Purification of 
-Amylase Isoenzymes from Scytalidium thermophilum on a Fluidized Bed of Alginate Beads Followed by Concanavalin A–Agarose Column Chromatography
Authors: Roy I.1; Sastry M.S.R.2; Johri B.N.2; Gupta M.N.1
Source: Protein Expression and Purification, Volume 20, Number 2, November 2000 , pp. 162-168(7)
Publisher: Academic Press
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Abstract:
An -amylase has been purified from the thermophilic fungus Scytalidium thermophilum. 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. Copyright 2000 Academic Press.
Keywords:
-amylase;
fluidized bed chromatography;
alginate beads;
S. thermophilum;
thermostable enzymes
Language: English
Document Type: Research article
Affiliations: 1: Chemistry Department, Indian Institute of Technology, Hauz Khas, New Delhi, 110 016, India 2: Department of Microbiology, G. B.Pant University of Agriculture and Technology, Pantnagar, 263145, India
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