Premium
LINAMARASE: IMMOBILIZATION OF A CRUDE ENZYME
Author(s) -
NOK ANDREW J.,
EMMANUEL GIMBA C.,
ISAAC ACHOBA I.,
JAMES KAGBU A.,
BAMISAIYE ABRAHAM F.,
AKINLOYE F.
Publication year - 1992
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.1992.tb00438.x
Subject(s) - enzyme , chemistry , immobilized enzyme , hydrolysis , michaelis–menten kinetics , glucoside , chromatography , enzyme assay , biochemistry , medicine , alternative medicine , pathology
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‐ nitrophenyl β D‐ glucoside, linamarin and p‐ nitrophenyl β‐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 pK a 5.7 and pK a 6.5.