23 results on '"Michael T. Morrissey"'
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2. CHARACTERIZATION OF PROTEINASE RECOVERED FROM PACIFIC WHITING SURIMI WASH WATER
- Author
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Haejung An, Michael T. Morrissey, Soottawat Benjakul, and Thomas A. Seymour
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Pharmacology ,chemistry.chemical_classification ,Chromatography ,biology ,Chemistry ,Biophysics ,Cell Biology ,biology.organism_classification ,Whiting ,Dithiothreitol ,Hydrolysis ,chemistry.chemical_compound ,Enzyme ,Casein ,Urea ,Specific activity ,Myofibril ,Food Science - Abstract
Pacific whiting surimi wash water (SWW) proteinase was recovered by ohmic heating, ultrafiltration, and freeze-drying. By these processes, 5.9-fold purification was achieved. The most efficient step was ohmic heating, which concentrated the proteinase by 4.8 fold. Specific activity of the recovered SWW proteinase on casein and Z-Phe-Arg-NMec was 28.2 and 0.17 U/mg protein, respectively. The SWW proteinase showed good hydrolytic activity towards casein, acid-denatured hemoglobin and myofibrils. Acidification increased specific activity on all substrates tested but reduced thermal stability. β-Mercaptoethanol, dithiothreitol and urea enhanced activity against Z-Phe-Arg-NMec. Proteinase activity on Z-Phe-Arg-NMec showed an optimum pH of 4.0. The recovered proteinase showed 18.5% residual activity after 7 week storage at 4C.
- Published
- 1998
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3. Protein Hydrolysates from Pacific Whiting Solid Wastes
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Soottawat Benjakul and Michael T. Morrissey
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Hydrolyzed protein ,Chromatography ,biology ,Tryptophan ,chemistry.chemical_element ,General Chemistry ,biology.organism_classification ,Whiting ,Nitrogen ,Hydrolysate ,Hydrolysis ,chemistry ,Protein hydrolysates ,General Agricultural and Biological Sciences ,Chemical composition - Abstract
Alcalase and Neutrase showed optimum activity against Pacific whiting solid wastes (PWSW) at pH 9.5, 60 °C and pH 7.0, 55 °C, respectively. Alcalase had a higher proteolytic activity than Neutrase. Enzyme concentration, reaction time, and waste/buffer ratio significantly affected the hydrolysis and nitrogen recovery (NR) (p < 0.05). Optimum conditions for PWSW hydrolysis were 20 AU Alcalase/kg, 1 h reaction time, waste/buffer ratio of 1:1 (w/v). Correlation between the degree of hydrolysis (DH) and NR (R2 = 0.970−0.978) was high. Freeze-dried hydrolysate was brownish yellow in color (L* = 54.59, a* = 6.70, b* = 27.89) and contained 2.77% moisture, 79.97% protein, 13.44% ash, and 3.83% lipid. Amino acid composition of freeze-dried hydrolysate was similar to that of PWSW and Pacific whiting muscle but tryptophan was reduced to 21.50% and 14.74%, respectively. Keywords: Waste; Pacific whiting; hydrolysate; Alcalase; Neutrase
- Published
- 1997
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4. Surimi Gel Enhancement by Bovine Plasma Proteins
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Margo Y. Peters, Thomas A. Seymour, Haejung An, and Michael T. Morrissey
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chemistry.chemical_classification ,Chromatography ,biology ,medicine.diagnostic_test ,Chemistry ,Tissue transglutaminase ,viruses ,animal diseases ,Proteolysis ,Serum albumin ,General Chemistry ,biology.organism_classification ,Fibrinogen ,Whiting ,Blood proteins ,Enzyme ,Biochemistry ,medicine ,biology.protein ,Bovine serum albumin ,General Agricultural and Biological Sciences ,medicine.drug - Abstract
Gel strength enhancement of Pacific whiting surimi was studied by using an α2-macroglobulin (α2-M)-enriched plasma fraction (FIV-1) and a transglutaminase (TG)-enriched plasma fraction (FI-S). Fluorescent amine-incorporating activity was detected in FIV-1, FI-S, and bovine plasma protein (BPP), indicating potential protein cross-linking activity by α2-M and TG. Inhibition of autolytic activity was observed with FIV-1 and BPP. FIV-1 in combination with bovine serum albumin, fibrinogen, or FI-S enhanced gelation more than FIV-1 alone. These results indicate various components in BPP function both to enhance gelation of Pacific whiting surimi and to inhibit proteolysis. Keywords: Plasma protein; transglutaminase; α2-macroglobulin; surimi; gelation
