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Alpha -Glucosidase and glucoamylase


, : Alpha -Glucosidase and glucoamylase. Nippon Nogeikagaku Kaishi 69(8): 1050-1054

The conformationally different actions of alpha -glucosidase and glucoamylase on a glycosidic linkage are considered, kinetic indices against 7 substrates (maltose to maltoheptaose and starch) are tabulated for Paecilomyces varioti glucoamylase and Aspergillus niger alpha -glucosidase, and subsite affinities of these enzymes are indicated; functions and structure-activity relationships of these and certain other amylase-family enzymes from other microorganisms are discussed, e.g. amino acid sequences in 4 molecular regions of 3 alpha -amylases and 4 alpha -glucosidases, and the splitting of glycosides via the formation of oxocarbonium ions or beta -carboxyacetals.

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Related references

Schumacher, D.; Hirsch, D.; Caemmerer, B.; Kroh, L.W., 1996: Studies on the degradation of Maillard-products by amylolytic enzymes: 3. Inhibition of glucoamylase, alpha-amylase and alpha-glucosidase by heat-treated alpha-glucans and melanoidines. Amylolytic enzymes are only slightly inhibited by thermal treated alpha-glucans (10-15%). The addition of glycine to the thermolysis mixture produces no increase of the inhibition. The inhibition of the enzyme activity is probably caused by short-...

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