文献类型：期刊文献

英文题名：A novel tyrosinase inhibitory peptide obtained from Sipunculus nudus gelatin hydrolysate: Preparation, identification, and action mechanism

作者：Zhuang, Yuxiu[1];Lin, Haisheng[1,2,3,4];Du, Lei[5];Gao, Jialong[1,2,3,4];Cao, Wenhong[1,2,3,4];Qin, Xiaoming[1,2,3,4];Chen, Zhongqin[1,2,3,4];Zheng, Huina[1,2,3,4];Zhong, Saiyi[1,2,3,4]

机构：[1]Guangdong Ocean Univ, Coll Food Sci & Technol, Zhanjiang, Peoples R China;[2]Guangdong Ocean Univ, Guangdong Prov Key Lab Aquat Prod Proc & Safety, Zhanjiang, Peoples R China;[3]Guangdong Ocean Univ, Guangdong Prov Engn Lab Marine Biol Prod, Zhanjiang, Peoples R China;[4]Guangdong Ocean Univ, Guangdong Prov Engn Technol Res Ctr Marine Food, Zhanjiang, Peoples R China;[5]East China Univ Sci & Technol, Sch Biotechnol, Dept Food Sci & Engn, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China

年份：2024

卷号：202

外文期刊名：LWT-FOOD SCIENCE AND TECHNOLOGY

收录：SCI-EXPANDED(收录号：WOS:001259845500001)、、WOS

基金：The study was carried out under the financial support of the Natural Science Foundation of Guangdong Province, China (2024A1515012130) and Innovative Team Program of High Education of Guangdong Province (2021KCXTD021) .

语种：英文

外文关键词：Sipunculus nudus; Tyrosinase inhibitory peptides; Molecular docking; Molecular dynamics simulation; Inhibition kinetics

外文摘要：Tyrosinase inhibitory peptides (TIPs) derived from food resources have attracted immense attention in the food, cosmetic, and pharmaceutical industries owing to their excellent biological safety and ease of absorption. In this study, single-factor experiment and response surface optimization were used to prepare the Sipunculus nudus gelatin enzymatic hydrolysis (SNGH) product. Subsequently, a novel tyrosinase inhibitory peptide was screened out through ultrafiltration classification, biological activity prediction, molecular docking, and molecular dynamics simulation, and its inhibitory mechanism was analyzed. The results revealed that the optimal enzymatic hydrolysis process was: the enzyme addition was 4768.87 U/g, the enzymatic hydrolysis time was 4.72 h, and the enzymatic hydrolysis temperature was 42.76 degrees C. A total of 287 peptides were detected in the ultrafiltration component I (SNGH-I) with a high tyrosinase inhibitory activity, and 161 peptides with binding energies < -7.0 kcal/mol were screened out through molecular docking. Subsequently, 91 peptides with a biological activity score >0.3 were obtained after biological activity screening. Finally, 5 possible TIPs were screened out according to their hydrophobicity, peptide score, and molecular weight. Among them, IIAPPERKY, VWDESFKVF, and FAGDDAPRAVFPS exhibited a superior tyrosinase inhibitory activity. Molecular dynamics simulations revealed that IIAPPERKY had better conformational stability and belonged to the group of reversible competitive inhibitors.