Abstract
The enzymic hydrolysis of glycosyl fluorides is conveniently followed by using a pH-stat. Reactions involving glucosyl or galactosyl fluorides can also be followed by using glucose oxidase or galactose oxidase respectively. The pH-stat allows the rapid assay of intestinal α-glucosidase in crude homogenates. Use of glycosyl fluorides as substrates for glycosidases facilitates the polarimetric or g.l.c. determination of the anomeric nature of the initial product of hydrolysis. Hydrolysis by fungal amyloglucosidase proceeds with inversion of configuration whereas that by yeast and rat intestinal α-glucosidase, coffee-bean α-galactosidase and almond emulsin β-glucosidase proceeds with retention of configuration. β-d-Glucopyranosyl azide was not a detectable substrate for almond emulsin β-d-glucosidase.
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Selected References
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