3 research outputs found
Induction, immobilization, modification and natural inhibitors of α-glucosidase from Penicillum chrysogenum
No full textα-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 T0.5 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
Purification and characterization of α-glucosidase from Penicillium chrysogenum.
No full textα-glucosidase (EC: 3.2.1.20) was isolated and purified from Penicillium chrysogenum Thom ATCC 10106 by ammonium sulphate precipitation (75%), DEAE-cellulose and Sephadex G-200. The specific activity was 140 units (U) mg-1 protein. The enzyme expressed a single band using SDS-PAGE and the molecular weight of the enzyme was nearly 43KDa. The optimal pH and temperature were 8 and 40ºC. The activation energy was 17.94 k J mol-1. The optimal incubation time was 40 min. Glutamine, glutamic acid, cysteine, alanine, phenylalanine, glycine, methionine, asparagine enhanced the enzyme activity and cysteine was the best enhancer. However, cystine and arginine inhibited α-glucosidase activity. The Vmax values were 48 and 38.1 U mg-1 protein with and without of cysteine, respectively. However, Km values were 0.21 and 0.25 mM in absence and presence of cysteine, respectively
Induction, immobilization, modification and natural inhibitors of α-glucosidase from Penicillum chrysogenum
No full textα-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 T0.5 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
