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

α-glucosidase (EC: 3.2.1.20) was isolated fromPenicillum 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 T0.567, 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+ inhibitedα-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 ofDatura 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.
Source: International Journal of Phytomedicine - Category: Science Authors: Source Type: research
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