Avicel cellobiose from

Figure 7. Production of glucose and cellobiose from Avicel. The reaction mixture contained 1% Avicel PH-101, 1% Trichoderma reesei QM 9123 cellulose protein produced in a pH 3.6 culture medium, and 0.05M sodium acetate buffer, pH 5.0. Incubation conditions and analysis are...

In 1972 Ogawa and Toyama (56) purified three components— A-I-a, A-I-b, and A-II-1—which were adsorbed on a gauze column during purification from Cellulase Onozuka P1500, a commercial preparation of T. viride cellulase. These three components had molecular weights of 32,000, 48,000, and 48,000 as determined by gel filtration and contained 7-16% carbohydrate. Each is reported to carry out the random hydrolysis of CM-cellulose and to degrade hydrocellulose (Avicel) and cellooligosaccharides except for cellobiose. The order of reactivity toward either cotton or Avicel was A-II-1 > A-I-b > A-I-a. The proteins adsorbed on cellulose comprised 38% of the total cellulase protein. 

None of the six enzymes cleaved cellobiose, but in comparing the products released from swollen Avicel by hydrocellulase C with those from cellulodextrin by the Cellulases, further evidence of contamination of cellulases II and III was found. For the latter cases both glucose and cellobiose are produced whereas both hydrocellulase C and Cellulase IV yield predominantly cellobiose. Cellulase IV produced much more cellobiose than glucose from cellotetraose whereas the other Cellulases yielded only slightly more cellobiose than glucose. 

Purification and Physical and Chemical Properties. Extracellular cellulase components A and B and cell-bound cellulase component C were purified through the steps summarized in Figure 7 from the cultures of Ps. fluorescens on 0.5% Avicel and on 0.5% cellobiose, respectively. The purified cellulase components (Cellulases A, B, and C) thus obtained showed a single peak in zone electrophoresis on cellulose acetate film and starch bed. 

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