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Please use this identifier to cite or link to this item: http://hdl.handle.net/2074/1355

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contributor.authorRoy, Ipsita-
contributor.authorSharma, Aparna-
contributor.authorGupta, Munishwar N-
date.accessioned2006-02-21T04:47:06Z-
date.available2006-02-21T04:47:06Z-
date.issued2004-
identifier.citationBioorganic & Medicinal Chemistry Letters, 14(4), 887-889en
identifier.urihttp://eprint.iitd.ac.in/dspace/handle/2074/1355-
description.abstractThree phase partitioning (protein precipitate obtained as an interfacial layer between lower aqueous and upper t-butanol phases, formed by the addition of ammonium sulphate and t-butanol to the aqueous solution of protein) followed by lyophilization in the presence of two-component excipient resulted in 400–480× increases in transesterification activity of lyophilized powders of subtilisin Carlsberg, depending on the solvent. The three phase partitioned enzyme, ‘dried’ by washing with butanol, gave 3–4× higher rates (depending on the solvent used) than the enzyme preparation dried by lyophilization in the presence of two-component excipient system.en
format.extent136679 bytes-
format.mimetypeapplication/pdf-
language.isoenen
subjectCryoprotectanten
subjectLyoprotectanten
subjectSubtilisin Carlsbergen
subjectThree phase partitioningen
subjectTransesterificationen
titleObtaining higher transesterification rates with subtilisin carlsberg in nonaqueous mediaen
typeArticleen
Appears in Collections:Chemistry

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