- Published
- 1997
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5. Physicochemical Changes in Pacific Whiting Muscle Proteins during Iced Storage
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Haejung An, Michael T. Morrissey, Thomas A. Seymour, and Soottawat Benjakul
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Autolysis (biology) ,biology ,medicine.diagnostic_test ,Chemistry ,Myosin ATPase ,Proteolysis ,ATPase ,Fish fillet ,biology.organism_classification ,Whiting ,Biochemistry ,Myosin ,medicine ,biology.protein ,Food science ,Actin ,Food Science - Abstract
No changes in actomyosin Ca 2+ -, Mg 2+ -, or Mg 2+ -Ca 2+ -ATPase activities were observed during iced storage of Pacific whiting fillets, but Mg 2+ -EGTA-ATPase increased with a loss of Ca 2+ -sensitivity. Surface hydrophobicity of actomyosin increased substantially within 2 days, but not total sulfhydryl (SH) content. During longer storage, the SH content decreased gradually, but surface hydrophobicity remained constant. Autolytic degradation products increased in fish muscle with storage time. Myosin heavy chain (MHC) was degraded by 45% within 8 days, but no noticeable difference was observed in actin. Results indicated that autolysis may be the main cause of physicochemical changes in Pacific whiting muscle proteins during iced storage.
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- 1997
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6. RECOVERY OF PROTEINASE FROM PACIFIC WHITING SURIMI WASH WATER
- Author
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Soottawat Benjakul, Haejung An, Thomas A. Seymour, and Michael T. Morrissey
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Pharmacology ,Chromatography ,biology ,Chemistry ,Biophysics ,Ultrafiltration ,Cell Biology ,biology.organism_classification ,Whiting ,Cathepsin L ,Freeze-drying ,Wash water ,Wastewater ,Cathepsin B activity ,biology.protein ,Specific activity ,Food Science - Abstract
A proteinase from Pacific whiting surimi wash water (SWW) was recovered by ohmic heating, ultrafiltration and freeze drying with overall yield of 0.83 g protein/L SWW and 78% recovery of activity. Ohmic heating conditions were optimized for the maximum recovery of the enzyme. Different applied voltages (50, 70, 90 V) showed no differences in efficiency for removing protein and retaining cathepsin L activity. Cathepsin L activity reached its maximum after ohmic heating to 55C whereas cathepsin B activity decreased constantly with increased temperature. A constant reduction in protein content was observed with the increase in temperatures from 45C to 60C and holding time up to 5 min. The highest retention of both total and specific activity of cathepsin L was obtained with the treatment at 55C for 3 min. Under these conditioner, 193% activity was recovered from SWW although a large amount of the activity was lost by the subsequent steps of ultrafiltration and freeze drying.
- Published
- 1997
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7. Proteinase in Pacific Whiting Surimi Wash Water: Identification and Characterization
- Author
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Thomas A. Seymour, Michael T. Morrissey, Haejung An, and Soottawat Benjakul
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Cathepsin ,chemistry.chemical_classification ,Gel electrophoresis ,Chromatography ,biology ,Molecular mass ,Chemistry ,Size-exclusion chromatography ,biology.organism_classification ,Whiting ,Cathepsin B ,Cathepsin L ,Enzyme ,biology.protein ,Food Science - Abstract
A proteinase in Pacific whiting surimi wash water (SWW) was characterized to be cathepsin L based on molecular mass (M r ), substrate specificity, and SDS-substrate gel electrophoresis. The proteinase was highly active on Z-Phe-Arg-NMec, and the native M r was 27,400 based on size exclusion (SEC)-HPLC. Acidification of the SEC-HPLC fractions showed a two-fold increase in activity on Z-Phe-Arg-NMec. SWW proteolytic activity was found at M r 54,200 on SDS-substrate gel. However, acidification shifted the activity zone to M r 39,500 corresponding to cathepsin L. No evidence of activity by calpain or cathepsin B or H was found in Pacific whiting SWW.
