文献类型：期刊文献

英文题名：Tracking protein aggregation behaviour and emulsifying properties induced by structural alterations in common carp (Cyprinus carpio) myofibrillar protein during long-term frozen storage

作者：Sun, Qinxiu[1,2];Kong, Baohua[3];Zheng, Ouyang[2];Liu, Shucheng[2];Dong, Xiuping[1]

机构：[1]Dalian Polytech Univ, Sch Food Sci & Technol, Dalian 116034, Peoples R China;[2]Guangdong Ocean Univ, Coll Food Sci & Technol, Zhanjiang 524088, Guangdong, Peoples R China;[3]Northeast Agr Univ, Coll Food Sci, Harbin 150030, Heilongjiang, Peoples R China

年份：2024

卷号：264

外文期刊名：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES

收录：SCI-EXPANDED(收录号：WOS:001220661400001)、、EI(收录号：20241115733529)、Scopus(收录号：2-s2.0-85187204003)、WOS

基金：Acknowledgements This study was supported by the Youth Fund of the National Naturalr Science Foundation of China (32302165) , Scientific and Technological Innovation Strategy of Guangdong Province (2022A05036) , and Guang Dong Basic and Applied Basic Research Foundation (2023A1515011513) .

语种：英文

外文关键词：Common carp; Freezing method; Frozen storage; Myofibrillar protein structure; Emulsifying properties

外文摘要：The effect of ultrasound-assisted immersion freezing (UIF), air freezing (AF), and immersion freezing (IF) on the protein structure, aggregation, and emulsifying properties of common carp (Cyprinus carpio) myofibrillar protein during frozen storage were evaluated in the present study. The result showed that, compared with AF and IF samples, UIF sample had higher reactive/total sulfhydryl, protein solubility, and lower protein turbidity (P < 0.05), indicating that UIF was beneficial to inhibit protein oxidation and aggregation induced by frozen storage. UIF inhibited the alteration of secondary structure and tertiary structure during frozen storage. Meanwhile, UIF sample had higher emulsifying activity index, and smaller emulsion droplet diameter than AF and IF samples (P < 0.05), suggesting that UIF was beneficial for maintaining the emulsifying properties of protein during storage. In general, UIF is a potential and effective method to suppress the decrease in protein emulsifying properties during long-term frozen storage.