{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T23:46:20Z","timestamp":1790725580176,"version":"4.1.0"},"reference-count":53,"publisher":"Wiley","issue":"12","license":[{"start":{"date-parts":[[2016,6,23]],"date-time":"2016-06-23T00:00:00Z","timestamp":1466640000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J. Basic Microbiol."],"published-print":{"date-parts":[[2016,12]]},"abstract":"<jats:sec><jats:label\/><jats:p>Present study underlines an unusual non\u2010cumbersome\u2010powerful strategy for purification of SHG10 keratinolytic alkaline protease from <jats:italic>Bacillus licheniformis<\/jats:italic> SHG10 DSM 28096 with robust stability properties. The enzyme was impressively purified to homogeneity with specific activity, purification fold, and yield of 613.82\u2009U\u2009mg<jats:sup>\u22121<\/jats:sup>, 58.91 and 99%, respectively, via a sequential two\u2010step purification strategy: precipitation with 65% (NH<jats:sub>4<\/jats:sub>)<jats:sub>2<\/jats:sub>SO<jats:sub>4<\/jats:sub> and flow through fractions of DEAE\u2010cellulose DE 53 column. SDS\u2013PAGE conferred a monomeric enzyme with a molecular mass of 30.4\u2009kDa. The enzyme demonstrated optimal activity at pH (10.0\u201311.0) and at 65\u2009\u00b0C. It exhibited full stability at pH (6.0\u201311.0) over 38\u2009h at 4\u2009\u00b0C and at 65\u2009\u00b0C for 15\u2009min. Remarkable enhanced enzyme activity (130.15 and 126.37%) was retained in presence of commercial laundry detergents Oxi and Ariel after 1\u2009h, respectively. Organic solvent stability of the enzyme was verified in butanol, ether, acetonitrile, isopropanol, and chloroform. Imposingly, full storage stability (100%) of the enzyme along 1 year in \u221220\u2009\u00b0C was confirmed. <jats:italic>K<\/jats:italic><jats:sub>m<\/jats:sub><jats:italic>\u2013V<\/jats:italic><jats:sub>max<\/jats:sub> was 0.00174 mM\u2010534.2\u2009mM\u2009Sub\u2009\u00b7\u2009min<jats:sup>\u22121<\/jats:sup>\u2009\u00b7\u2009mg\u2009protein<jats:sup>\u22121<\/jats:sup> and 1.266\u2009mg\u201028.89\u2009mg\u2009Sub\u2009\u00b7\u2009h<jats:sup>\u22121<\/jats:sup>\u2009\u00b7\u2009mg\u2009protein<jats:sup>\u22121<\/jats:sup> on N\u2010Suc\u2010Ala\u2010Ala\u2010Pro\u2010Phe\u2010<jats:italic>p<\/jats:italic>NA and keratin azure, respectively. Robust stability properties of SHG10 keratinolytic alkaline protease along with rapid\u2010efficient purification underpin its potential commercialization for industrial exploitation.<\/jats:p><\/jats:sec>","DOI":"10.1002\/jobm.201600073","type":"journal-article","created":{"date-parts":[[2016,6,24]],"date-time":"2016-06-24T10:53:28Z","timestamp":1466765608000},"page":"1317-1330","source":"Crossref","is-referenced-by-count":4,"title":["SHG10 keratinolytic alkaline protease from <i>Bacillus licheniformis<\/i> SHG10 DSM 28096: Robust stability and unusual non\u2010cumbersome purification"],"prefix":"10.1002","volume":"56","author":[{"given":"Amira M.","family":"Embaby","sequence":"first","affiliation":[{"name":"Department of Biotechnology, Institute of Graduate Studies and Research Alexandria University Egypt"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hesham","family":"Saeed","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, Institute of Graduate Studies and Research Alexandria University Egypt"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ahmed","family":"Hussein","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, Institute of Graduate Studies and Research Alexandria University Egypt"},{"name":"Department of Chemistry and Biochemistry Texas Tech University Lubbock Texas USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2016,6,23]]},"reference":[{"key":"e_1_2_6_2_1","doi-asserted-by":"publisher","DOI":"10.1590\/S1517-83822001000100002"},{"key":"e_1_2_6_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0960-8524(97)00182-X"},{"key":"e_1_2_6_4_1","first-page":"1","article-title":"Purification and characterization of detergent stable alkaline protease from Bacillus amyloliquefaciens SP1 isolated from apple rhizosphere","volume":"55","author":"Guleria S.","year":"2015","journal-title":"J. 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