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

Abstract

α-glucosidase (EC: 3.2.1.20) was isolated from Penicillum chrysogenum. The enzyme was enhanced by plant growth regulators such as gibberellic acid (GA₃), 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 Ca²⁺ and Mg²⁺. However, Pb²⁺, Cd²⁺, Zn²⁺, Ni²⁺ and Hg²⁺ inhibited α-glucosidase activity. The enzyme was immobilized on Ca alginate and the optimal concentration for 3% w/v. The optimal concentration of CaCl₂ was recorded at 3 mM. The optimal CaCl₂ 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 IC₅₀ values for the four extracts were 59.1, 73.6, 68.5 and 77.1 µg ml^-1, respectively.