Please use this identifier to cite or link to this item: http://ir.juit.ac.in:8080/jspui/jspui/handle/123456789/10264
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dc.contributor.authorV., Sreeraj-
dc.contributor.authorNadda, Ashok Kumar [Guided by]-
dc.date.accessioned2023-10-30T04:34:33Z-
dc.date.available2023-10-30T04:34:33Z-
dc.date.issued2022-
dc.identifier.urihttp://ir.juit.ac.in:8080/jspui/jspui/handle/123456789/10264-
dc.descriptionEnrollment No. 207833en_US
dc.description.abstractEsterases (EC 3.1.1.x) are a family of hydrolases that catalyze the synthesis and breakdown of ester bonds. They're found in a wide range of sources including animals, plants, and microbes, and many of them have a wide range of substrate tolerance, implying that they developed to have access to carbon sources or to participate in the catabolic process. Esterases are one of the most commonly utilised biocatalysts since they don't require cofactors, are usually quite stable, and can even function in organic solvents. Esterase activity is often checked using either chromophoric compounds (e.g. p-nitro phenyl esters) or tributyrin-supplemented agar plates. (Bornscheuer ,2002 ) and the activity can be measured in terms of amount of enzyme that releases 1 μmol of p-nitro phenol from a p-nitrophenyl ester per minute (Sood et al., 2016).en_US
dc.language.isoen_USen_US
dc.publisherJaypee University of Information Technology, Solan, H.P.en_US
dc.subjectEsteraseen_US
dc.subjectBacterial strainen_US
dc.subjectPolyurethaneen_US
dc.subjectTributyrinen_US
dc.titleProduction and Characterization of Esterase Producing Bacterial Strainen_US
dc.typeDissertationen_US
Appears in Collections:Dissertations (M.Sc.)

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