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α -glucosidase (EC: 3.2.1.20) was isolated from Penicillum chrysogenum . The enzyme was enhanced by plant growth regulators such as gibberellic acid (GA 3 ), benzylaminopurine (BAP) and kinetin. Dansyl chloride inhibited the enzyme at 1, 2, 3, 4 and 5 mM with T 0.5 67, 52.2, 34.4 and 23.3 min, respectively. The substrate offered partial protection for the enzyme against dansyl chloride inhibition. The enzyme was activated by Ca 2+ and Mg 2+ . However, Pb 2+ , Cd 2+ , Zn 2+ , Ni 2+ and Hg 2+ inhibited α -glucosidase activity. The enzyme was immobilized on Ca alginate and the optimal concentration for 3% w/v. The optimal concentration of CaCl 2 was recorded at 3 mM. The optimal CaCl 2 concentration and the optimum time for immobilization was 3mM and 4hr. The enzyme was inhibited by aqueous extracts of Datura stramonium, Trigonella foenum-graecum, Hyoscymus muticus and Cynodon dactylon . The IC 50 values for the four extracts were 59.1, 73.6, 68.5 and 77.1 µg ml -1 , respectively.

Induction, immobilization, modification and natural inhibitors of α-glucosidase from Penicillum chrysogenum