文献类型：期刊文献

英文题名：Molecular insights into the antifreeze mechanism of collagen peptides based on their interaction with ice crystals

作者：Liang, Jiajian[1,2];Chen, Xiujuan[1,2];Tan, Mingtang[1,2,3];Chen, Zhongqin[1,2,3];Lin, Haisheng[1,2,3];Gao, Jialong[1,2,3];Zheng, Huina[1,2,3];Cao, Wenhong[1,2,3]

机构：[1]Guangdong Ocean Univ, Shenzhen Inst, Shenzhen 518108, Peoples R China;[2]Guangdong Ocean Univ, Coll Food Sci & Technol, 1 Haida Rd, Zhanjiang 524088, Peoples R China;[3]Guangdong Prov Engn Technol Res Ctr Seafood, Guangdong Prov Key Lab Aquat Prod Proc & Safety, Zhanjiang 524088, Peoples R China

年份：2025

卷号：26

外文期刊名：FOOD CHEMISTRY-X

收录：SCI-EXPANDED(收录号：WOS:001442803400001)、、EI(收录号：20251018000362)、Scopus(收录号：2-s2.0-85219712831)、WOS

基金：This work was supported by the Shenzhen Science and Technology Program (JCYJ20220530162011026) . We gratefully acknowledge the anonymous referees for the comments and constructive suggestions provided for improving the manuscript.

语种：英文

外文关键词：Cod collagen peptide; Channa argus surimi; Antifreeze activity; Protein denaturation; Molecular docking

外文摘要：This study explores the molecular-level cryoprotective effect of cod collagen peptide-1 (CCP-1) on surimi during freeze-thaw cycles, examining its interaction with ice crystals and its role in maintaining the structural integrity of surimi. Results indicated that CCP-1 exhibited the most effective cryoprotection on catalase, preserving 83.4 % of its residual enzyme activity, and prevented myofibrillar protein (MP) from freeze denaturation by sustaining the activity of Ca2+-ATPase and maintaining structural integrity. The antifreeze effect of CCP-1 (1.0 % and 3.0 %, w/w) is comparable to that of commercial antifreeze containing 0.5 % compound phosphate (w/w). Moreover, CCP-1's ability to interact with ice crystals is closely tied to its primary structure, where hydrophilic and hydrophobic amino acids work in tandem. Specifically, alkaline and acidic amino acids are capable of forming stronger hydrogen bonds, thereby enhancing their interaction with ice crystals. This work offers a theoretical basis for analyzing the binding behavior of antifreeze peptides with varying amino acid compositions.