Biochemical Characterization of a Thiol-Activated, Oxidation Stable Keratinase from Bacillus pumilus KS12英文文献资料.docVIP

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Biochemical Characterization of a Thiol-Activated, Oxidation Stable Keratinase from Bacillus pumilus KS12英文文献资料.doc

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Biochemical Characterization of a Thiol-Activated, Oxidation Stable Keratinase from Bacillus pumilus KS12英文文献资料

SAGE-HindawiAccesstoResearch EnzymeResearch Volume2010,ArticleID132148,7pages doi:10.4061/2010/132148 ResearchArticle BiochemicalCharacterizationofaThiol-Activated, OxidationStableKeratinasefromBacilluspumilusKS12 RinkyRajput,RichaSharma,andRaniGupta DepartmentofMicrobiology,UniversityofDelhi,SouthCampus,NewDelhi110021,India CorrespondenceshouldbeaddressedtoRaniGupta,ranigupta15@redi? Received23January2010;Accepted16June2010 AcademicEditor:RobertoFernandezLafuente Copyright?2010RinkyRajputetal.ThisisanopenaccessarticledistributedundertheCreativeCommonsAttributionLicense, whichpermitsunrestricteduse,distribution,andreproductioninanymedium,providedtheoriginalworkisproperlycited. AnextracellularkeratinasefromBacilluspumilusKS12waspuri?edbyDEAEionexchangechromatography.Itwasa45kDa monomerasdeterminedbySDSPAGEanalysis.Itwasfoundtobeanalkaline,serineproteasewithpHandtemperatureoptima ? of10and60 C,respectively.Itwasthiolactivatedwithtwo-andeight-foldenhancementinpresenceof10mMDTTandβ- mercaptoethanol, respectively. In addition, its activity was stimulated in the presence of various surfactants, detergents, and oxidizingagentswhereanearly2-to3-foldenhancementwasobservedinpresenceofH2O2andNaHClO3.Ithydrolyzedbroad rangeofcomplexsubstratesincludingfeatherkeratin,haemoglobin,?brin,casein,andα-keratin.Analysisofamidolyticactivity revealedthatite?cientlycleavedphenylalanine → leucine → alanine-p-nitroanilides.ItalsocleavedinsulinBchainbetween Val -Asn ,Leu -Cys7andHis -Leu residues. 11 2 3 6 10 1.Introduction and protein engineering [5, 6]. Thus, keratinases with robustcharacteristicslikeoxidationstability,alkalinestabil- ity,detergentcompatibility,andtemperaturetolerancecan fetch a good market among detergent proteases. Here we reportthedetailedcharacterizationofadetergentcompatible and oxidation stable keratinase from Bacillus pumilus KS 12. Keratinases[3.4.21/24/99.11]areproducedbyalargenum- ber of bacteria, actinomycetes, and fungi, with unique ability to act on “ha