文献类型：期刊文献

英文题名：Insight into the structure-activity relationship of thermal hysteresis activity of cod collagen peptides through peptidomics and bioinformatics approaches

作者：Liang, Jiajian[1,2];Chen, Xiujuan[1,2];Majura, Julieth Joram[1,2];Tan, Mingtang[1,2,3];Chen, Zhongqin[1,2,3];Gao, Jialong[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：463

外文期刊名：FOOD CHEMISTRY

收录：SCI-EXPANDED(收录号：WOS:001331902400001)、、EI(收录号：20244117160400)、Scopus(收录号：2-s2.0-85205594648)、WOS

基金：Acknowledgments 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; Antifreeze peptide; Thermal hysteresis activity; Peptideomics; Bioinformatics

外文摘要：To elucidate the correlation between variations in thermal hysteresis activity (THA) and the physicochemical properties and structure, antifreeze peptides (AFPs) of isolated fractions (CCP-1 and CCP-2) were characterized on based peptidomics and bioinformatics. The results revealed a positive correlation between the THA of cod collagen antifreeze peptide (CCAFP) and peptide chain length, isoelectric point, and hydrophobic amino acid content. Notably, the THA of CCP-1, which has higher alkaline amino acid content, was 2.60 degrees C at a concentration of 10 mg/mL, significantly higher than CCP (1.90 degrees C) and CCP-2 (2.27 degrees C). Glycine, proline, and valine were the vital amino acids to the formation of hydrogen bonds. Conversely, aspartic and glutamic acids at terminal regions of AFPs tended to introduce kinks in their structures. This distortion reduced binding sites for ice crystals, thereby decreasing their THA, providing a theory for understanding the physicochemical properties and structure of AFPs that influence their THA.