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Immobilization of α-amylase from anoxybacillus sp. SK3-4 on relizyme and immobead supports

Kahar, U. M. and Sani, M. H. and Chan, K. G. and Goh, K. M. (2016) Immobilization of α-amylase from anoxybacillus sp. SK3-4 on relizyme and immobead supports. Molecules, 21 (9). ISSN 1420-3049

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Abstract

α-Amylase from Anoxybacillus sp. SK3-4 (ASKA) is a thermostable enzyme that produces a high level of maltose from starches. A truncated ASKA (TASKA) variant with improved expression and purification efficiency was characterized in an earlier study. In this work, TASKA was purified and immobilized through covalent attachment on three epoxide (ReliZyme EP403/M, Immobead IB-150P, and Immobead IB-150A) and an amino-epoxide (ReliZyme HFA403/M) activated supports. Several parameters affecting immobilization were analyzed, including the pH, temperature, and quantity (mg) of enzyme added per gram of support. The influence of the carrier surface properties, pore sizes, and lengths of spacer arms (functional groups) on biocatalyst performances were studied. Free and immobilized TASKAs were stable at pH 6.0-9.0 and active at pH 8.0. The enzyme showed optimal activity and considerable stability at 60 ?C. Immobilized TASKA retained 50% of its initial activity after 5-12 cycles of reuse. Upon degradation of starches and amylose, only immobilized TASKA on ReliZyme HFA403/M has comparable hydrolytic ability with the free enzyme. To the best of our knowledge, this is the first report of an immobilization study of an α-amylase from Anoxybacillus spp. and the first report of α-amylase immobilization using ReliZyme and Immobeads as supports.

Item Type:Article
Uncontrolled Keywords:amylase, bacterial protein, immobilized enzyme, Anoxybacillus, chemistry, enzyme stability, enzymology, heat, pH, alpha-Amylases, Anoxybacillus, Bacterial Proteins, Enzyme Stability, Enzymes, Immobilized, Hot Temperature, Hydrogen-Ion Concentration
Subjects:Q Science > QH Natural history
Divisions:Biosciences and Medical Engineering
ID Code:72157
Deposited By: Fazli Masari
Deposited On:22 Nov 2017 20:07
Last Modified:22 Nov 2017 20:07

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