LINAMARASE: IMMOBILIZATION OF A CRUDE ENZYME

Autor:	Abraham F. Bamisaiye, Andrew J. Nok, Gimba C. Emmanuel, Achoba I. Isaac, Kagbu A. James, F. Akinloye
Rok vydání:	1992
Předmět:	Pharmacology chemistry.chemical_classification Chromatography Linamarase Immobilized enzyme biology Biophysics Glycoside Cell Biology Linamarin Enzyme assay chemistry.chemical_compound Enzyme chemistry Biochemistry Hydrolase biology.protein Polyacrylamide gel electrophoresis Food Science
Zdroj:	Journal of Food Biochemistry. 16:109-118
ISSN:	1745-4514 0145-8884
DOI:	10.1111/j.1745-4514.1992.tb00438.x
Popis:	Linamarase from cassava cortex was immobilized on polyacrylamide gel. A crude extract of the enzyme containing most of the intracellular proteins was used for the technique to simulate the enzyme in cassava. Immobilization of the enzyme increased the Michaelis constants for all substrates when compared with the native enzyme. Both free and immobilized linamarase hydrolyzed p-nitrophenylβ D-glucoside, linamarin and p-nitrophenylβ-D-galactoside. The immobilized enzyme was more stable than the free enzyme at room temperature (25C) and 41C. Both forms gave a bell-shaped curve with maximal activity at pH 6.0; these data indicated two catalytic ionizable residues with pKa 5.7 and pKa 6.5.
Databáze:	OpenAIRE
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