Abstract
An extracellular amylase secreted by Aspergillus niveus was purified using DEAE fractogel ion exchange chromatography and Sephacryl S-200 gel filtration. The purified protein migrated as a single band in 5% polyacrylamide gel electrophoresis (PAGE) and 10% sodium dodecyl sulfate (SDS-PAGE). The enzyme exhibited 4.5% carbohydrate content, 6.6 isoelectric point, and 60 and 52kDa molar mass estimated by SDS-PAGE and Bio-Sil-Sec-400 gel filtration column, respectively. The amylase efficiently hydrolyzed glycogen, amylose, and amylopectin. The end-products formed after 24h of starch hydrolysis, analyzed by thin layer chromatography, were maltose, maltotriose, maltotetraose, and maltopentaose, which classified the studied amylase as an α-amylase. Thermal stability of the α-amylase was improved by covalent immobilization on glyoxyl agarose (half-life of 169min, at 70°C). On the other hand, the free α-amylase showed a half-life of 20min at the same temperature. The optima of pH and temperature were 6.0 and 65°C for both free and immobilized forms.
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