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从脱脂核桃(Juglans regia L.)粕水解物中分离、鉴定和对接酪氨酸酶抑制肽。

Separation, identification, and molecular docking of tyrosinase inhibitory peptides from the hydrolysates of defatted walnut (Juglans regia L.) meal.

机构信息

Beijing Key Laboratory of Forest Food Processing and Safety, College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing 100083, People's Republic of China.

Hebei Huang Jin Long Agricultural Technology Co. LTD, (Heibei province, She County), People's Republic of China.

出版信息

Food Chem. 2021 Aug 15;353:129471. doi: 10.1016/j.foodchem.2021.129471. Epub 2021 Mar 9.

DOI:10.1016/j.foodchem.2021.129471
PMID:33730668
Abstract

Defatted walnut meal protein was hydrolyzed using alcalase to yield tyrosinase inhibitory peptides. After separation by ultrafiltration and Sephadex G-25, the fraction with the highest tyrosinase inhibitory activity was identified using liquid chromatography-tandem mass spectrometry and 606 peptides were obtained. Then, molecular docking was used to screen for tyrosinase inhibitory peptides and to clarify the theoretical interaction mechanism between the peptides and tyrosinase. A peptide with the sequence Phe-Pro-Tyr (FPY, MW: 425.2 Da) was identified and the synthesized peptide inhibited tyrosine monophenolase and diphenolase with IC values of 1.11 ± 0.05 and 3.22 ± 0.09 mM, respectively. The inhibition of tyrosinase by FPY was competitive and reversible. Good stability of FPY toward digestion was observed in an in vitro gastrointestinal digestion simulation experiment. These results indicated that FPY can be used as a potential tyrosinase inhibitor in the food, medicine, and cosmetics industries.

摘要

脱脂核桃蛋白粉用碱性蛋白酶水解,得到具有酪氨酸酶抑制活性的肽段。经超滤和葡聚糖凝胶 G-25 分离后,采用液相色谱-串联质谱鉴定出具有最高酪氨酸酶抑制活性的级分,得到 606 条肽段。然后,利用分子对接筛选出具有酪氨酸酶抑制活性的肽段,并阐明了肽段与酪氨酸酶之间的理论相互作用机制。鉴定出一种具有序列为苯丙氨酸-脯氨酸-酪氨酸(FPY,MW:425.2 Da)的肽段,合成的肽段对酪氨酸单酚酶和二酚酶的抑制 IC 值分别为 1.11±0.05 和 3.22±0.09 mM。FPY 对酪氨酸酶的抑制作用是竞争性和可逆的。在体外胃肠消化模拟实验中观察到 FPY 对消化的良好稳定性。这些结果表明,FPY 可作为食品、医药和化妆品行业潜在的酪氨酸酶抑制剂。

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