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