INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2024
·
IF 7.7
Zhiyu Xiong,Xiangdai Wang,Ying Tian,Xin Wang,Li Yuan,Wengang Jin,Jianrong Li,Ruichang Gao
The effects of ethanol, 1,2-propanediol, and glycerol at concentrations from 10 % to 40 % on the thermal denaturation and aggregation of silver carp ( Hypophthalmichthys molitrix ) myosin were investigated. The results revealed that ethanol and 1,2-propanediol induced thermal denaturation of myosin more rapidly than glycerol, which minimally impacted the secondary structure. At 10 % concentration, 1,2-propanediol significantly influenced myosin's secondary structure more than ethanol. While at a concentration of 20 %, ethanol prompted faster thermal denaturation and aggregation, resulting in higher turbidity than 1,2-propanediol ( P < 0.05). Notably, higher concentrations of ethanol (30 % and 40 %) and 1,2-propanediol (40 %) induced the formation of non-disulfide covalent bonds, contributing to excessive myosin aggregation. Furthermore, hydrophobic interactions emerged as crucial within myosin aggregation in glycerol solutions during heating. Additionally, the effects of three alcohols at 1 %, 3 %, and 5 % on the gel properties were investigated. The results showed that an appropriate concentration of 1,2-propanediol (3 %) and glycerol (5 %) significantly enhanced the gel properties by inducing desirable unfolding and aggregation of myosin molecules. These findings offer a theoretical foundation for utilizing alcohol additives to enhance the gel quality of heat-induced surimi.
研究领域:
食品科学
·
蛋白质化学
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产品关联
DOI
PubMed
高影响因子
Food Bioscience
·
2019
·
IF 3.22
Li Wei,Liwei Cao,Shanbai Xiong,Juan You,Yang Hu,Ru Liu
The effects of pH on myosin self-assembly at low temperature to improve the structural attributes by controlling the solution conditions were studied. Myosin from silver carp was dissolved in solutions at various pH (5.0, 5.5, 6.0, 6.5, 7.0, 8.0 and 9.0). Effects of pH on the particle size, intermolecular forces, and micro-morphology of myosin at low temperature were investigated. The structures of myosin assemblies were observed to be influenced by varying pH using the variations in the degree of protonation and surface charge state of myosin molecules. The low electrostatic repulsion in acidic conditions resulted in the assembly before unfolding of myosin, leading to a relatively high turbidity and UV absorption as well as a decreased solubility. Confocal laser scanning microscopy analysis showed that myosin assemblies with coarse filamentous structure were formed in acid conditions. In alkaline conditions, the increased electrostatic repulsion led to a higher rate of unfolding than assembly and exposure of more hydrophobic residues, as showed by increased S 0 -ANS values and free SH contents. This relatively high rate of unfolding contributed to the formation of assemblies with a fine and ordered structure. At pH 7.0, the most active structure of myosin molecules was maintained as shown by the highest Ca 2+ -ATPase activity. Myosin assemblies with an ordered and uniform structure were obtained at pH 7.0.
研究领域:
食品科学
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生物化学
✓ 已验证
DOI
高影响因子
JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE
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2024
·
IF 3.3
Yulong Bao,Dan Yan,Guoliang Xu,Hui Hong,Ruichang Gao
BACKGROUND Morden advanced analytical tools offer valuable information into the understanding of molecular mechanism of traditional food processing. Chopping temperature is well-known to affect the surimi gel quality of silver carp, but the detailed molecular mechanism is not very clear. In this study, a gel-based proteomics was performed on the extracted surimi proteins under different chopping temperatures (0, 5, 10, and 25 °C) along with other physicochemical characterization of surimi proteins and gels. RESULTS With increased chopping temperature, protein extractability (in 3% sodium chloride) generally decreased, while the extracted protein generally exhibited larger surface hydrophobicity, reduced intrinsic fluorescence intensity, lower sulfhydryl content. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) profile of extracted protein showed a clear difference at 25 °C when compared with the other three temperatures, and more protein fragmentation occurred. Proteomic analysis of selected bands indicated that major myofibrillar proteins react differently with chopping temperatures, especially at 25 °C. The selected bands contained a variety of other proteins or their fragments, including adenosine triphosphate (ATP) synthase, glyceraldehyde-3-phosphate dehydrogenase, glucose-6-phosphate isomerase, heat shock protein, parvalbumin, collagen, and so forth. For the surimi gel, water-holding capacity and gel strength generally decreased with increased chopping temperature. CONCLUSION Our results suggested that chopping at 0–10 °C is acceptable for the production of silver carp surimi in terms of gel strength and water-holding capacity. However, a chopping temperature near 0 °C led to less protein oxidation and denaturation. The inferior gel quality at 25 °C is linked to a decreased concentration of extracted protein and degradation of major myofibrillar protein, the latter is likely crosslinked with sarcoplasmic proteins. © 2024 Society of Chemical Industry.
