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Purification of Alpha-Amylase Isoenzymes From Scytalidium Thermophilum on a Fluidized Bed of Alginate Beads Followed by Concanavalin A-agarose Column Chromatography

Purification of Alpha-Amylase Isoenzymes From Scytalidium Thermophilum on a Fluidized Bed of Alginate Beads Followed by Concanavalin A-agarose Column Chromatography

I Roy, M S Sastry, B N Johri, M N Gupta

Protein Expr Purif. 2000 Nov;20(2):162-8.

PMID: 11049740

Abstract:

An alpha-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 degrees 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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42411045	Protein A-Agarose macrobeads			Price

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