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Please use this identifier to cite or link to this item: http://eprint.iitd.ac.in/handle/2074/1146

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dc.contributor.authorMondal, Kalyani-
dc.contributor.authorSharma, Aparna-
dc.contributor.authorGupta, Munishwar Nath-
dc.date.accessioned2006-01-04T13:28:19Z-
dc.date.available2006-01-04T13:28:19Z-
dc.date.issued2003-
dc.identifier.citationProtein Expression and Purification, 28(1), 190-195en
dc.identifier.urihttp://eprint.iitd.ac.in/dspace/handle/2074/1146-
dc.description.abstractStarch-degrading enzymes glucoamylase (from Aspergillus niger), and pullulanase (from Bacillus acidopullulyticus) were purified using alginates (polysaccharides consisting of mannuronic acids and guluronic acids) by a recently developed technique called macroaffinity ligand-facilitated three-phase partitioning (MLFTPP). In this process, a crude preparation of the enzyme was mixed with alginate. On addition of appropriate amounts of ammonium sulfate and t-butanol, the alginate bound enzyme appeared as an interfacial precipitate between the lower aqueous and the upper t-butanol phase. Enzyme activity from this interfacial precipitate was recovered using 1 M maltose. Glucoamylase and pullulanase were purified 20- and 38-fold with 83% and 89% activity recovery, respectively. Both the purified preparations showed a single band on SDS–PAGE.en
dc.format.extent191701 bytes-
dc.format.mimetypeapplication/pdf-
dc.language.isoenen
dc.subjectAlginatesen
dc.subjectSmart polymersen
dc.subjectGlucoamylaseen
dc.subjectPullulanaseen
dc.subjectThree-phase partitioning (TPP)en
dc.subjectMacroaffinity ligand-facilitated three-phase partitioning (MLFTPP)en
dc.titleMacroaffinity ligand-facilitated three-phase partitioning for purification of glucoamylase and pullulanase using alginateen
dc.typeArticleen
Appears in Collections:Chemistry

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