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dc.contributor.authorSharma, Aparna
dc.contributor.authorMondal, Kalyani
dc.contributor.authorGupta, Munishwar Nath
dc.date.accessioned2006-01-19T06:19:47Z
dc.date.accessioned2019-02-10T14:24:05Z
dc.date.accessioned2019-02-11T06:18:03Z
dc.date.available2006-01-19T06:19:47Z
dc.date.available2019-02-10T14:24:05Z
dc.date.available2019-02-11T06:18:03Z
dc.date.issued2003
dc.identifier.citationJournal of Chromatography A, 995(1-2), 127-134en
dc.identifier.urihttp://localhost:8080/iit/handle/2074/1188
dc.description.abstractPectinase and cellulase were separated from a commercial enzyme preparation called Pectinex Ultra SP-L. This was carried out using a process called macroaffinity ligand-facilitated three-phase partitioning (MLFTPP). In this method, a water-soluble polymer is floated as an interfacial precipitate by adding ammonium sulfate and tert.-butanol. The polymer (appropriately chosen) in the presence of an enzyme for which it shows affinity, selectively binds to the enzyme and floats as a polymer–enzyme complex. In the first step, pectinase was purified (with alginate as the polymer) 13-fold with 96% activity recovery. In the second MLFTPP step, using chitosan, cellulase was purified 16-fold with 92% activity recovery. Both preparations showed a single band on sodium dodecylsulfate–polyacrylamide gel electrophoresis. This illustrative example shows that the strategy of sequential MLFTPP can be used to separate important biological activities from a crude brothen
dc.format.extent296056 bytes
dc.format.mimetypeapplication/pdf
dc.language.isoenen
dc.subjectEnzymesen
dc.subjectPectinaseen
dc.subjectCellulaseen
dc.titleSeparation of enzymes by sequential macroaffinity ligand-facilitated three-phase partitioningen
dc.typeArticleen


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