Cellobiose inducer, 8-glucosidase

The principal features of a mathematical model described for the enzymatic hydrolysis and fermentation of cellulose by Trichoderma reesei are the assumption of two forms of cellulose (crystalline and amorphous), two sugars (cellobiose and D-glucose), and two enzymes (cellulase and j3-D-glucosidase). An inducer-repressor-messenger RNA mechanism is used to predict enzyme formation, and pH effects are included. The model consists of 12 ordinary differential equations for 12 state variables and contains 38 parameters. The parameters were estimated from four sets of experimental data by optimization. The results appear satisfactory, and the computer programs permit simulation of a variety of system changes. 

Cellobiose or cellulose were necessary to induce the production of fS-D-glucosidase activity by Sporotrichum pulverulentum. Purification via preparative slab gel isoelectric focusing and affinity chromatography on a phenyl derivative of agarose gave five active fractions (p/ s 4.5—5.2, mol. wts. 1.65—1.82 X 10 by sodium dodecyl sulphate-polyacrylamide gel electrophoresis). 

Streptomyces granaticolor after induction with different inducers arbutin (lane 1), methyl-3-D-glucosidase (lane 2), cellobiose (lane 3), salicin (lane 4), cellobiose + glycerol (lanes 5,6) -the protein band which exhibit the 3-D-glucosidase activity was partially purified by elution from preparative polyacrylamide gel. White bands at the right side of each lane indicate the position of -D-glucosidase activity. 

When Arbutin, MeG, Cellobiose and Salicin served as inducers, the 3-D-glucosidase activity (PNPG used as substrate) was localized in the cytoplasm and in the periplasm. With CMC and MC as inducers the enzyme activity was found mostly in medium. The enzyme(s) formed after induction with different inducers possess the same electrophoretic mobility in the 7,5% polyacrylamide gel. The possibility that the enzymic activities are... 

Table 1. The Effect of Different Inducers (Cellobiose, CMC and MC) on the Synthesis and Localization of 3-D-glucosidase Activity. 

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