文献类型：期刊文献

英文题名：The cryoprotective effect of Litopenaeus vannamei head-derived peptides and its ice-binding mechanism

作者：Majura, Julieth Joram[1];Chen, Xiujuan[1];Chen, Zhongqin[1,2,3];Tan, Mingtang[1,2,3];Zhu, Guoping[1,2,3];Gao, Jialong[1,2,3];Lin, Haisheng[1,2,3];Cao, Wenhong[1,2,3]

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

年份：2024

卷号：9

外文期刊名：CURRENT RESEARCH IN FOOD SCIENCE

收录：SCI-EXPANDED(收录号：WOS:001338763600001)、、Scopus(收录号：2-s2.0-85206443278)、WOS

基金：This work was funded by the National Natural Science Foundation of China (Grant No. 32172163) . We gratefully acknowledge and are indebted to the anonymous referees for the comments and constructive suggestions that helped improve the manuscript.

语种：英文

外文关键词：Litopenaeus vannamei shrimp; Antifreeze peptides; Ice-binding mechanism; Protein by-product; Molecular docking; Thermal hysteresis

外文摘要：Although discarded as waste, shrimp heads are a potential source of antifreeze peptides, which can be used as cryoprotectants in the food industry. Their utilization in frozen foods can help mitigate the negative effects caused by the freezing technique. Litopenaeus vannamei s hrimp heads were autolyzed, and the shrimp head autolysate (SHA) was separated via ultra-filtration and ion exchange chromatography. The antifreeze effect of SHA on the biochemical properties of myofibrillar proteins of peeled shrimps during five freeze-thaw cycles was evaluated. Peptide screening was done using the LC-MS/MS technique. A molecular docking (MD) study of the interaction between ice and shrimp head-derived antifreeze peptides was done. Results showed that shrimp-head autolysate has a maximum thermal hysteresis value of 1.84 degrees C. During the freeze-thaw cycles, the shrimp-head autolysate exhibited an antifreeze effect on frozen peeled shrimps. 1.0 and 3.0%-SHA groups showed significantly lower freeze denaturation than the negative control group. The muscle tissues of SHA-treated groups were not as severely damaged as the negative control group. The molecular docking study revealed that the shrimp head-AFPs bound to ice via hydrogen bonding, and both hydrophilic and hydrophobic amino acid residues were involved in the ice-binding interactions. 6 ice-binding sites were involved in the peptide-ice interaction. Our findings suggest that shrimp head-derived AFPs can be developed into functional additives in frozen foods and add more insights into the existing literature on antifreeze peptides.