A model for the action of cereal alpha amylases on amylose
โ Scribed by Elizabeth A. MacGregor; Alex W. MacGregor
- Publisher
- Elsevier Science
- Year
- 1985
- Tongue
- English
- Weight
- 936 KB
- Volume
- 142
- Category
- Article
- ISSN
- 0008-6215
No coin nor oath required. For personal study only.
โฆ Synopsis
A model is proposed to explain the action of cereal alpha amylases (EC 3.2.1.1) on such linear substrates as amylose. It is suggested that, at the active site of the enzyme, there are nine contiguous subsites, each capable of interacting with a glucose residue. An estimate is made of the energies involved in subsite-glucose interaction, and values obtained for the binding energies are used to predict the distributions of small oligosaccharides to be expected at intermediate stages of amylose hydrolysis catalyzed by cereal alpha amylases.
๐ SIMILAR VOLUMES
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 incr
The effect of the oligosaccharide analog maltotriitol (G3OH) on the action pattern of porcine pancreatic alpha-amylase (PPA) was examined using amylose as a substrate. Fluorescence titration indicated that two molecules of G3OH can bind to one molecule of PPA. The slope in the blue value versus exte
Glucoamylase and alpha-amylase have been purified from a crude enzyme preparation of Aspergillus sp. K-27. The former was thermostable and seemed to have a "starch-binding site", judging from the results of a kinetic study, and the latter synergistically enhanced the degradation of starch granules w