Separation and characterization of endoglucanases from culture filtrates of Cellulomonas sp

Six major components exhibiting endo-1,4-\-d-glucanase activity were partially purified from culture filtrates of a newly isolated Cellulomonas sp. using ion-exchange chromatography. Molecular weights (44,000 to 140,000), pH optima (6.0 to 7.0), temperature optima (40 to 50°C), half-life, energy of activation, Kmand other kinetic parameter investigations indicate the existence of 6 different endoglucanases. Further support for this assumption comes from inhibition studies, whereby glucose inhibited the enzyme activities between 15 and 50% at a concentration of 0.034% (1.65 mM) and cellobiose between 0 and 50% at a concentration of 0.1% (2.92 mM). Of all the metals (Hg2+, Co2+, Cu2+, Ca2+, Mg2+, Zn2+, Fe3+) tested, only Hg2+ exhibited a 55% inhibition at 5.0 mM.