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Please use this identifier to cite or link to this item: http://eprint.iitd.ac.in/handle/2074/965

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dc.contributor.authorRoy, Ipsita-
dc.contributor.authorSastry, M S R-
dc.contributor.authorJohri, B N-
dc.contributor.authorGupta, Munishwar N-
dc.identifier.citationProtein Expression and Purification, 20(2), 162–168en
dc.description.abstractAn a-amylase has been purified from the thermophilic fungus Scytalidium hermophilum. A ninefold purification was achieved in a single step using fluidized bed chromatography wherein alginate was used as the affinity matrix. There are at least two isoenzymes as shown by concanavalin A (Con A)–agarose column chromatography. The isoenzyme binding to Con A is stable for at least 3 h at 80°C in the presence of calcium ions. The isoenzymes have similar molecular weights of around 45,000 Da as shown by SDS PAGE analysis. The isoenzymes differ only slightly in their pH optima and temperature optima but the isoenzyme binding to Con A–agarose has slightly higher thermal stability.en
dc.format.extent1678122 bytes-
dc.subjectfluidized beden
dc.subjectalginate beadsen
dc.subjects. thermophilumen
dc.subjectthermostable enzymes.en
dc.titlePurification of a-amylase isoenzymes from scytalidium thermophilum on a fluidized bed of alginate beads followed by concanavalin a-agarose column chromatographyen
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