An endoglycosidase from grape berry skin of Cv. M. Alexandria hydrolyzing potentially aromatic disaccharide glycosides
1998
Gunata, Z. | Blondeel, C. | Vallier, M.J. | Lepoutre, J.P. | Sapis, J.C. | Watanabe, N.
We present evidence on the presence of an endoglycosidase in grape skins able to split the heterosidic linkage of disaccharide glycosides, releasing disaccharide and aglycon. Its extraction from grape skins (cv. Muscat of Alexandria) was possible with the use of a detergent (poly(ethylene glycol)). The enzyme was purified about 1000-fold successively by chromatography on DEAE Sepharose CL 6B, CM 20 Poros, and Protein-Pak SW 300. The optimum pH and temperature activity were found to be similar to levels reported for other plant glycosidases. K(m) and V(max) values for pNP-beta-rutinoside were 1.69 mM and 275 nkat/mg, respectively, with a molecular mass of 58000. The enzyme was quite tolerant to glucose inhibition (K(i) = 212 mM). Hydrolysis of monoterpenyl and 2-phenylethyl glycosides (arabinofuranosyl-, rhamnopyranosyl-, apiofuranosylglucosides) from grape and arabinopyranosyl- and xylopyranosylglucosides from other plants yielded the corresponding disaccharides and aglycons. The identity of the released sugars was confirmed by GC-EIMS/GC-NCIMS analysis of trifluoroacetylated derivatives.
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