Open AccessPurification and Characterization of Endoglucanase from local isolate of Aspergillus flavus
Author(s) -
Baghdad Science Journal
Publication year - 2013
Publication title -
mağallaẗ baġdād li-l-ʿulūm
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.167
H-Index - 6
eISSN - 2411-7986
pISSN - 2078-8665
DOI - 10.21123/bsj.10.3.844-853
Subject(s) - size exclusion chromatography , aspergillus flavus , chromatography , chemistry , enzyme assay , enzyme , ammonium sulfate precipitation , cellulase , specific activity , ammonium , yield (engineering) , incubation , ion chromatography , precipitation , sephadex , biochemistry , food science , organic chemistry , materials science , physics , meteorology , metallurgy
Endoglucanase produced from Aspergillus flavus was purified by several steps including precipitation with 25 % ammonium sulphate followed by Ion –exchange chromatography, the obtained specific activity was 377.35 U/ mg protein, with a yield of 51.32 % .This step was followed by gel filtration chromatography (Sepharose -6B), when a value of specific activity was 400 U/ mg protein, with a yield of 48 %. Certain properties of this purified enzyme were investigated, the optimum pH of activity was 7 and the pH of its stability was 4.5, while the temperature stability was 40 °C for 60 min. The enzyme retained 100% of its original activity after incubation at 40 °C for 60 min; the optimum temperature for enzyme activity was 40 °C.