{"title":"马氏珠母贝肉酪氨酸酶抑制肽的分离、鉴定和制备。","authors":"Jinhao Meng, Jiaojiao Liu, Jing Lu, Pingyingzi Jiang, Yunxia Bai, Xiaoling Liu, Shubo Li","doi":"10.1007/s10529-023-03437-0","DOIUrl":null,"url":null,"abstract":"<p><p>Recently, natural tyrosinase inhibitors have gained attention in clinical cosmetology research. In this study, the enzymatic hydrolysis of Pinctada martensii meat by protease from Bacillus licheniformis, 401 peptides with tyrosinase inhibitory were identified after isolated by ultrafiltration and Sephadex G-15 from the fraction F4. The peptide effects on the tyrosinase activity and structure were evaluated using molecular docking. Three synthetic peptides classified as W1 (WDRPKDDGGSPIK), W2 (DRGYPPVMF), and W3 (SGGGGGGGLGSGGSIRSSY), which had the lowest binding energies were selected for in vitro synthesis and biological activity investigation. The W3 peptide (5 mg/mL) had the highest tyrosinase activity, SPF, DPPH, and ABTS clearance values, and total antioxidant capacity. W3 did not affect the survival rate of mouse melanoma B16-F10 cells (1.0-5.0 mg/mL) but decreased the melanin content. Hence, W3 could be suitable for multifunctional tyrosinase inhibition and provides a novel method to use marine organisms as natural tyrosinase inhibitor sources.</p>","PeriodicalId":2,"journal":{"name":"ACS Applied Bio Materials","volume":null,"pages":null},"PeriodicalIF":4.6000,"publicationDate":"2023-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Isolation, identification, and preparation of tyrosinase inhibitory peptides from Pinctada martensii meat.\",\"authors\":\"Jinhao Meng, Jiaojiao Liu, Jing Lu, Pingyingzi Jiang, Yunxia Bai, Xiaoling Liu, Shubo Li\",\"doi\":\"10.1007/s10529-023-03437-0\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Recently, natural tyrosinase inhibitors have gained attention in clinical cosmetology research. In this study, the enzymatic hydrolysis of Pinctada martensii meat by protease from Bacillus licheniformis, 401 peptides with tyrosinase inhibitory were identified after isolated by ultrafiltration and Sephadex G-15 from the fraction F4. The peptide effects on the tyrosinase activity and structure were evaluated using molecular docking. Three synthetic peptides classified as W1 (WDRPKDDGGSPIK), W2 (DRGYPPVMF), and W3 (SGGGGGGGLGSGGSIRSSY), which had the lowest binding energies were selected for in vitro synthesis and biological activity investigation. The W3 peptide (5 mg/mL) had the highest tyrosinase activity, SPF, DPPH, and ABTS clearance values, and total antioxidant capacity. W3 did not affect the survival rate of mouse melanoma B16-F10 cells (1.0-5.0 mg/mL) but decreased the melanin content. Hence, W3 could be suitable for multifunctional tyrosinase inhibition and provides a novel method to use marine organisms as natural tyrosinase inhibitor sources.</p>\",\"PeriodicalId\":2,\"journal\":{\"name\":\"ACS Applied Bio Materials\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":4.6000,\"publicationDate\":\"2023-12-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"ACS Applied Bio Materials\",\"FirstCategoryId\":\"5\",\"ListUrlMain\":\"https://doi.org/10.1007/s10529-023-03437-0\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2023/10/24 0:00:00\",\"PubModel\":\"Epub\",\"JCR\":\"Q2\",\"JCRName\":\"MATERIALS SCIENCE, BIOMATERIALS\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"ACS Applied Bio Materials","FirstCategoryId":"5","ListUrlMain":"https://doi.org/10.1007/s10529-023-03437-0","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2023/10/24 0:00:00","PubModel":"Epub","JCR":"Q2","JCRName":"MATERIALS SCIENCE, BIOMATERIALS","Score":null,"Total":0}
Isolation, identification, and preparation of tyrosinase inhibitory peptides from Pinctada martensii meat.
Recently, natural tyrosinase inhibitors have gained attention in clinical cosmetology research. In this study, the enzymatic hydrolysis of Pinctada martensii meat by protease from Bacillus licheniformis, 401 peptides with tyrosinase inhibitory were identified after isolated by ultrafiltration and Sephadex G-15 from the fraction F4. The peptide effects on the tyrosinase activity and structure were evaluated using molecular docking. Three synthetic peptides classified as W1 (WDRPKDDGGSPIK), W2 (DRGYPPVMF), and W3 (SGGGGGGGLGSGGSIRSSY), which had the lowest binding energies were selected for in vitro synthesis and biological activity investigation. The W3 peptide (5 mg/mL) had the highest tyrosinase activity, SPF, DPPH, and ABTS clearance values, and total antioxidant capacity. W3 did not affect the survival rate of mouse melanoma B16-F10 cells (1.0-5.0 mg/mL) but decreased the melanin content. Hence, W3 could be suitable for multifunctional tyrosinase inhibition and provides a novel method to use marine organisms as natural tyrosinase inhibitor sources.