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Alpha -Glucosidase and glucoamylase






Nippon Nogeikagaku Kaishi 69(8): 1050-1054

Alpha -Glucosidase and glucoamylase

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.


Accession: 002549278



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