{"title":"PURIFICATION AND PARTIAL CHARACTERISATION OF AN ANTIFUNGAL BACTERIOCIN FROM Bacillus sp. Sh10 ASSOCIATED WITH MARINE CARPET CLAM (Paphia textile)","authors":"F. Shayesteh, Asmat Ahmad, G. Usup","doi":"10.15414/JMBFS.2513","DOIUrl":null,"url":null,"abstract":"This study was conducted to purify and characterize an anti- C. albicans bacteriocin produced by Bacillus sp. Sh10 isolated from marine carpet clam, Paphia textile. Extracellularly produced bacteriocin was purified by 80 % ammonium sulfate precipitation and size exclusive gel chromatography using superdex-200 column chromatographyThe purification steps resulted in 3.68-fold increase in specific activity and recovery of 20.66 % of total activity. The purity rate and molecular mass of 11 KDa of this compound were determined using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Profile analysis of this bacteriocin by electrospray mass spectrometry (LC/MS/MS) showed 43% protein sequence coverage with a putative uncharacterized protein from Bacillus cereus strain B4264.","PeriodicalId":22746,"journal":{"name":"The Journal of Microbiology, Biotechnology and Food Sciences","volume":"18 1","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2021-04-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"3","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"The Journal of Microbiology, Biotechnology and Food Sciences","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.15414/JMBFS.2513","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 3
Abstract
This study was conducted to purify and characterize an anti- C. albicans bacteriocin produced by Bacillus sp. Sh10 isolated from marine carpet clam, Paphia textile. Extracellularly produced bacteriocin was purified by 80 % ammonium sulfate precipitation and size exclusive gel chromatography using superdex-200 column chromatographyThe purification steps resulted in 3.68-fold increase in specific activity and recovery of 20.66 % of total activity. The purity rate and molecular mass of 11 KDa of this compound were determined using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Profile analysis of this bacteriocin by electrospray mass spectrometry (LC/MS/MS) showed 43% protein sequence coverage with a putative uncharacterized protein from Bacillus cereus strain B4264.
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