especially the α1(I)CB7 subunit. However, CD had significantly lesser influence on the rate of meat tenderisation than ES.
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- 2019
50. Biochemical and Utralmicroscopic Evaluation of Myofibril Proteins and Collagen during Ageing in Broiler Chicken PSE (Pale, Sof, Exudative) Meat
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Flávia Maria Beteto, Massami Shimokomaki, Elza Iouko Ida, Gleice Rocha dos Santos Almeida, Adriana Lourenço Soares, Denis Fabrício Marchi, and Francisco Javier Hernandez-Blazquez
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Proteases ,Multidisciplinary ,animal structures ,Chemistry ,lcsh:Biotechnology ,Broiler ,Myofibrillar Fragmentation Index ,food and beverages ,CARNES E DERIVADOS ,Tenderness ,Sarcomere ,Collagen solubility ,Collagen content ,Ageing ,lcsh:TP248.13-248.65 ,medicine ,Food science ,medicine.symptom ,Myofibril ,Cooking loss ,PSE meat - Abstract
The aim of this work was to study the myofibril proteins and collagen fraction changes in broiler chickens PSE (pale, soft, exudative) meat during ageing and their relationship to meat quality. The results presented an increase of myofibril proteins and collagen solubility promoted by the enhanced proteases activities during storage. Ultramicroscopically, the PSE meat samples revealed intracellularly a sarcomere super contraction and lacunas within the A and I bands while Z-lines appeared very dense and fragmented in comparison to normal samples. This observation was noticed already at 4h storage while extracellularly collagen fibrils decreased visually within the endomysium only after 24h of conditioning. These results influenced the quality as the PSE meat presented better functional properties at the first hours of conditioning before further proteins degradation by proteases. Thereafter, at the later ageing stage a further disintegration of the abnormal meat structure would affect the meat functional properties.
- Published
- 2019
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