Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10235370 | Process Biochemistry | 2013 | 8 Pages |
Abstract
In this study raw starch digesting amylase (RSDA) from Aspergillus carbonarius (Bainier) Thom IMI 366159 was stabilized by covalent binding on polyglutaraldehyde (PG), glutaraldehyde (G) activated chitosan beads or post immobilization cross linking of enzyme adsorbed on chitosan. Presence of Ca2+ ions (0.5-1.5Â mM) activated the PG and G derivatives but repressed the crosslinked enzyme. Optimum pH for cross linked derivative increased by 2Â units but was unaltered for PG and G derivatives. Immobilized amylase exhibited improved thermal and storage stability. Immobilized derivatives had no loss of activity after 1Â month storage and retained above 90% activity after 10 batch reactions of 60Â min each. Immobilization successfully stabilized RSDA and immobilized enzyme from A. carbonarius can be applied in numerous industries for cheap, cost effective and environmentally friendly starch hydrolytic processes to simple sugars.
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Authors
Tochukwu Nwamaka Nwagu, Bartholomew Okolo, Hideki Aoyagi, Shigeki Yoshida,