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ISOLATION, PURIFICATION AND ELECTROPHORETIC PROPERTIES OF AN α‐AMYLASE FROM MALTED BARLEY
Author(s) -
MacGregor A. W.
Publication year - 1977
Publication title -
journal of the institute of brewing
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.523
H-Index - 51
eISSN - 2050-0416
pISSN - 0046-9750
DOI - 10.1002/j.2050-0416.1977.tb06424.x
Subject(s) - chemistry , chromatography , amylase , electrophoresis , carboxymethyl cellulose , ion exchange , polyacrylamide gel electrophoresis , ion chromatography , extraction (chemistry) , aqueous solution , enzyme , biochemistry , ion , sodium , organic chemistry
An α‐amylase component from malted barley was isolated and purified using aqueous extraction at pH 8·0, heat treatment of the extract at 70°C, specific precipitation with glycogen and ion exchange chromatography on carboxymethyl (CM) and diethylaminoethyl (DEAE) cellulose. The enzyme preparation was shown to be pure by disc electrophoresis at pH 8·9 and iso‐electricfocusing on polyacrylamide gel in a pH 4–8 gradient.