Beta-glycosidase system of sunflowers. Isolation of enzyme and study of their substrate specificity

The beta-glucosidase, beta-galactosidase, beta-xylosidase and alpha-L-arabinosidase activities of a partially purified preparation from sunflower seeds were studied by chromatography, polyacrylamide gel electrophoresis and isoelectrofocusing. beta-Glucosidase was isolated as two fractions with high...

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Bibliographic Details
Published in:	Biokhimiia (Moscow, Russia) Vol. 45; no. 12; p. 2158
Main Authors:	Zhdanov, Iu A, Kessler, R M, Kolokolova, N S, Beletskiĭ, Iu D, Sherstnev, K B
Format:	Journal Article
Language:	Russian
Published:	Russia (Federation) 01-12-1980
Subjects:	Glycoside Hydrolases - isolation & purification Glycoside Hydrolases - metabolism Helianthus - enzymology Kinetics Molecular Weight Plants - enzymology Substrate Specificity
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Summary:	The beta-glucosidase, beta-galactosidase, beta-xylosidase and alpha-L-arabinosidase activities of a partially purified preparation from sunflower seeds were studied by chromatography, polyacrylamide gel electrophoresis and isoelectrofocusing. beta-Glucosidase was isolated as two fractions with high molecular weights. One form of beta-glucosidase does not possess strict specificity to stereochemistry of hexosides C-4 and C-6 and pentosides C-5, whereas the second form exhibits a narrow specificity for C-4 and is low specific towards substituents of C-5. The sunflower seeds also contain acid beta-galactosidase, which possesses a narrow specificity and is not coupled with the beta-glucosidase activity. The molecular weight of beta-galactosidase is 62000.
ISSN:	0320-9725