Enzymatic Depilation of Animal Hide Identification of Elastase (LasB) from Pseudomonas aeruginosa MCM B-327 as a Depilating Protease 英文参考文献.docVIP

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Enzymatic Depilation of Animal Hide Identification of Elastase (LasB) from Pseudomonas aeruginosa MCM B-327 as a Depilating Protease 英文参考文献.doc

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Enzymatic Depilation of Animal Hide Identification of Elastase (LasB) from Pseudomonas aeruginosa MCM B-327 as a Depilating Protease 英文参考文献

EnzymaticDepilationofAnimalHide:Identificationof Elastase(LasB)fromPseudomonasaeruginosaMCMB- 327asaDepilatingProtease EmmanuelVijayPaulPandeeti1,GopiKrishnaPitchika1,JyotsnaJotshi2,SmitaS.Nilegaonkar2, PradnyaP.Kanekar2,DayanandaSiddavattam1* 1Department of Animal Sciences, School of Life Sciences, University of Hyderabad, Hyderabad, Andhra Pradesh, India, 2Microbial Sciences Division, MACS-Agharkar ResearchInstitute,Pune,Maharashtra,India Abstract Conventionalleatherprocessinginvolvingdepilationofanimalhidebylimeandsulphidetreatmentgeneratesconsiderable amounts of chemical waste causing severe environmental pollution. Enzymatic depilation is an environmentally friendly processandhasbeenconsideredtobeaviablealternativetothechemicaldepilationprocess.Weisolatedanextracellular proteasefromPseudomonasaeruginosastrainMCMB-327withhighdepilationactivityusingbuffalohideasasubstrate. This 33kDa protease generated a peptide mass fingerprint and de novo sequence that matched perfectly with LasB (elastase),ofPseudomonasaeruginosa.InsupportofthisdataalasBmutantofMCMB-327strainlackeddepilatoryactivity and failed to produce LasB. LasB heterologously over-produced and purified from Escherichia coli also exhibited high depilatingactivity.Moreover,reintroductionofthelasBgenetotheP.aeruginosalasBmutantviaaknock-instrategyalso successfullyrestoreddepilationactivitythusconfirmingtheroleofLasBasthedepilatingenzyme. Citation:PandeetiEVP,PitchikaGK,JotshiJ,NilegaonkarSS,KanekarPP,etal.(2011)EnzymaticDepilationofAnimalHide:IdentificationofElastase(LasB)from PseudomonasaeruginosaMCMB-327asaDepilatingProtease.PLoSONE6(2):e16742.doi:10.1371/journal.pone.0016742 Editor:LeonardoSechi,UniversitadiSassari,Italy ReceivedNovember29,2010;AcceptedDecember29,2010;PublishedFebruary11,2011 Copyright: ? 2011 Pandeeti et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricteduse,distribution,andreproductioninanymedium,provide