文献类型：期刊文献

英文题名：Optimization of a Novel Tyrosinase Inhibitory Peptide from Atrina pectinata Mantle and Its Molecular Inhibitory Mechanism

作者：Wang, Wen[1];Lin, Haisheng[1,2,3,4,5,6,7];Shen, Weiqiang[1];Qin, Xiaoming[1,2,3,4,5,6,7];Gao, Jialong[1,2,3,4,5,6,7];Cao, Wenhong[1,2,3,4,5,6,7];Zheng, Huina[1,2,3,4,5,6,7];Chen, Zhongqin[1,2,3,4,5,6,7];Zhang, Zhishu[1]

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 Key Lab Aquat Prod Proc & Safety, Zhanjiang 524088, Peoples R China;[4]Guangdong Prov Engn Technol Res Ctr Seafood, Zhanjiang 524088, Peoples R China;[5]Guangdong Prov Engn Lab Marine Biol Prod, Zhanjiang 524088, Peoples R China;[6]Guangdong Ocean Univ, Shenzhen Inst, Shenzhen 518108, Peoples R China;[7]Dalian Polytech Univ, Collaborat Innovat Ctr Seafood Deep Proc, Dalian 116034, Peoples R China

年份：2023

卷号：12

期号：21

外文期刊名：FOODS

收录：SCI-EXPANDED(收录号：WOS:001103307700001)、、Scopus(收录号：2-s2.0-85176613624)、WOS

基金：This work was supported by the Earmarked Fund for China Agriculture Research System(CARS-49), the Doctoral Startup Project of Guangdong Ocean University (R17082), the Science and Technology Special Fund Project of Guangdong Province (2021A05197), the Innovative Team Program of High Education of Guangdong Province (2021KCXTD021) and the Postgraduate Education Innovation Project of Guangdong Ocean University (202262).

语种：英文

外文关键词：Atrina pectinata mantle; gelatin peptide; inhibition kinetic; molecular docking

外文摘要：In order to realize the multi-level utilization of marine shellfish resources and to develop the potential biological activity of processing by-products of Atrina pectinata, gelatin was extracted from the mantle and the potential whitening effect of its enzymatic peptides was explored. Taking tyrosinase inhibitory activity as the evaluation index, the enzyme hydrolysate process was optimized by response-surface methodology, and the optimal enzyme hydrolysate conditions were as follows: pH 5.82, 238 min enzyme hydrolysate time, and temperature of 54.5 degrees C. Under these conditions, the tyrosinase inhibition activity of Atrina pectinata mantle gelatin peptide (APGP) was 88.6% (IC50 of 3.268 +/- 0.048 mg/mL). The peptides obtained from the identification were separated by ultrafiltration and LC-MS/MS, and then four new peptides were screened by molecular docking, among which the peptide Tyr-Tyr-Pro (YYP) had the strongest inhibitory effect on tyrosinase with an IC50 value of 1.764 +/- 0.025 mM. The molecular-docking results indicated that hydrogen bonding is the main driving force for the interaction of the peptide YYP with tyrosinase. From the Lineweaver-Burk analysis, it could be concluded that YYP is inhibitory to tyrosinase and exhibits a mixed mechanism of inhibition. These results suggest that YYP could be widely used as a tyrosinase inhibitor in whitening foods and pharmaceuticals.