Abstract
The major challenge faced by the biotechnological industries is the suitable source of biocatalysts. This work was aimed at sourcing for α-amylase from pearl millet. Crude α-amylase was extracted from malted pearl millet with 50 mM sodium acetate buffer pH 5.5; 70% ammonium sulphate saturation precipitated protein with highest α-amylase activity. Upon gel filtration, two major peaks were observed and the active fractions were pooled together and characterized. The optimal pH of α-amylase were 4.5 and 5.5 for peak A and B respectively. Both peaks were observed to have the same optimum temperature of 50°C. The Michealis constant (Km) and maximum velocity (Vmax) obtained from the Lineweaver-Burk plot of initial velocity at different substrate concentrations were 0.57 mg/mL and 476.19 μmol/min for peak A and 0.4 mg/mL and 250 μmol/min for peak B. Results from the kinetic parameters (Km and Vmax), optimal pH and temperature of this enzyme suggest that this enzyme could be useful in some biotechnological applications that involves starch hydrolysis such as in starchy food processing, textile industries, brewery industries, etc.
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