Purification and characterization of a small size protease from Bacillus sp. APR-4.

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dc.contributor.authorKumar, Den_US
dc.contributor.authorBhalla, T Cen_US
dc.date.accessioned2009-05-28T13:23:14Z
dc.date.available2009-05-28T13:23:14Z
dc.date.issued2004-05-06en_US
dc.description.abstractA thermostable extracellular protease of Bacillus sp. APR-4 was purified by size-exclusion and ion-exchange chromatographic methods and its properties were studied. The purified enzyme had a specific activity of 21,000 U/mg of protein and gave single band on SDS/PAGE with a molecular mass of 16.9 KDa. This protease had an optimal pH of 9 and exhibited its highest activity at 60 degrees C. The enzyme activity was inhibited by EDTA, suggesting the presence of metal residue at the active site. Ca2+ (5 mM) had stabilising effect on the activity of protease, but Cu2+ (5 mM) had inhibitory effect. The enzyme exhibited highest specificity towards casein (1%) and had a Km of 26.3 mg/ml and a Vmax of 47.6 U/mg with casein as a substrate. The stability of this enzyme was evaluated in the presence of some organic solvents and the enzyme was stable in methanol, petroleum ether and ethanol. Detergents (Wheel, Farishta) had stimulatory effect on the activity of this enzyme.en_US
dc.description.affiliationDepartment of Biotechnology, Himachal Pradesh University, Summer Hill, Shimla 171 005, India.en_US
dc.identifier.citationKumar D, Bhalla TC. Purification and characterization of a small size protease from Bacillus sp. APR-4. Indian Journal of Experimental Biology. 2004 May; 42(5): 515-21en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/59341
dc.language.isoengen_US
dc.source.urihttps://www.niscair.res.in/ScienceCommunication/ResearchJournals/rejour/ijeb/ijeb0.aspen_US
dc.subject.meshAlkanes --chemistryen_US
dc.subject.meshBacillus --enzymologyen_US
dc.subject.meshBinding Sitesen_US
dc.subject.meshCalcium --chemistryen_US
dc.subject.meshCaseins --chemistryen_US
dc.subject.meshChromatography, Gelen_US
dc.subject.meshChromatography, Ion Exchangeen_US
dc.subject.meshDetergents --pharmacologyen_US
dc.subject.meshElectrophoresis, Polyacrylamide Gelen_US
dc.subject.meshEndopeptidases --chemistryen_US
dc.subject.meshEthanol --chemistryen_US
dc.subject.meshHydrogen-Ion Concentrationen_US
dc.subject.meshKineticsen_US
dc.subject.meshMagnesium --metabolismen_US
dc.subject.meshMethanol --chemistryen_US
dc.subject.meshProteins --chemistryen_US
dc.subject.meshSolvents --chemistryen_US
dc.subject.meshSubstrate Specificityen_US
dc.subject.meshTemperatureen_US
dc.titlePurification and characterization of a small size protease from Bacillus sp. APR-4.en_US
dc.typeJournal Articleen_US
dc.typeResearch Support, Non-U.S. Gov'ten_US
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