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- 1996
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8. Linear Regression, Neural Network and Induction Analysis to Determine Harvesting and Processing Effects on Surimi Quality
- Author
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Gilbert Sylvia, G. Peters, John Bolte, and Michael T. Morrissey
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Artificial neural network ,biology ,media_common.quotation_subject ,biology.organism_classification ,Whiting ,Warehouse ,Nonlinear system ,Linear regression ,Statistics ,%22">Fish ,Quality (business) ,Water content ,Food Science ,media_common ,Mathematics - Abstract
Harvesting and processing input combinations and product quality attributes for the Pacific whiting surimi industry were collected and analyzed. Multiple linear regression, neural networks, and M5-induction were used to determine significant variables in the industry. Significant factors included variables intrinsic to the fish (moisture content, salinity, pH, length, weight) and processing variables (processing time, storage temperature, harvest date, wash time, wash ratios). Most variables were highly interactive and nonlinear. Information derived from these models have implications for production and management decisions.
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- 1996
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9. Proteolytic Activity in Pacific Whiting and Effects of Surimi Processing
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Michael T. Morrissey, Polla S. Hartley, and Haejung An
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Pathology ,medicine.medical_specialty ,Protease ,biology ,medicine.medical_treatment ,Flesh ,Zoology ,Aquatic Science ,biology.organism_classification ,Whiting ,digestive system diseases ,Rockfish ,medicine ,Food Science - Abstract
Pacific whiting showed high levels of proteolytic activity compared with other species, i.e., rockfish and squawfish. A wide variation of activity was found in individual whiting. The level of protease activity was highly correlated with the number of white pseudocysts in the muscle. Although correlation of proteolytic activity with black pseudocysts was low, higher activity was observed in tissue infected with black pseudocysts when compared to tissue without black pseudocysts. The protease activity of intact flesh was decreased by 83% during surimi processing.
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- 1996
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10. Whey Protein Concentrate as a Proteinase Inhibitor in Pacific Whiting Surimi
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Vasana C. Weerasinghe, Haejung An, Michael T. Morrissey, and Yun-Chin Chung
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Whey protein ,Chromatography ,biology ,Proteinase inhibitor ,Chemistry ,biology.organism_classification ,Trypsin ,Whiting ,Papain ,chemistry.chemical_compound ,medicine ,Proteinase activity ,Food science ,Food Science ,medicine.drug - Abstract
The most effective inhibition of autolytic proteinase activity was found at 3% whey protein concentrate (WPC) with residual proteinase activity at 14.2%. WPC reduced papain and trypsin activities linearly with lowest residual activities of 8.7% and 41.4%, respectively. An unidentified high-molecular-weight protein was inhibitory for papain and trypsin with no inhibitory components detected at the region
- Published
- 1996
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11. Activity Staining of Pacific Whiting (Merluccius products) Protease
- Author
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Xianbin Fan, Michael T. Morrissey, Haejung An, and Polla S. Hartley
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Gel electrophoresis ,Protease ,biology ,medicine.medical_treatment ,Proteolytic enzymes ,biology.organism_classification ,Whiting ,Merluccius ,Staining ,Cathepsin L ,Arrowtooth flounder ,Biochemistry ,medicine ,biology.protein ,Food Science - Abstract
An activity staining method using SDS-substrate gel was used to determine Pacific whiting proteolytic activity. The most active protease band was resolved at an apparent M, of 39,500 corresponding to the activity of cathepsin L. The activity was more pronounced for ocean-caught Pacific whiting than Puget Sound Pacific whiting or ocean-caught arrowtooth flounder. Gel electrophoresis activity staining of proteolytic enzymes in Pacific whiting was not as sensitive as the TCA-azocasein assay but provided information on the molecular properties of the enzyme and a semi-quantitative estimation of activity.
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- 1995
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12. Effects of Varying Sucrose Concentrations in Pacific Whiting(Merluccius productus)Stabilized Mince Used for Surimi Production
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Edward Kolbe, Michael T. Morrissey, Ricardo Simpson, Tyre C. Lanier, and Grant A. MacDonald
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Sucrose ,biology ,Cryoprotectant ,business.industry ,Food technology ,Aquatic Science ,biology.organism_classification ,Whiting ,Merluccius ,chemistry.chemical_compound ,chemistry ,Frozen storage ,Food science ,business ,Food Science - Abstract
Stabilized mince (SM) was made from fresh Pacific whiting mixed with varying levels of sucrose (6 to 12% w/w) including 0.2% w/w polyphosphates. SM samples were maintained in frozen storage and used at different time intervals for surimi production. Comparisons with control surimi made from fresh mince showed that acceptable surimi can be produced from SM stored at -20°C with cryoprotectant levels at 6% w/w sucrose and 0.2% w/w polyphosphates. There was a slight decrease in whiteness in surimi made from the SM samples when compared to the control. Surimi yields from SM were comparable to yields of surimi made from fresh mince.
