Okochi, “Properties of endoglucanase of Penicillium chrysogemumPCL501,”Australian

Abstract

Abstract: Crude extracellular enzyme from a 3-day culture of Penicillium chrysogenum (PCL 501), in basal medium containing cellulose as the sole carbon source, yielded 0.67 ± 0.03, 19.94 ± 1.30 and 8.50 ± 0.50 units mg protein of 1, 4-â-endoglucanase, â-glucosidase and xylanase activity -1 respectively. The crude enzyme was subjected to ammonium sulphate precipitation (80% saturation) and gel filtration. A purification-fold of 7.5 was achieved. Two active fractions of 1, 4 â-endoglucanase (EC 3. 2. 1. 4), which exhibited about the same activity towards carboxymethylcellulose (CMC), were obtained and pooled for the subsequent analyses. The endoglucanase gave a Vmax of 10.0 ± 0.4 µmol min mg protein and Km of 11.8 ± 0.4 gL with CMC. The enzyme was Zn , Hg and EDTA inhibited the enzyme activity. The effect of Ca was not significant. Over 3- fold increase in the enzyme activity was recorded with Mn . Percentage inhibition of 65.9 and 79.7 2+ respectively was obtained with Hg and EDTA. The organism appears to produce two types of 2+ endoglucanase which differed in their molecular weight but not significantly in their activity. The enzyme activity was highly stimulated by manganese ion and inhibited by the metal-chelating agent, EDTA