Abstract
The extracellular enzyme cyclodextrin gluconotransferase (CGTase, EC 2.4.1.19) was produced by Bacillus macerans ATCC 8244 at optimized conditions. The CGTase activity was found to be 495 μg β-CD/(ml min). The enzyme was partially purified by 40–60% ammonium sulfate precipitation. The enzyme was immobilized by sodium alginate beads and kinetic studies were performed. The enzymatic activity of both free and immobilized CGTase was highest at temperature 60 °C and pH 7.5. The analysis of kinetic parameters K m and V max was obtained by the action of CGTase on the starch with respect to β-CD. The enzyme exhibits substrate inhibition and the values are 10 and 5.5 μg starch/ml for free and immobilized enzyme, respectively. The effect of salt concentration on enzyme activity was studied and it was found that Cu 2+, Fe 2+, Zn 2+, Co 2+, Mg 2+ and Hg 2+ were inhibitory, however Ca 2+ showed a relative increase in enzyme activity. The immobilization of the enzyme showed a high operational stability by retaining almost 75% of the initial activity after seventh use.
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