Isolation and Purification of Quercetin 2,3-dioxygenase from Aspergillus Flavus via Lectin Affinity Chromatography
نویسندگان
چکیده
Quercetinase is an enzyme excreted by the mold, Aspergillus flavus when grown on rutin. Characterization of the enzyme involves first isolating and purifying the enzyme from media in which A. flavus has been grown. Improved techniques for this isolation are presented using methods including lectin affinity chromatography and capillary electrophoresis. A pure sample of quercetinase has been obtained and found to have K m = 3.5 x 10M.
منابع مشابه
Enzymatic characteristics of quercetinases from some indigenous Aspergillus flavus strains.
Five indigenous Aspergillus flavus strains MTCC-2206, 1884, 1883, 1783 and 2456 were screened for the secretion of quercetinase. Fungal strains MTCC-2206, 1884, 1883, and 1783 were found to secrete the quercetinase in the range of 0.24-0.36 enzyme unit/mL of the culture medium, while MTCC-2456 secreted only 0.04 enzyme unit/mL. The enzymatic characteristics of quercetinase were determined. The ...
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