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A fibrin degrading serine metallo protease of Bacillus circulans with α-chain specificity

Yogesh, Devaraj. and Halami, P. M. (2015) A fibrin degrading serine metallo protease of Bacillus circulans with α-chain specificity. Food Bioscience, 11. pp. 72-78.

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The additionofa fibrinolytic enzymefrom Bacillus to afoodsystemcontributestoits functionality andmayhelpinpreventiveprophylaxisofthrombosis-relateddisorders.In the presentstudy,a fibrinolyticserine-metalloproteasewithsubstratespecificity was identified andpartiallypurified from Bacillus circulans CFR11. Theenzymewasactive toward α-chain moietyofhuman fibrinandAα and Bβ chains of fibrinogen andwastermed as CFR11-protease.Withthespecific activityof1399.57U/mgofprotein,maximumactivity of enzymewasobservedatpH7.4andtemperatureof50 1C. DivalentcationsMg2þ and Mn2þ were foundtoenhanceproteaseactivitybutitwasinhibitedbyphenylemethyl sulphonyl fluoride (PMSF)andethylenediaminetetraaceticacid(EDTA).Fromthedata obtained, theenzymehadanapparentmolecularweightof190kDaasperSDS-PAGE analysis andzymography.The in-vitro Activated PartialThromboplastinTime(APTT)and Prothrombin Time(PT)valuesshowednosignificant differenceinbothdoseandtime- dependent assay,inferringthesaferpropertyoftheCFR11enzymeforthrombolytic purpose. FromtheseresultsitcanbeconcludedthatanewenzymeCFR11protease, isolated withspecificity towards α-chain moietyof fibrin, canbecomeaneffective fibrin specific agentforthesafeprophylaxisofthrombosis.

Item Type: Article
Uncontrolled Keywords: Bacillus circulans Fibrino(geno)lytic activity α-Chain Serine-metallo protease Zymogram Thrombolytic
Subjects: 500 Natural Sciences and Mathematics > 07 Life Sciences > 04 Microbiology
600 Technology > 08 Food technology > 16 Nutritive value > 05 Enzymes
Divisions: Food Microbiology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 28 Nov 2016 06:36
Last Modified: 28 Nov 2016 06:36
URI: http://ir.cftri.res.in/id/eprint/12571

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