Partial Purification and Characterization of Thermostable, Alkaline and Chelator-resistant Protease from a Newly Isolated Bacillus sp. CY7 and its potential applications in various industries

Journal of Applied Biological Sciences

Yelis MAAŞOĞLU¹  Burhan ARIKAN¹  Nihan ARABACI¹  Yasemin CAF¹ 

关键词: Alkali-Aggregate Reaction;    Inhibitor;    Slag;    Silica Fume;    Test Concrete Siliceous;    Silica;   

DOI  :  

学科分类：生物科学（综合）

来源: Nobel Bilim ve Arasirma Merkezi/Nobel Science and Research Cente

【 摘 要 】

AthermophilealkalineproteaseproducingBacillussp.strainsisolatedfromsoilsamples.Enzymesynthesisoccurredattemperaturesbetween20ºCand60ºCwithanoptimumof55°CandbetweenthepHrangeof6.0-13.0withanoptimumpHof10.0onskimmilkagarplates.AnalysesofmolecularmassofthepartiallypurifiedenzymewascarriedoutbySDS-PAGEwhichrevealedtwobandsas112and97kDa.Theenzymewasactiveinabroadtemperaturerangebetween30ºCand100ºC,withanoptimumat70ºC,andmaximumactivitywasatpH11.0.Theenzymealsopresentedthealkaline-stablepropertieswitharemainingactivityaround94%,atpH6.0-13.0for24h,at55°C.Theenzymeactivitywashighlystablebetween30-100°Cwitharemainingactivity91%,afterpre-incubationfor1h.EnzymewasexposuredtovariousNaClconcentrations(3-30%),andthehighestresidualactivitywasdeterminedinthepresenceof3%NaCl(87%).Whileafterbeingexposedwithβ-mercaptoethanol(1%),PMSF(3mM),Tween20(0.1%),Tween80(0.1%),SDS(1%),TritonX100(1%),H2O2(1%),MnCl2(5mM),CaCl2(5mM),BaCl2(5mM),MgCl(5mM),FeCl2(5mM)andEDTA(5mM),theenzymeexhibitedthefollowingactivities105%,101%,107%,119%,72%,99%,98%,98%,99%,98%,97%,97%,96%and99%,respectively.Accordingtotheseresults,CY7proteaseshowsthermostable,highalkaline,alkali-stableandchelatorresistantproperties.Owingtoitsmentionedpropertiesthisproteaseisanidealchoiceforapplicationindetergentformulations,leatherandtextileindustries.

【 授权许可】

Unknown