{"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":8929,"journal":{"name":"Biotechnology Letters","volume":null,"pages":null},"PeriodicalIF":2.0000,"publicationDate":"2023-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biotechnology Letters","FirstCategoryId":"5","ListUrlMain":"https://doi.org/10.1007/s10529-023-03437-0","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2023/10/24 0:00:00","PubModel":"Epub","JCR":"Q3","JCRName":"BIOTECHNOLOGY & APPLIED MICROBIOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
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.
期刊介绍:
Biotechnology Letters is the world’s leading rapid-publication primary journal dedicated to biotechnology as a whole – that is to topics relating to actual or potential applications of biological reactions affected by microbial, plant or animal cells and biocatalysts derived from them.
All relevant aspects of molecular biology, genetics and cell biochemistry, of process and reactor design, of pre- and post-treatment steps, and of manufacturing or service operations are therefore included.
Contributions from industrial and academic laboratories are equally welcome. We also welcome contributions covering biotechnological aspects of regenerative medicine and biomaterials and also cancer biotechnology. Criteria for the acceptance of papers relate to our aim of publishing useful and informative results that will be of value to other workers in related fields.
The emphasis is very much on novelty and immediacy in order to justify rapid publication of authors’ results. It should be noted, however, that we do not normally publish papers (but this is not absolute) that deal with unidentified consortia of microorganisms (e.g. as in activated sludge) as these results may not be easily reproducible in other laboratories.
Papers describing the isolation and identification of microorganisms are not regarded as appropriate but such information can be appended as supporting information to a paper. Papers dealing with simple process development are usually considered to lack sufficient novelty or interest to warrant publication.