Article
Multidisciplinary Sciences
Juliany Cristiny Sonda Bordignon, Amanda Teixeira Badaro, Douglas Fernandes Barbin, Lilian Regina Barros Mariutti, Flavia Maria Netto
Summary: This study investigated the oxidative susceptibility of whey protein isolate (WPI) dispersions treated by microwave or thermal convection before freeze-drying. The results suggest that microwave heating increased the degree of protein oxidation.
Article
Food Science & Technology
Haifeng Wang, Zhi Yang, Huijuan Yang, Jing Xue, Yunyan Li, Shitong Wang, Lijun Ge, Qing Shen, Manman Zhang
Summary: The gel properties of myofibrillar proteins (MPs) from different meat sources were compared, showing variations in gel strength and structure. Pork MPs exhibited the highest gel strength and most compact structure, while fish MPs had the lowest gel strength and loosest structure. Pork MPs also had the highest content of myosin heavy chain and actin.
LWT-FOOD SCIENCE AND TECHNOLOGY
(2022)
Review
Food Science & Technology
Yuemei Zhang, Genpeng Bai, Guofeng Jin, Ying Wang, Jinpeng Wang, Eero Puolanne, Jinxuan Cao
Summary: Understanding the mechanisms of myofibrillar protein gelation is crucial for the development of gel-type muscle foods. This review elaborates on the role of low molecular additives in modifying intermolecular interactions during gelation. The strengthening of hydrophobic interactions is found to be the main contributing factor to improved gelation.
CRITICAL REVIEWS IN FOOD SCIENCE AND NUTRITION
(2022)
Article
Chemistry, Applied
Yueyue Liu, Yuqing Tan, Yongkang Luo, Xingmin Li, Hui Hong
Summary: The thawing process has a significant impact on the oxidation and property changes of myofibrillar proteins (MPs) in frozen stored fish fillets, causing degradation and intensified oxidation reactions of MPs.
Article
Chemistry, Applied
Wenhui Ma, Qi Yang, Xin Fan, Xianqi Yao, Jiwei Kuang, Cong Min, Yungang Cao, Junrong Huang
Summary: The effects of inulin, glutathione, and their combination on the structure and gel properties of oxidized pork myofibrillar protein were investigated. Glutathione prevented protein oxidation and aggregation, while inulin enhanced the gel behavior of the protein. Treatment with inulin and glutathione together resulted in the highest cooking yield and improved texture characteristics.
Article
Nutrition & Dietetics
Haihua Cong, Qiming Wu, Zhuoran Zhang, Juntao Kan
Summary: By glycosylation with protein using appropriate sugar donors, the stability and emulsification properties of fish proteins can be improved. This research explores the impact of enzymatic chitosan oligosaccharide (CO) at different concentrations on silver carp myofibrillar protein (MP), aiming to understand the influence of electrostatic binding between MP and CO on protein conformation. The study reveals that CO and MP form complexes through hydrogen bonding and electrostatic interactions, and CO modification enhances the solubility, foaming, and foaming stability of MP.
FRONTIERS IN NUTRITION
(2023)
Article
Chemistry, Applied
Deyin Pan, Jinming Ma, Jingjing Diao, Jiaqi Li, Hongsheng Chen
Summary: This study investigated the effects of eugenol on the structure and gel properties of oxidized pork myofibrillar protein. The results showed that a high concentration of eugenol could protect the protein structure and enhance the gel properties.
Article
Food Science & Technology
Wenhui Wang, Xiaolei Jia, Chuanyu Guo, Jinfeng Pan, Xiuping Dong, Shengjie Li
Summary: The present study compared two common oxidizing systems in meat for their effects on protein oxidation patterns, focusing on lysine-derived markers for protein carbonylation. The results demonstrated that both oxidizing systems can contribute to the formation of specific lysine markers and may also directly impact protein structure and functionality.