研究领域:
食品科学
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蛋白质组学
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分子生物学
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产品关联
DOI
PubMed
高影响因子
JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE
·
2024
·
IF 3.3
Wenmin Wu,Pei Gao,Qixing Jiang,Fang Yang,Dawei Yu,Peipei Yu,Wenshui Xia,Dongxing Yu
BACKGROUND The gelation properties of surimi gel under various high temperatures (115, 118, and 121 °C) and sterilization intensities ( F 0 values of 3–7 min) were systematically investigated. A kinetic model detailed quality changes during heat treatment through mathematical analysis, elucidating mechanisms for gel quality degradation. RESULTS Increased sterilization intensity significantly reduced the quality characteristics of surimi gel. Compared to the gel without sterilization treatment, when the sterilization intensity was increased to 7 min, the gel strength of the groups treated at 115 °C, 118 °C, and 121 °C decreased by 68.35%, 51.4%, and 51.71%, respectively, and the water-holding capacity decreased by 24.87%, 16.85%, and 22.5%, respectively. The hardness, chewiness, and whiteness of the gel also significantly decreased, and the changes in these indicators all conformed to a first-order kinetic model. Activation energy of 291.52 kJ mol −1 highlighted gel strength as the least heat-resistant. At equivalent sterilization intensities, 115 °C exhibited the poorest gel quality, followed by 121 °C, with 118 °C showing relatively better gel quality. Increased T 22 and decreased PT 22 suggested heightened water mobility and transition of immobilized water within the gel into free water. Protein degradation, weakened disulfide bonds and hydrophobic interaction, and protein conformation changes collectively led to a rough and incoherent gel network structure with large fissures, as verified by the results of scanning electron microscopy. Correlation analysis indicated potential for precise control over surimi gel quality by modulating physicochemical attributes. CONCLUSION The outcomes may be beneficial to improve the production and quality control of ready-to-eat surimi-based products. © 2024 Society of Chemical Industry.
研究领域:
食品科学
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生物化学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
LWT-FOOD SCIENCE AND TECHNOLOGY
·
2025
·
IF 6.6
Lingxia Su,Mengting Qiu,Qing jiang,Huiling Li,Wenjun Liu,Xumei Wang,Jun Liu,Zongcai Tu,Yanhong Shao
The aim was to evaluate the protective effects of 0.4% L-lysine (Lys) on the gel strength, water holding capacity and protein structure of frozen silver carp surimi, and to explore the mechanism of Lys delaying the quality deterioration of frozen silver carp surimi. Compared with control groups and commercial antifreeze agents, Lys-treated frozen surimi demonstrated superior rheological properties, gel strength, water holding capacity, and whiteness after 30 d of frozen storage while exhibiting a compact gel network. The mechanism of action was mainly due to the rise of pH value in the freezing process to form myofibrillar protein aggregates that exhibited high resistance to degradation, which prevented the exposure of hydrophobic amino acids and the oxidation of sulfhydryl groups, thus affecting the effective cross-linking of proteins during the gelation process and forming a denser fiber structure. The findings demonstrated the potential of Lys as a cryoprotectant, thereby establishing a theoretical foundation for the development of eco-friendly alternatives to antifreeze and high-gel frozen surimi products.
