Abstract
The adsorption of purified cellobiohydrolases (CBH I and II) and endoglucanases (EG I and II) from Trichoderma reesei strain L27 to microcrystalline cellulose (Avicel) has been studied. Scatchard analysis of the adsorption data indicated that Avicel possessed high– and low–affinity binding sites for the cellulase components and gave the maximum amount of each component that bound to Avicel at saturation. Hydrolysis of Avicel was thus carried out by saturating and non–saturating concentrations of purified cellulase components alone and in combination with each other. Synergism between them was greatest when Avicel was incubated with non–saturating concentrations of EG I or EG II with CBH I and CBH II. This finding could lead to a dramatic reduction in the enzyme requirement for cellulose utilization.
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References
Shoemaker, S., Watt, K., Tsitovsky, G. and Cox, R. 1983. Characterization and properties of cellulases purified from Trichoderma reesei strain L27. Bio/Technology 1:687–690.
Fägerstam, L.G. and Pettersson, L.G. 1980. The 1,4-β-glucan cello-biohydrolases of Trichoderma reesei QM 9414. A new type of cellulolytic synergism. FEES Lett. 119:97–100.
Beldman, G., Searle-Van Leewven, M.F., Rombouts, F.M. and Voragen, F.G.J. 1985. The cellulase of Trichoderma viride. Eur. J. Biochem. 146:301–308.
Chernoglazov, V.M., Ermolova, O.V. and Klësov, A.A. 1985. Production of highly purified multiple forms of endo-1,4-β-glucanases from Trichoderma viride, differing in adsorption capacity by affinity chromatography on cellulose and highly effective chromatofocusing. Biokhimiya 50:1108–1119.
Wood, T.M. 1985. Properties of cellulolytic enzyme systems. Biochem. Soc. Trans. 13:407–410.
Wood, T.M. and McCrae, S.I. 1982. Purification and some properties of the extracellular (β-D-glucosidase of the cellulolytic fungus Trichoderma koningii. J. Gen. Microbiol. 128:2973–2982.
Wood, T.M. and McCrae, S.I. 1986. The cellulase of Penicillium pinophilium. Biochem. J. 234:93–99.
Stuart, J.Y. and Ristroph, D.L. 1985. Analysis of cellulosc-cellulase adsorption data: a fundamental approach. Biotechnol. Bioeng. 27:1056–1059.
Converse, A.O. and Grethlein, H.E. 1987. On the use of an adsorption model to represent the effect of steam explosion pretreatment on the enzymatic hydrolysis of lignocellulosic substances. Enzyme Microb. Technol. 9:79–82.
Peitersen, N., Medeiros, J. and Mandels, M. 1977. Adsorption of Trichoderma cellulase on cellulose. Biotechnol. Bioeng. 19:1091–1094.
Ryu, D.D.Y., Kim, C. and Mandels, M. 1984. Competitive adsorption of cellulose components and its significance in a synergistic mechanism. Biotechnol. Bioeng. 26:488–496.
Reese, E.T. 1982. Elution of cellulase from cellulose. Process Biochem. 17:2–8.
Grethlein, H.E. 1985. The effect of pore size distribution on the rate of enzymatic hydrolysis of cellulosic substrates. Bio/Technology 3:155–160.
Klysov, A.A., Mitkevich, O.V. and Sinitsyn, A.P. 1986. Role of the activity and adsorption of cellulases in the efficiency of the enzymatic hydrolysis of amorphous and crystalline cellulose. Biochemistry 25:540–542.
Henrissat, B., Driguez, H., Viet, C. and Shuülein, M. 1985. Synergism of cellulases from Trichoderma reesei in the degradation of cellulose. Bio/Technology 3:722–726.
Rabinovich, M.L., Van Viet, N. and Klesov, A.A. 1982. Adsorption of cellulolytic enzymes on cellulose and kinetics of the action of adsorbed enzymes. Two types of interaction of the enzymes with an insoluble substrate. Biokhimiya 47:465–477.
Chanzy, H., Henrissat, B. and Vuong, R. 1984. Colloidal gold labelling of 1,4-β-D-glucan cellobiohydrolase adsorbed on cellulose substrates. FEES Lett. 172:193–197.
Woodward, J., Marquess, H.J. and Picker, C.S. 1986. Affinity chromatography of β-glucosidase and endo-β-glucanase from Aspergillus niger on concanavalin A-Sepharose: Implications for cellulase component purification and immobilization. Prep. Biochem. 16:337–352.
Segel, I.H. 1975. Enzyme Kinetics. John Wiley, New York.
Woodward, J. and Arnold, S.A. 1981. The inhibition of β-glucosidase activity in Trichoderma reesei C30 cellulase by derivatives and isomers of glucose. Biotechnol. Bioeng. 23:1553–1562.
Miller, G.L. 1959. Use of denitrosalicyclic acid reagent for determination of reducing sugar. Anal. Chem. 31:426–428.
Bradford, M.M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248–254.
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Woodward, J., Hayes, M. & Lee, N. Hydrolysis of Cellulose by Saturating and Non–Saturating Concentrations of Cellulase: Implications for Synergism. Nat Biotechnol 6, 301–304 (1988). https://doi.org/10.1038/nbt0388-301
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DOI: https://doi.org/10.1038/nbt0388-301
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