Foods
·
2024
·Vol. 13
·期 24
·4153
·
IF 4.7
Mengcong Liu,Fuhua Li,Yuan Tang,Jichun Zhao,Xiaojuan Lei,Jian Ming
The aim of this study was to investigate the promotion of linoleic acid (OLA)-induced myofibrillar protein (MP) oxidation by boiling treatment. The effect of the boiling treatment on grass carp MP oxidation induced by OLA was investigated. The total sulfhydryl content, fluorescence intensity, and amino acid content were reduced with the increasing OLA concentration after the boiling treatment, while the boiled oxidized MP’s carbonyl content (4.76 ± 0.14 nmol/mg) was 2.14 times higher than that of the native MP (2.22 ± 0.02 nmol/mg) at an OLA concentration of 10 mM. Additionally, the secondary structure of MP became more disordered, shifting from an α-helix to random coils and β-turns. When the concentration of OLA was higher than 5 mM, both the surface hydrophobicity and water holding capacity (WHC) decreased with the increasing OLA concentration. Furthermore, the boiling treatment led to a reduction in immobile water and an increase in free water content in the MP gel. These findings establish a theoretical basis for regulating MP oxidation to improve fish quality during boiling.
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
Antioxidants
·
2021
·Vol. 10
·期 8
·1186
·
IF 6.313
Noman Walayat,Xiukang Wang,Asad Nawaz,Zhongli Zhang,Abdullah,Ibrahim Khalifa,Muhammad Hamzah Saleem,Bilal Sajid Mushtaq,Mirian Pateiro,José M. Lorenzo,Sajid Fiaz,Shafaqat Ali
This study was done to analyze the cryoprotective influence of ovalbumin (OVA) with kappa-carrageenan (KC) in grass carp myofibrillar proteins during frozen storage. Ca2+-ATPase activity of MP was significantly reduced due to protein denaturation and showed a direct association with decreased sulphydryl (SH) contents and tertiary structural properties. Besides that, an increase in carbonyl, surface hydrophobicity, and dityrosine contents was observed. The addition of OVA-KC significantly restricted the decline in Ca2+-ATPase and SH groups, which were further confirmed by the retarded increase in carbonyls. Furthermore, the addition of OVA-KC increased the stability of α-helix contents. Moreover, MP treated with 6% OVA-KC also improved intermolecular interaction forces linked with gelling and water holding properties of MP. Therefore, it can be concluded that OVA-KC could be used as an effective cryoprotectant in fish and related products for preservation and commercialization.Keywords:myofibrillar protein;cryoprotective effect;oxidative stability
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
Foods
·
2022
·Vol. 11
·期 2
·173
·
IF 5.561
Yanjiao Chu,Shanggui Deng,Guancheng Lv,Mingao Li,Hongli Bao,Yuanpei Gao,Ru Jia
In order to improve the quality of squid surimi products, squid surimi gels were prepared using several types of organic salts under two heating conditions to study the effects of organic salts on squid gel properties. Compared with the NaCl group, organic salts reduced the solubilization capacity of myofibrillar protein, and significant (p< 0.05) decreases in the breaking force, breaking distance, texture, and water-holding capacity of the gel were observed in the sodium gluconate group, while significant (p< 0.05) increases in the breaking force, breaking distance, texture, and water-holding capacity of the gel were observed in the sodium citrate and sodium tartrate groups. Although the mixed addition of NaCl and organic salt improved surimi gel quality, the effective improvement was still lower than that of only organic salt. Rheological properties indicated that sodium citrate and sodium tartrate had high viscoelasticity. The squid surimi gel prepared by direct heating exhibited better properties than gels prepared by two-step heating. The chemical force of squid gel prepared with sodium citrate and sodium tartrate formed a stronger matrix than the gels prepared with other salts. For color, the addition of sodium citrate resulted in an undesirable color of squid surimi gels, while the addition of sodium tartrate improved the whiteness of the surimi gel. The results showed that the quality of surimi gel was dependent upon the choice of heating method and the types of salt used. Sodium citrate and sodium tartrate could significantly improve the gel properties of squid surimi. This study provides reliable guidance for improving the overall quality of squid surimi gels.Keywords:squid surimi;myofibrillar protein;gel properties;organic salt
