Substrate specificity of sweet almond beta-glucosidase

Beta-Glucosidase, beta-galactosidase, beta-xylosidase and alpha-L-arabinosidase activities of partially purified preparation of almond emulsin were investigated using chromatography, electrophoresis in polyacrylamide gel and isoelectric focusing. Beta-Glucosidase was found to exist as two components...

Full description

Saved in:

Bibliographic Details
Published in:	Biokhimiia (Moscow, Russia) Vol. 42; no. 1; p. 26
Main Authors:	Zhdanov, Iu A, Kessler, R M, Iakubova, H R, Sherstnev, K B
Format:	Journal Article
Language:	Russian
Published:	Russia (Federation) 01-01-1977
Subjects:	Arabinose Galactosidases - metabolism Glucosidases - metabolism Glycoside Hydrolases - isolation & purification Glycoside Hydrolases - metabolism Macromolecular Substances Molecular Weight Nuts Plants - enzymology Structure-Activity Relationship Xylose
Online Access:	Get more information
Tags:	Add Tag No Tags, Be the first to tag this record!

Description
Summary:	Beta-Glucosidase, beta-galactosidase, beta-xylosidase and alpha-L-arabinosidase activities of partially purified preparation of almond emulsin were investigated using chromatography, electrophoresis in polyacrylamide gel and isoelectric focusing. Beta-Glucosidase was found to exist as two components having equal molecular weight. Aggregation of the components with inactive proteins probably results in the appearance of multiple native forms which have similar specific activities. In no case separation of the beta-glucosidase activity from the accompanied activities was achieved. It is concluded therefore that these activities are exhibited by an enzyme which is not strictly specific to the C4, C6 stereochemistry for hexosides and to that of C4, C5 for pentozides.
ISSN:	0320-9725