7 results on '"Pectinidae chemistry"'
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2. Novel microbial fermentation for the preparation of iron-chelating scallop skirts peptides-its profile, identification, and possible binding mode.
- Author
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Yan X, Yue Y, Guo B, Zhang S, Ji C, Chen Y, Dai Y, Dong L, Zhu B, and Lin X
- Subjects
- Animals, Iron chemistry, Iron metabolism, Fermentation, Pectinidae chemistry, Pectinidae metabolism, Pectinidae microbiology, Peptides chemistry, Peptides metabolism, Iron Chelating Agents chemistry, Iron Chelating Agents metabolism, Bacillus metabolism, Bacillus chemistry
- Abstract
Iron chelating peptides have been widely utilized as iron supplements due to their excellent absorption capacity, However, the high cost and cumbersome manufacturing process of these peptides significantly limit their industrial application. In this study, fermentation was used for the first time to prepare iron chelating peptides. Bacillus altitudinis 3*1-3 was selected as the most suitable strain from 50 strains. The hydrolysates of fermented scallop skirts showed excellent iron-chelating capacity (9.39 mg/g). Aspartic acid, glutamic acid, and histidine are crucial for the binding of peptides to ferrous ions. The heptapeptide (FEDPEFE) forms six binding bonds with ferrous irons. Compared with ferrous sulfate, peptide-ferrous chelate showed more stability in salt solution and simulated gastrointestinal juice (p < 0.05). Furthermore, the fermentation method could save >50% of the cost compared with the enzymatic method. The results can provide a theoretical basis for the preparation of ferrous-chelated peptides using the fermentation method., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)
- Published
- 2024
- Full Text
- View/download PDF
3. Integrated ultra-high pressure and salt addition to improve the in vitro digestibility of myofibrillar proteins from scallop mantle (Patinopecten yessoensis).
- Author
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Liu X, Tian G, Zhao J, Zhang Q, Huai X, Sun J, and Sang Y
- Subjects
- Animals, Humans, Proteins chemistry, Sodium Chloride, Dietary, Sodium Chloride metabolism, Pectinidae chemistry
- Abstract
Myofibrillar protein (MP) is susceptible to the effect of ionic strength and ultra-high pressure (UHP) treatment, respectively. However, the impact of UHP combined with ionic strength on the structure and in vitro digestibility of MP from scallop mantle (Patinopecten yessoensis) is not yet clear. Therefore, it is particularly important to analyze the structural properties and enhance the in vitro digestibility of MP by NaCl and UHP treatment. The findings demonstrated that as ionic strength increased, the α-helix and β-sheet gradually transformed into β-turn and random coil. The decrease of endogenous fluorescence intensity indicated the formation of a more stable tertiary structure. Additionally, the exposure of internal sulfhydryl groups increased the amount of total sulfhydryl content, and reactive sulfhydryl groups gradually transformed into disulfide bonds. Moreover, it reduces aggregation through increased solubility, decreased turbidity, particle sizes, and a relatively dense and uniform microstructure. When MP from the scallop mantle was treated with 0.5 mol/L ionic strength and 200 MPa UHP treatment, it had the highest solubility (90.75 ± 0.13%) and the lowest turbidity (0.41 ± 0.03). The scallop mantle MP with NaCl of 0.3 mol/L and UHP treatment had optimal in vitro digestibility (95.14 ± 2.01%). The findings may offer a fresh perspectives for developing functional foods for patients with dyspepsia and a theoretical foundation for the comprehensive utilization of scallop mantle by-products with low concentrations of NaCl., Competing Interests: Declaration of competing interest We declare that we do not have any commercial or associative interest that represents a conflict of interest in connection with the work submitted., (Copyright © 2024 Elsevier Ltd. All rights reserved.)
- Published
- 2024
- Full Text
- View/download PDF
4. Gelatin/dextran active films incorporated with cinnamaldehyde and α-tocopherol for scallop (Patinopecten yessoensis) adductor muscle preservation.
- Author
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Fan F, Yue C, Zhai Z, Liao H, Lian X, and Xie H
- Subjects
- Animals, Antioxidants pharmacology, Permeability, Shellfish analysis, Hydrophobic and Hydrophilic Interactions, Gelatin chemistry, Pectinidae chemistry, Acrolein analogs & derivatives, Acrolein pharmacology, Acrolein chemistry, Dextrans chemistry, Dextrans pharmacology, alpha-Tocopherol pharmacology, alpha-Tocopherol chemistry, Food Preservation methods, Food Packaging methods
- Abstract
Scallops are rich in eicosapentaenoic acid (EPA) and docosahexaenoic acid but perishable due to their microbial growth and lipid oxidation. In this study, gelatin/dextran films containing cinnamaldehyde and α-tocopherol (0% + 0%, 0.3% + 0.3%, 0.6% + 0.6%, 0.9% + 0.9%, and 1.2% + 1.2%, w/w) as active fillers were developed by solution casting method, and their preservation effects on scallop adductor muscle refrigerated at 4°C for 0, 3, 6, 9, and 12 days were evaluated. Inclusion of the two active fillers did not influence the thermal stability of the films but created heterogenous and discontinuous film microstructure and increased the film hydrophobicity. Increase in the concentrations of active fillers lowered the mechanical properties and water vapor permeability of the films but increased their crystallinity, thickness, water contact angle, opacity, antibacterial property, and antioxidant property. The longest release times for both cinnamaldehyde and α-tocopherol were found in 95% (v/v) ethanol solution. The gelatin/dextran films containing 1.2% (w/w) of active fillers (Gelatin [Ge]/Dextran [Dx]/1.2 film) improved the chemical stability of refrigerated scallop adductor muscle. The total viable count (TVC) of the unpackaged scallop adductor muscle exceeded the recommended limit of 7 lg CFU/g on day 6 (7.07 ± 0.50 lg CFU/g), whereas the TVC of the Ge/Dx/1.2 film-packaged scallop adductor muscle was still below the limit on day 9 (5.60 ± 0.50 lg CFU/g). Thus, the Ge/Dx/1.2 film can extend the shelf life of refrigerated scallop adductor muscle by at least 3 days. Overall, the developed gelatin/dextran active packaging films are promising for the preservation of aquatic food products., (© 2024 Institute of Food Technologists.)
