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THE CHROMATOGRAPHIC PROPERTIES OF BARLEY AND MALT β‐AMYLASES
Author(s) -
LaBerge D. E.,
Meredith W. O. S.
Publication year - 1969
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.2050-0416.1969.tb03177.x
Subject(s) - amylase , enzyme , germination , chemistry , hordeum vulgare , chromatography , biochemistry , food science , biology , botany , poaceae
Barley β‐amlyase occurs as a heterogeneous, polydisperse enzyme in thiol‐free extracts of Conquest barley. During malting, the polydisperse enzyme is altered, resulting in the formation of four distinct enzyme components which increase in activity as germination progresses. Addition of thioglycerol to a thiol‐free extract of barley, or initial extraction with thioglycerol, produces extracts containing two discrete β‐amylase enzymes. β‐amylase I is the major component of the extract; β‐amylase II occurs as a minor component. Similarly, malt extracts containing thioglycerol have two β‐amylase enzymes, β‐amylase III and IV. Barley β‐amylase II and malt β‐amylase III have similar chromatographic properties on CM‐cellulose but it is not known whether these enzymes are identical. During the early stages of germination, barley β‐amylase I disappears and cannot be detected in extracts of 1‐day malt; β‐amylase III is the major β‐amylase enzyme in this extract. Malt β‐amylase IV cannot be detected in barley extracts. It develops during germination until it becomes the major β‐amylase in malt extracts.

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