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The action of germinated barley alpha-amylases on linear maltodextrins

✍ Scribed by Alex.W. MacGregor; Joan E. Morgan; E.Ann MacGregor

Publisher: Elsevier Science
Year: 1992
Tongue: English
Weight: 915 KB
Volume: 227
Category: Article
ISSN: 0008-6215
DOI: 10.1016/0008-6215(92)85080-j

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✦ Synopsis

The actions of barley alpha-amylase isozymes 1 and 2 (EC 3.2.1.1) on malto-oligosaccharides and theirpnitrophenyl glycosides were similar, but not identical. For each isozyme, transglycosylation occurred with small substrates that were hydrolysed with difficulty, whereas the rates of hydrolysis increased with increase in the size of the substrate for both the malto-oligosaccharides and thepnitrophenyl glycosides. A pnitrophenyl group was found to mimic a glucose residue to a large extent. The differences in action of the isozymes are believed to be caused by differences at more than one subsite of the active site. A lysine-arginine substitution is postulated to account for some of the observed variations. * Dedicated to Professor David Manners.

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