研究领域:
食品科学
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生物化学
✓ 已验证
DOI
PubMed
高影响因子
JOURNAL OF FOOD PROCESSING AND PRESERVATION
·
2020
·Vol. 44
·期 5
·e14433
·
IF 1.405
Mai-Rui Gao,Qian-Da Xu,Wei-Cai Zeng
The effect and action mechanism of tea polyphenols (TP) on the tenderness of yak meat were investigated. With the treatment of TP at the low concentrations, the myofibril fragmentation index (MFI) value of yak meat was increased and its microstructure was obviously changed. By using fluorescence spectroscopy and the determination of surface hydrophobicity, the tertiary structure of myofibrillar protein (MP) showed the obvious changes with the treatment of epigallocatechin gallate (EGCG). In addition, the secondary structure of MP was also obviously changed according to the measurement of circular dichroism (CD) spectrum, while the α-helix structure of MP decreased and the β-sheet increased. Furthermore, according to the analysis of molecular docking, EGCG could interact tightly with myofibril protein by hydrogen bonds, and changed its spatial configuration and molecular force. All results suggested that TPs showed the potentially value to improve the tenderness of yak meat in food industry. Practical applications Yak meat is more and more popular by its high nutrition value. But due to its special myofibril protein, the tenderness of yak meat is unfavorably and affects its sensory properties, which may limit its processing and consumption in food industry. In present study, TPs was used to improve the tenderness of yak meat by changing the spatial configuration and molecular force of myofibril protein, which suggested that TPs showed the potential value to enhance the quality of yak meat during its processing in food industry.
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
INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY
·
2024
·Vol. 59
·期 4
·2249-2261
·
IF 2.6
Jianyou Zhang,Aodong Yue,Lei Sun,Lifeng Fei,Pengbo Cui,Yue Qiu,Fei Lyu,Yuting Ding
Summary This study aimed to evaluate the effect of chitosan (CHI) combined electrolytic water (EW) cold sterilisation on muscle quality and myofibril proteins (MP) of large yellow croaker ( Pseudosciaena crocea ) during 12 days of refrigerated storage (4 °C). After the storage period, the sample of the EW + CHI group had the highest rate of hardness (36.68%), springiness (16.11%) among the control group without any treatment (CON), CHI group and EW group and similar tendencies were found in chewiness and cohesiveness. The MP content in the CON group decreased sharply from 80.35 mg g −1 to 57.90 mg g −1 , in contrast to the EW + CHI group, which decreased from 81.65 mg g −1 initially to 80.83 mg g −1 . The conformation of MP α-helix and β-sheet was retained to protect the secondary structure, and the exposure of aromatic amino acid residues was constrained to defend the tertiary structure in EW + CHI treatment which effectively delayed the degradation of MP. Based on these outcomes, EW + CHI treatment could significantly maintain the MP of large yellow croakers and prevent corruption during refrigerated storage.
研究领域:
食品科学
·
蛋白质化学
✓ 已验证
产品关联
DOI
高影响因子
INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY
·
2024
·Vol. 59
·期 4
·2659-2666
·
IF 2.6
Jiandong Shen,Bijiang Zhong,Wenshui Xia,Yanshun Xu
Summary Textural deterioration is a severe problem in fish industry. In order to study the role of structural proteins in refrigerated grass carp, myofibrillar proteins and collagen degradation were investigated at different stages. Results revealed that connective tissues of fish muscle disintegrated from day 1, failing to hold muscle myotomes together, with a decrease of shear force. Meanwhile, collagen solubility increased from day 1 and degradation of nebulin was observed after 3 days, while there was no obvious change in the bands of myosin heavy chain and actin. Furthermore, Pearson coefficient analysis revealed that insoluble collagen (ISC) and nebulin were significantly correlated with shear force. Negative correlation was established between drip loss and contributing factors (ISC, titin and nebulin). All results suggested that textural loss of post-mortem grass carp fillets was mainly mediated by the degradation of collagen and to a lesser extent by myofibrillar proteins at the early storage.