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- 1995
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13. Isolation and activation of cathepsin L-inhibitor complex from Pacific whiting (Merluccius productus)
- Author
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Michael T. Morrissey, Haejung An, Margo Y. Peters, and Thomas A. Seymour
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chemistry.chemical_classification ,Chromatography ,biology ,Inhibitor complex ,Chemistry ,Cysteine Endopeptidases ,General Chemistry ,biology.organism_classification ,Ph stability ,Whiting ,Merluccius ,Cathepsin L ,Enzyme ,Biochemistry ,Enzyme inhibitor ,biology.protein ,General Agricultural and Biological Sciences - Abstract
Cathepsin L from Pacific whiting was separated into two activity peaks (P-I and P-II) on butyl-Sepharose. Acidification of the fractions at pH 3.3 resulted in an 11-fold increase in activity of P-I and a slight decrease in P-II on Z-Phe-Arg-NMec, suggesting that P-I is complex-formed with an inhibitor while P-II is the free enzyme. Analysis of further purified DEAE P-I fractions showed that only 55% of the activity was titrated by E-64 while low-pH-treated fractions were completely titrated. The DEAE P-I fractions showed highest pH stability at pH 4, while acidified DEAE P-I fractions showed the highest stability at pH 7.0
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- 1995
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14. Ohmic Heating Maximizes Gel Functionality of Pacific Whiting Surimi
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Jae W. Park, Michael T. Morrissey, Y. Abu Dagga, Jirawat Yongsawatdigul, and Edward Kolbe
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Crystallography ,Chemical engineering ,Moisture ,biology ,Chemistry ,Shear stress ,Degradation (geology) ,Network structure ,Joule heating ,biology.organism_classification ,Whiting ,Food Science - Abstract
Surimi without enzyme inhibitors containing 78% moisture and 2% NaCl was heated conventionally and ohmically to 90 o C after holding at 55 o C for 0, 1, 3 and 5 min. Gels heated slowly in a water bath exhibited poor gel quality, while the ohmically heated gels without holding at 55 o C showed more than a twofold increase in shear stress and shear strain over conventionally heated gels. Degradation of myosin and actin was minimized by ohmic heating, resulting in a continuous network structure. Ohmic heating with a rapid heating rate was an effective method for maximizing gel functionality of Pacific whiting surimi without enzyme inhibitors
- Published
- 1995
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15. Purification and characterization of Pacific whiting proteases
- Author
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Thomas A. Seymour, Haejung An, Margo Y. Peters, and Michael T. Morrissey
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Cathepsin ,chemistry.chemical_classification ,Proteases ,Protease ,Chromatography ,biology ,medicine.diagnostic_test ,medicine.medical_treatment ,Proteolysis ,General Chemistry ,biology.organism_classification ,Whiting ,Isoelectric point ,Enzyme ,Biochemistry ,chemistry ,Casein ,medicine ,General Agricultural and Biological Sciences - Abstract
Two forms (P-I and P-II) of a protease were purified to 560- and 21.5-fold from the sarcoplasmic fluid of Pacific whiting (Merluccius productus). The enzymes were assayed by hydrolysis of azocasein at 55 degrees C and pH 5.5. Both forms were composed of a single polypeptide of Mr 28 800; however, P-I also contained two low Mr components which were removed by low pH treatment prior to size exclusion chromatography. P-I and P-II showed pH optima at 5.5 and 6.0 and temperature optima of 55 and 60 degrees C, respectively. The enzymes had an identical isoelectric point of 4.91 with a minor band at 4.94. The proteases had high activity toward Z-Phe-Arg-NMec and casein. The activity of both forms was inhibited by all sulfhydryl reagents tested as well as the cathepsin L-specific inhibitor Z-Phe-Phe CHN2 and activated by reducing agents, suggesting the enzymes are forms of cathepsin L.
