Stabilization of a raw-starch-digesting amylase by multipoint covalent attachment on glutaraldehyde-activated amberlite beads

Journal of Microbiology and Biotechnology
Tochukwu N NwaguHideki Aoyagi

Abstract

Raw-starch-digesting enzyme (RSDA) was immobilized on Amberlite beads by conjugation of glutaraldehyde/ polyglutaraldehyde (PG)-activated beads or by crosslinking. The effect of immobilization on enzyme stability and catalytic efficiency was evaluated. Immobilization conditions greatly influenced the immobilization efficiency. Optimum pH values shifted from pH 5 to 6 for spontaneous crosslinking and sequential crosslinking, to pH 6-8 for RSDA covalently attached on polyglutaraldehyde-activated Amberlite beads, and to pH 7 for RSDA on glutaraldehyde-activated Amberlite. RSDA on glutaraldehyde-activated Amberlite beads had no loss of activity after 2 h storage at pH 9; enzyme on PG-activated beads lost 9%, whereas soluble enzyme lost 65% of its initial activity. Soluble enzyme lost 50% initial activity after 3 h incubation at 60 degrees C, whereas glutaraldehyde-activated derivative lost only 7.7% initial activity. RSDA derivatives retained over 90% activity after 10 batch reuse at 40 degrees C. The apparent Km of the enzyme reduced from 0.35 mg/ml to 0.32 mg/ml for RSDA on glutaraldehyde-activated RSDA but increased to 0.42 mg/ml for the PG-activated RSDA derivative. Covalent immobilization on glutaraldehyde Amberlite beads was ...Continue Reading

Citations

Oct 30, 2020·International Journal of Biological Macromolecules·Chika Jude Ugwuodo, Tochukwu Nwamaka Nwagu
Nov 7, 2020·Probiotics and Antimicrobial Proteins·Chika Jude UgwuodoChukwudi Ogbonnaya Onwosi

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