Purification and some properties of exo-1,4-beta-glucanase from Chaetomium olivaceum.
Exo-1,4-beta-glucanase (E.C. 3.2.1.91) was successively purified by precipitation with acetone, followed by gel filtration on Sephadex G-100 and chromatographed onto DEAE-cellulose. A typical procedure provided 47.14 fold purification with 72.8% yield. The molecular mass of the purified enzyme was found to be 88 kDa by SDS-PAGE. The pH optimum of the enzyme was 5.2 and maximum activity was obtained at 45 degrees C. Km value against alpha-cellulose was 0.65 mg mL(-1). Alpha-cellulose and filter paper were the best substrates for enzyme activity. Enzyme was activated by Mn2+ and Fe3+, inactivated by Cu2+ and completely inhibited by Hg2+ and Ag+.
El-Gindy
A A
AA
Dept. of Biological Sciences, Fac. of Education, Cairo, Egypt.
Saad
R R
RR
Fawzi
E
E
D002480:Cellulase / Q000302:isolation & purification* / Q000378:metabolism; D002482:Cellulose / Q000378:metabolism; D002597:Chaetomium / Q000201:enzymology*; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight
D002482:Cellulose; D002480:Cellulase