Abstract
THE glycosidic link can, theoretically, be hydrolysed by two alternative routes, proceeding with the fission of the bond between (a) the anomeric carbon atom and the glycosidic oxygen or (b) the aglycon group and the glycosidic oxygen. For a number of glycosides the mechanism of the acidic and/or enzymatic hydrolysis has been investigated1–8. Since it became possible to prepare highly purified glucamylase it was interesting to investigate the cleavage point when this enzyme acts on maltose.
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