研究领域:
食品科学
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生物化学
✓ 已验证
产品关联
DOI
高影响因子
Food Biophysics
·
2016
·Vol. 11
·期 3
·266-274
·
IF 1.605
Wang Lin,Zhang Min,Fang Zhongxiang,Bhandari Bhesh,Gao Zhongxue
Oxidation extent of myofibrillar protein (MP) from silver carp ( Hypophthalmichthys molitrix ) was affected by the content and type of lipid peroxidation (LPO) products. Oxidized linoleic acid (OLA) was selected as a main representative of lipid peroxidation to investigate the effects of oxidative modification of LPO products on MP structure. Structural changes of the oxidized myofibrillar protein were evaluated by the contents of carbonyl and total sulfhydryls, surface hydrophobicity, SDS-PAGE and Fourier transform infrared spectroscopy. Heating procedure was also applied for further evaluation of gelling properties. The results from SDS-PAGE indicated that aggregation and denaturation of myosin occurred in the oxidized system. The presence of OLA intensified oxidation-initiated loss of a-helix conformation as well as tertiary structure of MP. With the addition of OLA concentration less than 3 mM, a remarkably enhanced gelling capacity of MP was observed. While the excessive covalent bond (OLA > 5 mM) could lead to the breakage of protein-protein bonds, causing the collapse of the gel structure. The gelation procedure induced by OLA involved simultaneous protein oxidation and internal cross-linking.
研究领域:
食品科学
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生物化学
✓ 已验证
DOI
高影响因子
LWT-FOOD SCIENCE AND TECHNOLOGY
·
2022
·
IF 6.056
Xiangjun Li,Aonan Luan,Xianghong Li,Faxiang Wang,Yiqun Huang,Anping Li,Yongle Liu
This research was to investigate protein changes (protein molecular weight distribution, free amino acid (FAA), cathepsin activity) in silver carp ( Hypophthalmichthys molitrix ) muscle during the process of brine curing (10 g/L s alt, 4 °C, 3 h) and air-drying (45 °C, 24 h). The results showed that after air-drying for 4 h, the proportion of protein aggregates with molecular weight >1000 kDa increased by 7.47% compared to fresh fish. Meantime, activities of cathepsin B and B + L increased from 1.52 ± 0.35 and 2.05 ± 0.45 U/g to 2.33 ± 0.22 and 3.27 ± 0.18 U/g, respectively. However, total FAA content had not significantly different ( P > 0.05) in this drying period. Thus, although protein aggregation and protein degradation occurred simultaneously, protein aggregation was dominant in the early stage of drying processing. And the protein aggregation decreased, and total FAA content increased, activities of cathepsin decreased but remained relatively high with continuous drying. Thus, protein changes in silver carp muscle were mainly due to degradation. Protein analysis in this study favored to understand the silver carp muscle changes during drying processing and supported to improve freshwater fish drying processes.
研究领域:
食品科学
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蛋白质化学
·
水产加工
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产品关联
DOI
高影响因子
JOURNAL OF BIOMEDICAL MATERIALS RESEARCH PART B-APPLIED BIOMATERIALS
·
2023
·Vol. 111
·期 12
·2055-2063
·
IF 3.4
Yaru Sun,Zeyu Wei,Ke Wang,Tianyue Xu,Rui Duan,Junjie Zhang
Collagen is used in medical dressings because of its high hydrophilicity, low immunogenicity, excellent biocompatibility, and degradability. These features can promote cell proliferation and platelet agglomeration. Herein, we studied the preparation of gel dressing by using silver carp skin collagen and bovine collagen as raw materials. Their properties and the application effects of collagen gel dressing were evaluated and compared. The centrifugal stability, rheology, and water-loss rate of silver carp skin collagen gel (SCG) and bovine tendon collagen gel (CTG) were determined. Results showed that the two gels were stable, and SCG had better rheology and ductility than CTG. However, the denaturation temperature and water-retention rate of SCG were slightly lower than those of CTG. Two collagen gels were used in the burn-repair experiment of KM mice. Results showed that the SCG and CTG were consistent with the wound-repair effect of commercially available products for shallow II-degree scald and deep II-degree scald. In the superficial shallow II scald experiment, SCG had a faster healing rate in the first 8 days and a shorter recovery time than CTG. In the deep II-degree scald experiment, the wound-healing rate of SCG on the 14th day reached 94.24%, which was 2 days faster than the recovery time of CTG. Moreover, the skin after wound healing was shallower than the scar produced after CTG treatment. Therefore, SCG had the potential to be used as the medical dressing.
