文献类型：期刊文献

英文题名：The cryoprotective activity of tilapia skin collagen hydrolysate and the structure elucidation of its antifreeze peptide

作者：Cao, Lin[1];Majura, Julieth Joram[1];Liu, Lu[1];Cao, Wenhong[1,2,3,4,5];Chen, Zhongqin[1,2,3,4];Zhu, Guoping[1,2,3,4];Gao, Jialong[1,2,3,4,5];Zheng, Huina[1,2,3,4,5];Lin, Haisheng[1,2,3,4,5]

机构：[1]Guangdong Ocean Univ, Coll Food Sci & Technol, Zhanjiang 524088, Peoples R China;[2]Natl Res & Dev Branch Ctr Shellfish Proc Zhanjiang, 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;[4]Guangdong Prov Engn Lab Marine Biol Prod, Key Lab Adv Proc Aquat Prod Guangdong Higher Educ, Zhanjiang 524088, Peoples R China;[5]Guangdong Ocean Univ, Shenzhen Inst, Shenzhen 518108, Peoples R China

年份：2023

卷号：179

外文期刊名：LWT-FOOD SCIENCE AND TECHNOLOGY

收录：SCI-EXPANDED(收录号：WOS:000997078800001)、、EI(收录号：20231213777143)、Scopus(收录号：2-s2.0-85150362135)、WOS

基金：This work was supported by the Agricultural Technology Project of Zhanjiang (2021A05187) and the Natural Science Foundation of Shenzhen (JCYJ20220530162011026) . We gratefully acknowledge the anonymous referees for comments and constructive suggestions pro- vided for improving the manuscript.

语种：英文

外文关键词：Tilapia skin; Collagen hydrolysate; Antifreeze peptides; Cryoprotective activity; Frozen storage

外文摘要：Antifreeze peptides from fish byproducts have the potential to act as suitable and safe cryoprotectants, replacing synthetic additives currently utilized in the food industry. The main focus of this study was to explore the cryoprotective activity of antifreeze peptides from collagen hydrolysate of tilapia (Oreochromis niloticus) skin and deduce the relationship between its physio-chemical characteristics and antifreeze activity. Our results showed that the antifreeze peptides from tilapia skin collagen hydrolysate (TSCP) by alcalase had a lower molecular weight of <2500 Da, higher content of hydrophilic amino acids, and thermal hysteresis activity was 0.50 degrees C. TSCP33, the identified novel cryoprotectant peptide with a molecular weight of 454.26 Da, and the amino acid sequence-NHGK showed remarkable thermal hysteresis activity (THA) of 2.63 degrees C. Frozen scallop muscles treated with 3 g/100g TSCP exhibited higher salt soluble protein concentration, total sulfhydryl content, Ca2+-ATPase activity, and water-holding capacity during the 8 weeks storage period. The cryoprotective effect of 3 g/100g TSCP was equivalent to that of the commercial phosphorus antifreeze. Our findings provide a theoretical basis for developing safe peptide-based cryoprotectants which will maintain and improve the quality of frozen foods.