Purification of a soluble and a wall-bound form of beta-glucosidase from Mucor racemosus.
beta-Glucosidase activity in crude extracts of Mucor racemosus exists in a soluble form and in a wall-bound form which sediments at 3,500 x g. The soluble form and a wall-bound form were purified to homogeneity by ammonium sulfate fractionation. DEAE-Sephadex chromatography, and SP-Sephadex chromatography. Both forms were identical in all parameters measured. Each enzyme is a glycoprotein of 91,000 daltons, with an identical amino acid composition and N-terminal amino acid of lysine; both contain about 10% carbohydrate. Both forms catalyze the hydrolysis of cellobiose and p-nitrophenyl-beta-D-glucoside with identical kinetic constants.
D000596:Amino Acids / Q000032:analysis; D002473:Cell Wall / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D000939:Epitopes; D005959:Glucosidases / Q000302:isolation & purification*; D005960:Glucosides / Q000378:metabolism; D008970:Molecular Weight; D009089:Mucor / Q000201:enzymology*; D013379:Substrate Specificity; D001617:beta-Glucosidase / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism
D000596:Amino Acids; D000939:Epitopes; D005960:Glucosides; D005959:Glucosidases; D001617:beta-Glucosidase