A fibrin degrading serine metallo protease of Bacillus circulans with α-chain specificity
IR@CFTRI: CSIR-Central Food Technological Research Institute, Mysore
View Archive Info| Field | Value | |
| Relation |
http://ir.cftri.com/12571/
http://dx.doi.org/10.1016/j.fbio.2015.04.007 |
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| Title |
A fibrin degrading serine metallo protease
of Bacillus circulans with α-chain specificity
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| Creator |
Yogesh, Devaraj.
Halami, P. M. |
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| Subject |
04 Microbiology
05 Enzymes |
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| Description |
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.
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| Date |
2015
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| Type |
Article
PeerReviewed |
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| Format |
application/pdf
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| Language |
en
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| Rights |
—
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| Identifier |
http://ir.cftri.com/12571/1/Food%20Bioscience%2011%20%282015%29%2072%E2%80%9378.pdf
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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