- Published
- 2024
- Full Text
- View/download PDF
5. Effects of high-intensity ultrasound on physicochemical and gel properties of myofibrillar proteins from the bay scallop (Argopecten irradians).
- Author
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Liu B, Wu Y, Liang QY, and Zheng H
- Subjects
- Animals, Ultrasonic Waves, Chemical Phenomena, Hydrophobic and Hydrophilic Interactions, Emulsions chemistry, Pectinidae chemistry, Gels chemistry, Muscle Proteins chemistry
- Abstract
Myofibrillar proteins (MPs) have a notable impact on the firmness and flexibility of gel-based products. Therefore, enhancing the gelation and emulsification properties of scallop MPs is of paramount significance for producing high-quality scallop surimi products. In this study, we investigated the effects of high-intensity ultrasound on the physicochemical and gelation properties of MPs from bay scallops (Argopecten irradians). The carbonyl content of MPs significantly increased with an increase in ultrasound power (150, 350, and 550 W), indicating ultrasound-induced MP oxidation. Meanwhile, high-intensity ultrasound treatment (550 W) enhanced the emulsifying capacity and the short-term stability of MPs (up to 72.05 m
2 /g and 153.05 min, respectively). As the ultrasound power increased, the disulfide bond content and surface hydrophobicity of MPs exhibited a notable increase, indicating conformational changes in MPs. Moreover, in the secondary structure of MPs, the α-helix content significantly decreased, whereas the β-sheet content increased, thereby suggesting the ultrasound-induced stretching and flexibility of MP molecules. Sodium-dodecyl sulfate-polyacrylamide gel electrophoresis and scanning electron microscopy analysis further elucidated that high-intensity ultrasound induced MP oxidation, leading to modification of amino acid side chains, intra- and intermolecular cross-linking, and MP aggregation. Consequently, high-intensity ultrasound treatment was found to augment the viscoelasticity, gel strength, and water-holding capacity of MP gels, because ultrasound treatment facilitated the formation of a stable network structure in protein gels. Thus, this study offers theoretical insights into the functional modification of bay scallop MPs and the processing of its surimi products., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 The Authors. Published by Elsevier B.V. All rights reserved.)- Published
- 2024
- Full Text
- View/download PDF
6. Temporal variation in the concentrations and profiles of paralytic shellfish toxins and tetrodotoxin in scallop (Mizuhopecten yessoensis) and bloody clam (Anadara broughtonii) collected from the coast of Miyagi Prefecture, Japan.
- Author
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Shingai T, Chiba Y, Kondo M, and Yotsu-Yamashita M
- Subjects
- Animals, Japan, Marine Toxins analysis, Saxitoxin analysis, Saxitoxin analogs & derivatives, Shellfish Poisoning, Seasons, Food Contamination analysis, Tetrodotoxin analysis, Pectinidae chemistry, Bivalvia chemistry
- Abstract
For food safety, the concentrations and profiles of paralytic shellfish toxins (PSTs) and tetrodotoxin were examined in economically important scallops and bloody clams collected from the coast of the Miyagi Prefecture, Japan. PSTs were the major toxins in both species. The tetrodotoxin concentration in scallops increased in summer, although the highest value (18.7 μg/kg) was lower than the European Food Safety Authority guideline threshold (44 μg/kg). This confirmed the safety for tetrodotoxin in this area., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)
- Published
- 2024
- Full Text
- View/download PDF
7. Improving the physicochemical stability and release properties of curcumin using κ-carrageenan/scallop hydrolysates hydrogel beads.
- Author
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Yan JN, Wang YQ, Zhang ZJ, Du YN, and Wu HT
- Subjects
- Male, Animals, Hydrogels chemistry, Carrageenan chemistry, Drug Carriers chemistry, Curcumin chemistry, Pectinidae chemistry
- Abstract
Scallop (Patinopecten yessoensis) male gonad hydrolysates (SMGHs)/κ-carrageenan (KC)/KCl beads with SMGHs:KC ratios (0:10-5:5) were investigated. SMGHs/KC/KCl-Cur bead (5:5) exhibited the most intact spherical morphology and highest Cur loading content of 0.063 mg/0.1 g bead, ascribing to a shortened T
23 from 1607.9 to 966.4 ms, and red and blueshifts of OH, NH, amide I and II bands. The undetected fingerprint region within 7.82°-28.90° of SMGHs/KC/KCl-Cur beads indicated successful Cur entrapment. Moreover, SMGHs/KC/KCl-Cur beads exhibited shrinkage network backbones and larger void pores as SMGHs increased, with vessel percentage area, total number of junctions, total vessel length decreasing from 52.1, 1446.8, 57931.4 to 39.7, 530.5, 34458.4, and lacunarity increasing from 0.048 to 0.111, respectively. Furthermore, Cur showed approximately 50% release contents in colon phase and above 90% retention rate during 30 days of storage at 4 °C. These results suggested that SMGHs/KC/KCl-Cur beads exhibited sustained-release of Cur and promised stable Cur preservation., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2023 Elsevier Ltd. All rights reserved.)- Published
- 2024
- Full Text
- View/download PDF
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