{"title":"Impression of Insect’s Proteolytic Enzyme Cocoonase and Its Application: A Comprehensive Review","authors":"Aruna Rani, Dev Mani Pandey, Jay Prakash Pandey","doi":"10.1007/s10930-024-10246-5","DOIUrl":null,"url":null,"abstract":"<div><p>Cocoonase is a naturally secreted protease responsible for facilitating moth emergence from inside of cocoon. This protease is considered as of prime importance for all the cocooning lepidopteron. It specifically degrades sericin, the glue protein of the cocoon without damaging the fibroin and makes an escape hatch for adult emergence. Owing to this property cocoonase was characterized and explored for its prospective utilization in eco-friendly enzyme-based silk degumming. However, the applicability of cocoonase has not been explored much other than in silk degumming. Moreover, being a serine protease, and because of its similarity to trypsin, there is, tremendous potential for this enzyme to have biomedical applications, as well as numerous other uses that need to be investigated. This review article presents the comprehensive physicochemical properties of the cocoonase and its possible scope of applications in the near future.</p></div>","PeriodicalId":793,"journal":{"name":"The Protein Journal","volume":"44 1","pages":"48 - 61"},"PeriodicalIF":1.9000,"publicationDate":"2025-02-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"The Protein Journal","FirstCategoryId":"2","ListUrlMain":"https://link.springer.com/article/10.1007/s10930-024-10246-5","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
Cocoonase is a naturally secreted protease responsible for facilitating moth emergence from inside of cocoon. This protease is considered as of prime importance for all the cocooning lepidopteron. It specifically degrades sericin, the glue protein of the cocoon without damaging the fibroin and makes an escape hatch for adult emergence. Owing to this property cocoonase was characterized and explored for its prospective utilization in eco-friendly enzyme-based silk degumming. However, the applicability of cocoonase has not been explored much other than in silk degumming. Moreover, being a serine protease, and because of its similarity to trypsin, there is, tremendous potential for this enzyme to have biomedical applications, as well as numerous other uses that need to be investigated. This review article presents the comprehensive physicochemical properties of the cocoonase and its possible scope of applications in the near future.
期刊介绍：
The Protein Journal (formerly the Journal of Protein Chemistry) publishes original research work on all aspects of proteins and peptides. These include studies concerned with covalent or three-dimensional structure determination (X-ray, NMR, cryoEM, EPR/ESR, optical methods, etc.), computational aspects of protein structure and function, protein folding and misfolding, assembly, genetics, evolution, proteomics, molecular biology, protein engineering, protein nanotechnology, protein purification and analysis and peptide synthesis, as well as the elucidation and interpretation of the molecular bases of biological activities of proteins and peptides. We accept original research papers, reviews, mini-reviews, hypotheses, opinion papers, and letters to the editor.
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