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
MEAT SCIENCE
·
2024
·
IF 5.7
Rui Li,Xiaoqi Li,Chen Wang,Guiming Zhang,Yabin Niu,Fashan Wei,Lin Chen,Xianchao Feng
Excessive salt intake is associated with increased risks of cardiovascular disease, while directly reducing salt content significantly decreased the quality of meat. The objective of this study was to investigate the synergistic effects of sodium tripolyphosphate (STP) and ultrasound treatment on the gel properties of MP under low-salt conditions (0.3 M NaCl). The results of FTIR spectra showed that P 3 O 10 5− group of STP bound to -NH 2 or -OH group of MP form C-N-P or C-O-P bond, indicating the STP was successfully introduced to MP. The addition of STP significantly increased the absolute value of Zeta-potential, suggesting that the presence of STP increased the electrostatic interaction of MP-MP. Importantly, STP combined with ultrasound treatment under low salt condition (STP-U 0.3 ) significantly increased solubility and decreased particle size of MP. Besides, STP-U 0.3 treatment also promoted the exposure of hydrophobic groups and improved the rheological behavior of MP, resulting in the highest gel strength (37.78 ± 0.71 g) and the lowest cooking loss (26.73 ± 0.90 %) especially in 10 mM STP combined 100 W ultrasound treatment. These results corresponded by the gradually increases of α -helix content and the decrease of tryptophan fluorescence intensity. Furthermore, results of SEM illustrated that STP-U 0.3 treatment contributed to formation of more homogeneous and dense gel network of MP gel. The above results displayed that the STP-U treatment under 0.3 M NaCl resulted in an equivalent effect to control group of 0.6 M NaCl, indicating that the combined application of STP and ultrasound has a promising potential in the low-salt meat processing industry.
研究领域:
食品科学
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生物化学
✓ 已验证
DOI
PubMed
高影响因子
FOOD RESEARCH INTERNATIONAL
·
2022
·
IF 7.425
Qingqing Yu,Tong Shi,Zhiyu Xiong,Li Yuan,Hui Hong,Ruichang Gao,Yulong Bao
In order to study the effect of oxidation on the dye-binding behavior of myofibrillar proteins, selected dyes with different charges (positively charged Sarfarin O (SO), neutral bromophenol blue (BPB), and negatively charged Orange G (OG)) were incubated with myofibrils oxidized by the Fenton system with H 2 O 2 (10 mM). Upon oxidation, loss of free thiols, formation of carbonyls, particle size, and hydrophobicity of myofibrillar proteins (MPs) increased. The absolute value of Zeta-potential increased by 14.48 % after oxidation, the myofibrillar proteins shifted to a more acidic isoelectric point (pI) upon oxidation. Oxidation decreased net positive charges of myofibrillar protein and the binding ability of MPs towards OG in the environment with pH less than pI and the affinity of MPs towards SO in the environment with pH more than pI were thus increased. Here we propose a hypothesis that oxidation-induced change in net charges is the driving force affecting the amount of protein-bound dye. This paper aims to examine the effect of oxidation on the net charges of myofibrillar proteins and to provide insight into the mechanism of oxidation-induced changes in protein-bound dyes.
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
JOURNAL OF FOOD SCIENCE
·
2023
·Vol. 88
·期 3
·977-987
·
IF 3.9
Wenfu Hou,Yile Lin,Yujie Zhang,Tingting Liu,Juan Du,Yang Yi,Hongxun Wang
This study investigated the effect of 0.8% (m/v) kojic acid treatment on changes in the microstructure and myofibrillar protein of duck meat covered with oxygen-permeable polyvinylchloride (PVC) film (9 ± 0.5 µM) during superchilled storage (−1.65 ± 0.5°C). The superchilled samples exhibited wider gaps between muscle fibers at 5 weeks storage compared with kojic acid–treated groups. Based on the variation of water status, the water-holding capacity decreased significantly ( p < 0.05), and bound water and immobilized water were gradually converted into free water during superchilled storage. For kojic acid–treated samples, however, no major changes were observed with respect to muscle structure, water status, and protein degradation at 6 weeks. The 0.8% (m/v) kojic acid treatment increased the water-holding capacity, reduced carbonyl content and protein degradation, and decreased the α-helix contents loss of myofibrillar proteins. Kojic acid treatment effectively protected myofibrillar protein structure from being destroyed during superchilled storage, suggesting that this method was a good way to reduce protein oxidation and prolonged its shelf life.
