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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Abstract
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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