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Amylase generally known as an industrial enzyme that hydrolyzes starch and glycogen. The α-amylase hydrolyzes α-1,4 glycosidic linkage that acts on raw starch. This reaction is very important for direct starch processing for alcohol fermentation and functional oligosaccharide or food additives development. Amyl III gene was isolated from  Aspergillus awamori  KT-11 and inserted into  p DONR 201 as entry clone. The recombinant construct was subcloned into  p DEST 17 plasmid as the expression vector and into  E. coli  BL21AI cells. The objective of this study was to optimize induction temperatures in the expression process and to know the ability of recombinant Amyl III to hydrolyze raw starch. The expression study of Amyl III was performed using LB medium at 27°C and 37°C. Purification was done using affinity chromatography (His Tag) with 100 mM imidazole. Protein analysis was done using 7.5% of SDS-PAGE gel. Digestion on soluble starch and raw waxy maize starch by Amyl III was performed using TLC plate. The results show that the best protein expression was obtained by incubation at 27°C. Digestion on those starch by using recombinant Amyl III resulted in the production of malto-tetraose, -pentaose, -hexaose and -heptaose.

Expression of gene encoding raw starch digesting α -amylase (Amyl III) inEscherichia coli