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- 1994
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16. Cathepsin Degradation of Pacific Whiting Surimi Proteins
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Michael T. Morrissey, Vasana C. Weerasinghe, Thomas A. Seymour, and Haejung An
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Cathepsin ,Protease ,biology ,Chemistry ,medicine.medical_treatment ,macromolecular substances ,Protein degradation ,biology.organism_classification ,Whiting ,Cathepsin B ,Cathepsin L ,Biochemistry ,Myosin ,medicine ,biology.protein ,Myofibril ,Food Science - Abstract
Cathepsin B was the most active cysteine protease in Pacific whiting fish fillets; cathepsin L was predominant in surimi. Cathepsin L showed highest activity at 55°C in both fish fillets and surimi, indicating its function in myosin degradation during conventional heating of fillets and surimi, gels. Washing during surimi processing removed cathepsin B and H but not cathepsin L. Myosin heavy chain was the primary substrate during autolysis of surimi paste and actin and myosin light chain showed limited hydrolysis during 2 hr incubation. Purified Pacific whiting cathepsin L hydrolyzed myofibrils, myosin and native and heat-denatured collagen. The degradation pattern of myofibrils by the protease was the same as the autolytic pattern of surimi.
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- 1994
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17. Effects of pH and NaCl on Gel Strength of Pacific Whiting Surimi
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Lewis Richardson, Yun Chin Chung, and Michael T. Morrissey
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Chromatography ,biology ,Chemistry ,Increased ph ,Aquatic Science ,biology.organism_classification ,Whiting ,Merluccius ,Gel strength ,Low salt ,Ph range ,Shear stress ,Water holding capacity ,Food Science - Abstract
The effects of varying concentrations of salt and pH on the gel strength of Pacific whiting (Merluccius productus) surimi were investigated. Surimi gels were made with and without the protease inhibitor beef plasma protein (BPP). Gel strength was measured by torsion and reported as shear stress and shear strain. In general, surimi gels increased in gel strength with increased pH. Stress increased to a greater degree than strain about pH 7. Water holding capacity values increased up to pH7 and than leveled off. Surimi gels made with low salt (0.9%) or not salt had greater stress values that the higher salt surimi gels in the alkaline pH range. The results demonstrated that the effects of salt and pH are interactive on gels strength for Pacific whiting surimi
- Published
- 1994
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18. Comparison of Physical, Thermal and Chemical Methods to Measure Protein Denaturation in Frozen Pacific Whiting (Merluccius productus)
- Author
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Michael T. Morrissey, Grant A. MacDonald, D.Q. Wang, Edward Kolbe, and Cheng-Kuang Hsu
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biology ,Chemistry ,Enthalpy ,Analytical chemistry ,Aquatic Science ,biology.organism_classification ,Whiting ,Merluccius ,Crystallography ,Differential scanning calorimetry ,Myosin ,Congelation ,Shear stress ,Denaturation (biochemistry) ,Food Science - Abstract
The potential of using the torsion test and differential scanning calorimetry (DSC) to determine the effect of frozen storage on protein denaturation in fish fillets was investigated. Pacific whiting fillets were stored for 12 weeks at three temperature conditions: -20¦C, -8¦C, and at a level varying between 0 and -8¦C. Salt soluble protein (SSP) extractability and Ca++-ATPase activity were used to evaluate the torsion test and DSC. The shear strain value of the torsion test provided a good correlation with SSP extractability, Ca++-ATPase activity, and myosin transition enthalpy as measured by DSC. Therefore, shear strain can be considered as a useful tool for the determination of protein denaturation in Pacific whiting during periods of frozen storage. Because Ca++-ATPase activity, shear stress and shear strain, and myosin transition enthalpy all decreased within one week, protein deterioration in frozen Pacific whiting appears to be rapid at the temperatures tested.
- Published
- 1993
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19. Protease Inhibitor Effects on Torsion Measurements and Autolysis of Pacific Whiting Surimi
- Author
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Haejung An, Michael T. Morrissey, J.W. Wu, and D. Lin
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Gel electrophoresis ,Autolysis (biology) ,Chromatography ,Protease ,medicine.diagnostic_test ,biology ,Chemistry ,Proteolysis ,medicine.medical_treatment ,biology.organism_classification ,Whiting ,Blood proteins ,Merluccius ,medicine ,Food Science ,Egg white - Abstract
Beef plasma protein (BPP), egg white and potato extract were tested for their ability to inhibit proteolysis in fish mince and surimi made from Pacific whiting (Merluccius productus). Strong inhibition resulted from all three compounds in fish mince when measured by autolysis. However, when tested in surimi significant differences occurred among the compounds. BPP showed strongest inhibition of proteolytic effect followed by egg white and potato extract when measured by autolysis, gel electrophoresis and torsion. BPP was an effective inhibitor in surimi at a concentration as low as 1%.
