The maximum production of cellulose enzymes (FPactivity, CMcellulase and P-glucosidase) in the culture filtrate was observed a t 27°C and pH 5.0, except for P-glucosidase, being a t 6.0. The levels of extracellular enzymes in shake and stationary culture conditions was almost equal although they reached their maxima earlier in the former. The distribution of the three enzymes in extracellular, cytosol and cell debris fractions revealed most of the mactivity and CMcellulase occurring extracellulary. More than 50% of the 13-glucosidase was present in the cell debris fraction.
1986. Partial purification, characterization and regulation of celluloytic enzymes from Trichoderma longibrachiaturn. Journal of' Applied Bacteriology 61, 73-80. A net purification of 9.46-, 18.6and 16.7-fold for filter paper (FP) hydrolytic activity, carboxymethyl (CM) celiulase and P-glucosidase, respectively was achieved through ion exchange and gel chromatographies. The purified enzyme preparation showed an optimal pH of 5.0 for CM cellulase and 5.5 for the other two components. The enzyme activities increased up to 60"-6:j"C for the three enzyme components and they were stable at 30" or 40°C and pH 4.5 to 5.0 after 2&30 min treatment. The four enzyme components, that is, two F P activities (unadsorbed and adsorbed), a CM cellulase and a ,B-glucosidase, had K, values of 47.6 mg, 33.3 mg, 4.0 mg and 0.18 mmol/l with V, ,, of 4, 1.28, 66.5 and 1.28 units per mg protein. The molecular weights as determined with SDS-PAGE were found to be 44000, 38 000, 55 000 and 63 OOO for the above four enzyme components in the same sequence. A distinct type of synergistic action was observed between these components by their action on dewaxed cotton. Glycerol at 1 % strongly repressed the formation of all the cellulolytic enzymes. The role of proteolytic enzymes in in uitro inactivation of cellulases was not apparent.
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