Activators and Inhibitors of α-glucosidase from Penicillium chrysogenum
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Date
2018-02
Journal Title
Journal ISSN
Volume Title
Publisher
Science Domain International
Abstract
α-glucosidase (EC: 3.2.1.20) from Penicillium chrysogenum Thom ATCC 10106 was induced by GSH at the lower concentrations. H2O2 was inhibitor at all tested concentrations and the IC50 was 92.2%v/v. AMP, ADP and ATP enhanced the activity revealing that α-glucosidase is endothermic enzyme. The chelating agents are ethylenediaminetetraacetate (EDTA), α-α-dipyridyl and o-phenanthroline inhibited the enzyme. IC50 for these three compounds were 7.1, 10.2 and 10.9 mM, respectively. The highest activity of α-glucosidase was recorded at 150 mM phosphate buffer. Mannitol as polyol protected the enzyme against heat inactivation. The five sugars trehalose, lactose, raffinose, glucose and sucrose protected α-glucosidase against thermo-inactivation at 60ºC. Also, sarcosine as a product of glycine provided α-glucosidase with appreciable thermostability at 60ºC.
Description
Keywords
P chrysogenum, glutathione, adenosine compounds, chelating agents, trehalose, mannitol
Citation
El-Shora Hamed M., Ibrahim Mohsen E., Alfakharany Mohammad W.. Activators and Inhibitors of α-glucosidase from Penicillium chrysogenum. Annual Research & Review in Biology. 2018 Feb; 24(1): 1-9