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- 1993
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20. Effect of High Hydrostatic Pressure on Pacific Whiting Surimi
- Author
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Yildiz Karaibrahimoglu, Jovi Sandhu, and Michael T. Morrissey
- Subjects
Protease ,Chromatography ,Gel strength ,biology ,Chemistry ,medicine.medical_treatment ,Hydrostatic pressure ,medicine ,biology.organism_classification ,Whiting ,Holding time ,Processing methods - Abstract
The effects of high hydrostatic pressure (HHP) on gel strength, microbial numbers, proteolytic activity, color and pH of Pacific whiting surimi gels were investigated. Strong gels without the use of protease inhibitors were formed with HHP treatments from 1–4 kBars. Gel strength was not affected by holding time. Total plate counts showed that destruction of vegetative cells was accomplished with 4 kBar. Proteolytic activity was diminished but not eliminated with pressure treatments. The color of the surimi gels treated were translucent while the heat-treated gels were opaque. The pH was increased slightly with HHP treatment. HHP was an effective processing method for making high quality surimi gels from Pacific whiting.
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- 1998
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21. Determination of quality parameters for Pacific whiting (M. productus)
- Author
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Gregory J. Peters, Michael T. Morrissey, and Gilbert Sylvia
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biology ,Natural resource economics ,business.industry ,media_common.quotation_subject ,Consumer demand ,Distribution (economics) ,biology.organism_classification ,Whiting ,Quality (business) ,Groundfish ,Annual variation ,Business ,Product (category theory) ,Quality characteristics ,media_common - Abstract
Controlling groundfish product quality is one of the foremost problems facing the seafood industry and an issue related to numerous biological, technical and institutional factors. For example, groundfish seafood products are processed from over a hundred species with widely varying quality characteristics. Most groundfish are wild and their product characteristics cannot be as easily controlled or standardized as products processed from cultured organisms. Groundfish may also be captured far from processing and distribution centres, making it difficult to preserve product qualities. There is often large annual variation in supplies, which makes it risky and unprofitable to invest in the capital equipment necessary to improve and control product quality. Finally, this variation in product quality within species, across species, and across groundfish industries makes it extremely difficult to develop and distribute products that have the necessary characteristics to consistently satisfy consumer demand and improve market opportunities.
- Published
- 1995
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22. Frozen Stabilized Mince as a Source of Pacific Whiting Surimi
- Author
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Tyre C. Lanier, G. A. MacDonald, Edward Kolbe, R. Simpson, and Michael T. Morrissey
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biology ,Cryoprotectant ,Chemistry ,Pilot scale ,%22">Fish ,Food science ,West coast ,Control sample ,biology.organism_classification ,Whiting - Abstract
Pacific whiting is available off the U.S. West Coast for about six months each year. A plan to extend the period of shore-based surimi production from whiting was investigated. Headed/gutted fish, and mince stabilized with cryoprotectants, were frozen, stored for up to six months, then processed into surimi. Measurements of texture and color were compared with those for a surimi control sample. Frozen mince stabilized with 6% sucrose and stored at -20 ° C resulted in production of good quality surimi. Pilot scale yield and freezing rate studies indicated the potential feasibility of commercial-scale production.
- Published
- 1994
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23. Protein Denaturation of Frozen Pacific Whiting (Merluccius productus) Fillets
- Author
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Y.C. Chung, Michael T. Morrissey, Edward Kolbe, and Cheng-Kuang Hsu
- Subjects
Torsion test ,Chromatography ,biology ,Chemistry ,Congelation ,%22">Fish ,Fish fillet ,Denaturation (biochemistry) ,Food science ,biology.organism_classification ,Whiting ,Food Science ,Merluccius - Abstract
Protein denaturation in Pacific whiting fillets stored at −8, −20, −34, and −50°C was investigated over a 10-mo period by several methods, including salt-soluble protein extractability, Ca++-ATPase activity, and the torsion test. Changes in quality of fillets stored at −8°C were significantly greater than those stored at lower temperatures. Fillets stored at −34 and −50°C showed no significant advantage over those stored at −20°C as measured by salt-soluble protein extractability and Ca++-ATPase activity. However, fillets stored at the lower temperatures had slightly higher torsion shear strain.
- Published
- 1993
- Full Text
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