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

Title: Purification of a-amylase isoenzymes from scytalidium thermophilum on a fluidized bed of alginate beads followed by concanavalin a-agarose column chromatography
Authors: Roy, Ipsita
Sastry, M S R
Johri, B N
Gupta, Munishwar N
Keywords: a-amylase
fluidized bed
alginate beads
s. thermophilum
thermostable enzymes.
Issue Date: 2000
Citation: Protein Expression and Purification, 20(2), 162–168
Abstract: An 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.
URI: http://eprint.iitd.ac.in/dspace/handle/2074/965
Appears in Collections:Chemistry

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