文献类型：期刊文献

英文题名：Improvement of the antifreeze activity of tilapia skin collagen peptides through enzymatic supramolecular assembly approach

作者：Ouyang, Jijin[1,2];Han, Mei[1,2];Majura, Julieth Joram[1,2];Chen, Xiujuan[1,2];Tan, Mingtang[1,2,3,4];Chen, Zhongqin[1,2,3,4];Gao, Jialong[1,2,3,4];Zheng, Huina[1,2,3,4];Lin, Haisheng[1,2,3,4];Cao, Wenhong[1,2,3,4]

机构：[1]Guangdong Ocean Univ, Shenzhen Inst, Shenzhen 518120, Peoples R China;[2]Guangdong Ocean Univ, Coll Food Sci & Technol, 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

年份：2024

卷号：59

期号：5

起止页码：3360

外文期刊名：INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY

收录：SCI-EXPANDED(收录号：WOS:001194429400001)、、EI(收录号：20241515879065)、Scopus(收录号：2-s2.0-85189619148)、WOS

基金：This work was supported by the Natural Science Foundation of Shenzhen (JCYJ20220530162011026) and the Science and Technology Project of Zhanjiang (2021A05187). We appreciate Julieth Majura for her assistance in proofreading and revising the language of the manuscript.

语种：英文

外文关键词：Antifreeze activity; collagen peptides; enzymatic supramolecular assembly; thermal hysteresis activity

外文摘要：Enzymatic supramolecular assembly was applied to increase the thermal hysteresis activity (THA) of tilapia skin collagen peptides and their applicability as cryoprotectants. The THA value of the glutamine-assembled product increased by 61.5% and its ice crystal content dropped by 33.93% compared to the collagen peptides. Following initial separation and purification, the THA of Gln-AFPs was further elevated by 28.6%. After five freeze-thaw cycles, tilapia surimi treated with 8% Gln-AFPs had high levels of salt-soluble protein, total sulfhydryl content, Ca2+-ATPase activity, and water-holding capacity. Additionally, the cryoprotective effect of Gln-AFPs on the surimi was found to be superior to that of commercial antifreeze. The majority of the Gln-AFPs turns folded, according to FTIR analysis, and -helices were produced. After supramolecular assembly, the Gln-AFPs structure also smoothed out. As a result, the enzymatic supramolecular assembly drastically increased the antifreeze activity of the tilapia skin-collagen peptides, which could eventually be developed into a novel antifreeze additive in the food industry. Enzymatic supramolecular assembly leads to a significant increase in the antifreeze activity of tilapia collagen peptides. Freeze-thaw experiments showed that an 8% addition of Gln-AFPs had the best antifreeze effect. TGase crosslinks glutamine to protein molecules via an acyl transfer reaction, thereby improving its antifreeze activity. image