{"title":"Production and partial characterization of neutral protease by an indigenously isolated strain of Aspergillus tubingensis NIICC-08155","authors":"V. Morya, D. Yadav","doi":"10.5580/1b13","DOIUrl":null,"url":null,"abstract":"An indigenously isolated strain of Aspergillus tubingensis NIICC-08155 from soil of teak dominated vegetation of kusmi forest at Gorakhpur was subjected to neutral protease production and its partial characterization. The maximum production of neutral protease i.e. 68.50 U/ml was attained after 96h of incubation. The crude preparation of protease showed reasonable activity at temperature range of 40 to 60 °C with maximum activity at 40 oC and had a maximum enzyme activity at pH 6.4. The Km value of the enzyme was found to be 45.0 mg/ml and the molecular weight as determined by SDS-PAGE was approximately 45 kDa. The enzyme was completely inhibited by DTT and EDTA.","PeriodicalId":22514,"journal":{"name":"The Internet journal of microbiology","volume":"80 1","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2009-12-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"6","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"The Internet journal of microbiology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.5580/1b13","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 6
Abstract
An indigenously isolated strain of Aspergillus tubingensis NIICC-08155 from soil of teak dominated vegetation of kusmi forest at Gorakhpur was subjected to neutral protease production and its partial characterization. The maximum production of neutral protease i.e. 68.50 U/ml was attained after 96h of incubation. The crude preparation of protease showed reasonable activity at temperature range of 40 to 60 °C with maximum activity at 40 oC and had a maximum enzyme activity at pH 6.4. The Km value of the enzyme was found to be 45.0 mg/ml and the molecular weight as determined by SDS-PAGE was approximately 45 kDa. The enzyme was completely inhibited by DTT and EDTA.
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