{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T06:35:43Z","timestamp":1790058943459,"version":"4.0.1"},"reference-count":67,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2022,4,25]],"date-time":"2022-04-25T00:00:00Z","timestamp":1650844800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001503","name":"Indian Council of Agricultural Research","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001503","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Microbiol."],"abstract":"<jats:p>Microbial keratinases exhibit a momentous role in converting keratin biowastes into exceedingly valuable protein supplements. This study reports a novel, highly stable keratinase from<jats:italic>Bacillus pacificus<\/jats:italic>RSA27 for the production of pure peptides rich in essential amino acids from chicken feathers. Purified keratinase showed a specific activity of 38.73 U\/mg, 2.58-fold purification, and molecular weight of 36 kDa. Kinetic studies using a chicken feather as substrate report<jats:italic>K<\/jats:italic><jats:sub>m<\/jats:sub>and<jats:italic>V<\/jats:italic><jats:sub>max<\/jats:sub>values of 5.69 mg\/ml and 142.40 \u03bcg\/ml\/min, respectively, suggesting significant enzyme-substrate affinity\/biocatalysis. Identification and<jats:italic>in silico<\/jats:italic>structural-functional analysis of keratinase discovered the presence of distinct amino acid residues and their positions. Besides, keratinase possesses a high-affinity calcium-binding site (Asp<jats:sup>128<\/jats:sup>, Leu<jats:sup>162<\/jats:sup>, Asn<jats:sup>164<\/jats:sup>, Ile<jats:sup>166<\/jats:sup>, and Val<jats:sup>168<\/jats:sup>) and a catalytic triad of Asp<jats:sup>119<\/jats:sup>, His<jats:sup>151<\/jats:sup>, and Ser<jats:sup>308<\/jats:sup>, known attributes of serine protease (subtilisin family). Furthermore, a scale-up to 5 L fermenter revealed complete feather hydrolysis (94.5%) within 24 h with high activity (789 U\/ml) and total amino acid of 153.97 \u03bcmol\/ml. Finally, cytotoxicity evaluation of protein hydrolysate resulted in negligible cytotoxic effects (1.02%) on the mammalian hepatoblastoma cell line, signifying its potential biotechnological applications.<\/jats:p>","DOI":"10.3389\/fmicb.2022.882902","type":"journal-article","created":{"date-parts":[[2022,4,25]],"date-time":"2022-04-25T12:50:11Z","timestamp":1650891011000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":41,"title":["Chicken Feather Waste Valorization Into Nutritive Protein Hydrolysate: Role of Novel Thermostable Keratinase From Bacillus pacificus RSA27"],"prefix":"10.3389","volume":"13","author":[{"given":"Chhavi","family":"Sharma","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Svetlana","family":"Timorshina","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexander","family":"Osmolovskiy","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jyoti","family":"Misri","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rajni","family":"Singh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2022,4,25]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","first-page":"93","DOI":"10.3390\/microorganisms10010093","article-title":"Novel feather degrading keratinases from Bacillus cereus group: biochemical, genetic and bioinformatics analysis","volume":"10","author":"Almahasheer","year":"2022","journal-title":"Microorganisms"},{"key":"B2","doi-asserted-by":"publisher","first-page":"214","DOI":"10.1016\/j.pep.2013.01.007","article-title":"Purification and characterization of an extracellular keratinolytic protease from a new isolate of Aspergillus parasiticus","volume":"88","author":"Anitha","year":"2013","journal-title":"Protein Expr. 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