文献类型：期刊文献

英文题名：Cryoprotective effect of trehalose on myofibrillar protein of snakehead fish (Channa argus) during freeze-thaw cycles

作者：Zhang, Lin[1,2];Zhang, Nana[1,2];Yu, Xiliang[1,2];Wang, Yue[1,2];Sun, Qinxiu[3];Dong, Xiuping[1,2]

机构：[1]Dalian Polytech Univ, Natl Engn Res Ctr Seafood, Liaoning Prov Collaborat Innovat Ctr Marine Food D, Dalian Technol Innovat Ctr Chinese Prepared Food,S, Dalian 116034, Liaoning, Peoples R China;[2]Dalian Polytech Univ, Acad Food Interdisciplinary Sci, Sch Food Sci & Technol, Dalian 116034, Liaoning, Peoples R China;[3]Guangdong Ocean Univ, Coll Food Sci & Technol, Zhanjiang 524088, Peoples R China

年份：2025

卷号：474

外文期刊名：FOOD CHEMISTRY

收录：SCI-EXPANDED(收录号：WOS:001424894700001)、、EI(收录号：20250617819047)、Scopus(收录号：2-s2.0-85216903088)、WOS

基金：This work was funded by the National Key Research and Develop-ment Program of China (2023YFD2100200) and Liaoning Revitalization Talents Program (XLYC2202047) .

语种：英文

外文关键词：Channa argus; Myofibrillar protein; Trehalose content; Freeze-thaw cycles; Protein structure

外文摘要：This study investigated the cryoprotective effect of trehalose on myofibrillar protein (MP) of snakehead fish (Channa argus) during freeze-thaw (F-T) cycles. After 7 F-T cycles, trehalose reduced solubility loss by 9.8 % compared to control group. Turbidity and surface hydrophobicity increased significantly with repeated F-T cycles. However, trehalose, particularly at 1.5 %, effectively inhibited these changes by stabilizing the structure and reducing aggregation. Sulfhydryl content decreased by 10.8 % less in the trehalose group than in the control group, indicating reduced oxidative damage and maintaining sulfhydryl groups. Differential scanning calorimetry (DSC) and scanning electron microscope (SEM) showed that trehalose reduced freezable water content and minimized structural damage caused by ice crystals, with 1.5 % trehalose exhibiting the most pronounced effect. Trehalose's polyhydroxylated structure forms hydrogen bonds with polar residues, reducing hydrophobic interactions and maintaining protein stability. Additionally, trehalose reduced secondary structure degradation, offering optimal protection against oxidation, aggregation, and structural damage during F-T cycles.