FOOD RESEARCH INTERNATIONAL
(2023)
Article
Chemistry, Applied
Daojiu Zhang, Xu Yang, Yichun Wang, Biao Wang, Shaoyu Wang, Jinyang Chang, Suwen Liu, Hao Wang
Summary: This study investigated the effects of Proanthocyanidin B2 (PCB2) and transglutaminase (TGase) on the gel properties of myofibrillar protein (MP). The results showed that the addition of TGase and PCB2 increased the hydrophobicity and water holding capacity of MP, and also caused changes in its secondary and tertiary structures. Microscopic and nuclear magnetic resonance analysis revealed that the addition of TGase and PCB2 resulted in the formation of a dense MP network structure and reduced the amount of free water.
Article
Chemistry, Applied
Hua Chen, Gaiming Zhao, Xiaoling Yu, Qiuhui Zhang, Chaozhi Zhu, Lin Tong, Jiangang Hao
Summary: The study investigated the effects of different heating temperatures (40-115 degrees C) on the structure, oxidation, and digestibility of beef myofibrillar protein. The results showed that the protein underwent oxidation, with a decrease in sulfhydryl groups and an increase in carbonyl groups as the temperature increased. The protein underwent conformational changes and expanded at temperatures between 40 degrees C and 85 degrees C, but aggregated at temperatures over 85 degrees C due to thermal oxidation. The digestibility of the protein increased up to 85 degrees C and then decreased, suggesting that moderate heating and oxidation-induced protein expansion were beneficial to digestion, while excessive heating and protein aggregation were not.
Article
Biochemical Research Methods
Maria K. Koshkina, Mikhail D. Shelomov, Anastasia A. Pometun, Svyatoslav S. Savin, Vladimir I. Tishkov, Denis L. Atroshenko
Summary: In order to accelerate SDS-PAGE, an optimized version of the technique was proposed using experimental tuning and theoretical description. The resulting system involved diluting the gel buffer, supplementing with glycine, and applying a higher voltage, reducing runtime from 90 to 18 min. Despite the higher voltage, band resolution did not decrease compared to the original method. This acceleration approach can be applied to other variants of SDS-PAGE.
Article
Food Science & Technology
Jinyang Chang, Xu Yang, Jing Li, Qingquan Fu, Jiaping Zhou, Juan Zhao, Nan Zhang, Qingdai Liu, Tianxin Wang, Hao Wang
Summary: This study investigated the effects of chlorogenic acid (CA) and transglutaminase (TGase) on the physicochemical and gel properties of myofibrillar protein (MP). The results showed that TGase improved the gel structures of oxidized MP treated with CA at moderate doses. TGase also enhanced the water-holding capability and moisture distribution of the MP gel. Additionally, TGase enhanced protein cross-linking and improved gel properties.
LWT-FOOD SCIENCE AND TECHNOLOGY
(2023)
Article
Food Science & Technology
Sanjun Jin, Min Wang, Hao Yang, Anshan Shan, Xingjun Feng
Summary: Resveratrol supplementation was found to inhibit protein oxidation and improve the protein structure of duck breast muscle stored under specific conditions, with the dietary inclusion of 300-400 mg/kg being more effective.
Article
Food Science & Technology
Qingqing Yu, Tong Shi, Zhiyu Xiong, Li Yuan, Hui Hong, Ruichang Gao, Yulong Bao
Summary: This study investigated the effect of oxidation on the dye-binding behavior of myofibrillar proteins. Selected dyes with different charges were incubated with myofibrils oxidized by the Fenton system. The results showed that oxidation increased the particle size, hydrophobicity, and absolute value of Zeta-potential of myofibrillar proteins, while decreasing the net positive charges. The binding ability of myofibrillar proteins towards certain dyes was affected by the pH environment, suggesting that oxidation-induced change in net charges is the driving force affecting the amount of protein-bound dye.
FOOD RESEARCH INTERNATIONAL
(2023)
Article
Food Science & Technology
Wei Rao, M. S. Roopesh, Daodong Pan, Lihui Du
Summary: This study evaluated the effects of plasma-activated water (PAW) with different discharge times on the gel properties and conformational changes of duck myofibrillar protein (DMP). The results showed that PAW treatment significantly increased the gel strength and water-holding capacity of DMP gels. PAW improved the hydrophobic interactions between protein molecules, resulting in a more ordered and homogeneous gel microstructure.