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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.

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.

journal_name

Protein Expr Purif

journal_title

Protein expression and purification

authors

Roy I,Sastry MS,Johri BN,Gupta MN

doi

10.1006/prep.2000.1308

keywords:

subject

Has Abstract

pub_date

2000-11-01 00:00:00

pages

162-8

issue

2

eissn

1046-5928

issn

1096-0279

pii

S1046-5928(00)91308-1

journal_volume

20

pub_type

杂志文章

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