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 Biophysics
·
2020
·Vol. 15
·期 4
·397-408
·
IF 2.387
Li Xuepeng,Liu Cikun,Wang Jinxiang,Li Wenxie,Lin Boyan,Zhu Wenhui,Xu Yongxia,Yi Shumin,Mi Hongbo,Li Jianrong
This study investigated the effects of different concentrations (0, 5, 10, 20, 50, and 100 μmol/g protein) of tea polyphenols (TP) on the oxidative modification and the physicochemical, structural, and gelling properties of myofibrillar protein (MP) from grass carp ( Ctenopharyngodon idellus ) oxidized by a hydroxyl radical-generating system. The results showed that low concentrations (5 and 10 μmol/g protein) of TP could effectively inhibit the formation of carbonyl groups and dityrosine, the loss of sulfhydryl groups and α-helix conformation, and the change of the tertiary structure of MP caused by hydroxyl radicals. Moreover, the presence of TP in all concentrations decreased the surface hydrophobicity of MP. TP at 10 μmol/g protein had better effects on preventing the oxidation-induced cross-linking and aggregation of myosin heavy chain (MHC) and actin of MP, keeping the stability of MP solutions with lower turbiscan stability index (TSI) values, and improving gelling properties characterized by higher hardness and gel strength of MP gels. By contrast, excessive presence of TP (20, 50, and 100 μmol/g protein) showed pro-oxidative effects on oxidatively stressed MP, which was detrimental to the MP and contributed to the denaturation and irregular aggregation of MP, the loss of MP solution stability, and lower gelling capacity with poor texture and gel strength. The concentration-dependent effects of TP on MP depended on the extent of MP oxidative modification and MP-TP interactions, indicating that a proper amount of TP has the potential to protect MP from oxidation and to enhance the gelling capacity of surimi during processing.
研究领域:
食品科学
·
生物化学
✓ 已验证
DOI
高影响因子
FOOD CHEMISTRY
·
2025
·
IF 9.8
Hao-Xiang Gao,Nan Chen,Wei-Cai Zeng
The effects and mechanism of polyphenols, identified from Ligustrum robustum (Rxob.) Blume, on the structure of myofibrillar protein (MP) and pea protein (PP) during thermal processing were investigated. The thermal analysis revealed that polyphenols enhanced thermal stability of MP while reducing that of PP. Multispectral analysis showed PP required lower polyphenol concentrations for fluorescence quenching than MP, while elevated polyphenols reduced MP's random coil structures but increased PP's. Computational simulation demonstrated that polyphenols had more binding sites with PP but more hydrophobic interactions with MP. Furthermore, polyphenols improved fried protein foods' texture and microstructure by regulating proteins' structural changes during processing. The findings clarified the regulatory effect of L.robustum polyphenols on different protein structures at high temperatures, which altered MP and PP structures through distinct molecular interactions. The present results provide a new perspective for using LRE polyphenols to improve the quality and safety attributes of protein-based foods.
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
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2024
·
IF 7.7
Qingqing Yu,Hui Hong,Yueyue Liu,Abdul Razak Monto,Ruichang Gao,Yulong Bao
The pH buffering capacity is an important functionality of muscle proteins, and muscle foods are susceptible to being oxidized during storage and processing. In order to study the effect of oxidation on the pH buffering capacity of myofibrillar proteins, myofibrils extracted from snakehead fish ( Channa argus ) were oxidized with H 2 O 2 . Results showed that increased oxidation led to loss of free sulfhydryl groups, formation of carbonyl groups, increased surface hydrophobicity , and aggregation of myofibrillar proteins. In addition, there was a significant reduction in the content of histidine in oxidized myofibrillar proteins. The pH buffering capacity of myofibrillar proteins significantly decreased from 3.14 ± 0.03 mM H + /(mL × ΔpH) down to 2.55 ± 0.03 mM H + /(mL × ΔpH) after oxidation with 50 mM H 2 O 2 . Both oxidized myofibrillar proteins and histidine showed a high pH buffering capacity at pH near 5.8, which is the histidine pKa value. Here, we hypothesize that oxidation-induced changes in the pH buffering capacity of myofibrillar proteins were driven by oxidative modification of histidine and structural changes of myofibrillar proteins. The significance of this study to food industry may be the awareness that protein oxidation may affect pH through changes in buffering capacity. And the use of antioxidants, especially those targeting at histidine will be promising in addressing this issue.
研究领域:
食品科学
·
生物化学
✓ 已验证
DOI
PubMed
高影响因子
危险品化学品经营许可证（带存储）