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Improvement of the Thermal Hysteresis Activity of Tilapia Skin Collagen Peptides Through Enzymatic Supramolecular Assembly Approach  ( EI收录)  

文献类型:期刊文献

英文题名:Improvement of the Thermal Hysteresis 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]; Chen, Zhongqin[1,2,3]; Tan, Mingtang[1,2,3]; Gao, Jialong[1,2,3]; Zeng, Shaokui[1,2,3]; Cao, Wenhong[1,2,3]

机构:[1] Shenzhen Institute of Guangdong Ocean University, Shenzhen, 518120, China; [2] College of Food Science and Technology, Guangdong Ocean University, Zhanjiang, 524088, China; [3] Guangdong Provincial Key Laboratory of Aquatic Products Processing and Safety, Guangdong Provincial Engineering Technology Research Centre of Seafood, Zhanjiang, 524088, China

年份:2023

外文期刊名:SSRN

收录:EI(收录号:20230281387)

语种:英文

外文关键词:Amino acids - Assembly - Collagen - Hysteresis - Supramolecular chemistry

外文摘要:To improve the usefulness of aquatic collagen peptides as green antifreeze agents, enzymatic supramolecular assembly was used to improve the thermal hysteresis activity (THA) of tilapia skin collagen peptides. Compared to collagen peptides, the THA of the glutamine-assembled product increased by 61.5% and the ice crystal content decreased by 33.93%. The THA of Gln-AFPs obtained by preliminary isolation and purification was further increased by 28.6%. The basic properties characterized Gln-AFPs as substances with strong hydrophilicity and good stability, and mass to load ratio of 174.27-553.19Da. FTIR analysis showed that most of the Gln-AFPs β-turns become β-folded, and there were α-helices generated. Furthermore, the structure of Gln-AFPs became smooth after supramolecular assembly. Thus, the enzymatic supramolecular assembly significantly enhanced the antifreeze activity of tilapia skin collagen peptides, which had the potential to be developed as a new green antifreeze agent in the food industry. ? 2023, The Authors. All rights reserved.

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