研究领域:
生物材料学
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医学工程
·
创伤修复研究
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产品关联
DOI
PubMed
高影响因子
FOOD CHEMISTRY
·
2024
·
IF 8.5
Zhiyu Xiong,Jiaxin Liu,Ying Tian,Zhiyu Wang,Xinyue Wang,Tong Shi,Wengang Jin,Li Yuan,Ruichang Gao
This study investigated the effects of ethanol, 1,2-propanediol, and glycerol on the structure and aggregation behavior of silver carp ( Hypophthalmichthys molitrix ) myosin. All alcohols induced extensive alteration in the tertiary structure of myosin. Both ethanol and 1,2-propanediol further promoted an increase in the content of β-sheets in myosin and induced myosin aggregation. While glycerol had almost no impact on the secondary structure of myosin. Molecular dynamics simulations revealed that increasing the concentration of ethanol and 1,2-propanediol affected the overall structural changes in the myosin heavy chain (MHC), while glycerol exerted a more pronounced effect on the MHC tail when compared to the MHC head. Disruption of the hydration layers induced by ethanol and 1,2-propanediol contributed to local structural changes in myosin. Glycerol at a concentration of 20% induced the formation of a larger hydration layer around the MHC tail, which facilitated the stabilization of the protein structure.
研究领域:
食品科学
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生物化学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
FOOD CHEMISTRY
·
2021
·
IF 7.514
Shan Qian,Peipei Dou,Junlan Wang,Lin Chen,Xinglian Xu,Guanghong Zhou,Beiwei Zhu,Niamat Ullah,Xianchao Feng
The objective of this study was to explore the oxidative modification induced by AAPH (2,2′-azobis (2-amidinopropane) dihydrochloride) on the microbial transglutaminase (MTGase) cross-linking reaction and gelling properties of silver carp myofibril protein (SCMP). Compared to AAPH treatment, MTGase addition resulted further changes of protein properties as evidenced by the decreasing free amino and thiol group content, the decreased secondary and tertiary structure, and the increasing storage modulus (G′) and gel strength ( P < 0.05). The proper oxidation induced by AAPH (5 mM) promoted the glutamine-lysine and disulfide cross-linking due to MTGase (10 U/g). Therefore, the quality of the SCMP gel was improved with a good water-holding capacity (WHC), gel strength and G′. This results could lay a theoretical foundation for the development of silver carp surimi products with good quality. Chemical compounds: (2,2′-azobis(2-amidinopropane)dihydrochloride (PubChem CID:76344); O-Phthalaldehyde (PubChem CID:4807); 5,5′-Dithiobis(2-Nitrobenzoic Acid) (PubChem CID:6254); 8-Anilino-1-naphthalenesulfonic acid (PubChem CID:1369); Acrylamide (PubChem CID: 6579); β -Mercaptoethanol (PubChem CID: 1567); Sodium dodecyl sulfate (PubChem CID:3423265)
研究领域:
食品科学
·
生物化学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
FOOD CHEMISTRY
·
2020
·
IF 6.306
Huimin Zhang,Dan Wu,Qilin Huang,Zhiyu Liu,Xiaogang Luo,Shanbai Xiong,Tao Yin
Yeast β-glucan (YG) adsorbs off-odor in silver carp mince due to its more porous structure. To explore adsorption behavior and mechanism, adsorption kinetics and thermodynamics of YG for 3 off-odor compounds (hexanal, 1-octen-3-ol and nonanal) were investigated by pseudo-first/second-order models and isothermal equations (Langmuir, Freundlich and Redlich-Peterson). Kinetic experiments indicated adsorption process followed pseudo-first-order model. Adsorption isotherms indicated 3 off-odors could easily be adsorbed by YG and adsorption capacity was in the order of 1-octene-3-ol > hexanal > nonanal . Thermodynamic result suggested adsorption of 3 off-odors by YG was endothermic and spontaneous, and was driven predominantly by physisorption and hydrophobic interaction. Consequently, the contents of 3 off-odors that released from mince/YG complex decreased by 22.8%, 29.9%, and 24.5% ( p < 0.05), respectively, compared with those from mince without YG. Therefore, the addition of YG enhanced the binding capability to off-odors, thus reducing the release of off-odor from silver carp mince.
研究领域:
食品科学
·
化学工程
·
热力学
·
动力学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
危险品化学品经营许可证（带存储）