ISSN: 0973-7510

E-ISSN: 2581-690X

Open Access

Fahad A. Al-Dhabaan

Department of Biology, Science and Humanities College, Alquwayiyah, Shaqra University, Saudi Arabia.
J Pure Appl Microbiol. 2017;11(1):119-126
https://doi.org/10.22207/JPAM.12.1.15 | © The Author(s). 2018
Received: 25/02/2018 | Accepted: 02/03/2018 | Published: 31/03/2018
Abstract

The activity of a-glucosidase enzyme (EC 3.2.1.20) was inhibited by 40.3% by an extracellular inhibitory protein which isolated from the culture filtrate of Aspergillus brasiliensis ATCC-16404. The maximum activity of this protein and fungal mycelial dry weight were obtained at 28°C, 7 days, 6.5, 400 µl/ml, 140 rpm, and rice straw as the optimum incubation temperature, incubation period, pH value, inoculum size, agitation speed, and raw material respectively. The a-glucosidase inhibitory protein (AGIP) was purified and separated electrically as a single band at 40 KDa. There 17 amino acids of the purified protein were determined at different concentrations, where threonine has a highest percentage (90%) and aspartic acid has a lower percentage (24%). Kinetics of AGIP were determined, where Vmax, Km, kcat, and catalytic activity values were exactly calculated using Lineweaver-Burk plot compared with those of acarbose as an inhibitor standard. The maximum catalytic activity (7.808 M-1S-1) at 0.1 mg/mol was higher than that of acarbose (7.783 M-1S-1) at the same concentration.

Keywords

Antidiabetics, diabetes mellitus, enzyme kinetics, protein purification.

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