Please use this identifier to cite or link to this item: http://nopr.niscpr.res.in/handle/123456789/50511
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dc.contributor.authorGupta, Pritesh-
dc.contributor.authorNipunta-
dc.contributor.authorDutt, Kakoli-
dc.contributor.authorSaran, Saurabh-
dc.contributor.authorSaxena, Rajendra Kumar-
dc.date.accessioned2019-09-18T06:19:51Z-
dc.date.available2019-09-18T06:19:51Z-
dc.date.issued2019-10-
dc.identifier.issn0975-0959 (Online); 0301-1208 (Print)-
dc.identifier.urihttp://nopr.niscair.res.in/handle/123456789/50511-
dc.description358-362en_US
dc.description.abstractWe report binary immobilization of Thermomyces lanuginosus lipase enzyme using chitosan as the support. This method of enzyme immobilization is better than cross-linked enzyme aggregate (CLEA) in terms of better enzyme recovery and separation. This method of immobilization resulted in an increase in the thermostability of the binary immobilized lipase as against the crude free enzyme. This preparation could be used for nearly 15 consecutive cycles with 80-100% efficiency. Reusability of the immobilized enzyme makes it an economical alternative to the traditional way. Immobilized lipases in particular are a modern catalytic tool for various industrially significant reactions and applications.en_US
dc.language.isoen_USen_US
dc.publisherNISCAIR-CSIR, Indiaen_US
dc.rights CC Attribution-Noncommercial-No Derivative Works 2.5 Indiaen_US
dc.sourceIJBB Vol.56(5) [October 2019]en_US
dc.subjectBinaryen_US
dc.subjectChitosanen_US
dc.subjectImmobilizationen_US
dc.subjectReusabilityen_US
dc.subjectThermomyces lanuginosus lipaseen_US
dc.subjectThermostabilityen_US
dc.titleBinary immobilization: a newer approach for immobilizing lipase from a thermophilic sp. of Thermomyces lanuginosusen_US
dc.typeArticleen_US
Appears in Collections:IJBB Vol.56(5) [October 2019]

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