Lignocellulose represents a considerable challenge to enzymatic hydrolysis on account of its heterogeneous composition and physical structure evolved to resist degradation. Its main component, cellulose, is composed of long, unbranched glucose polymers packed onto each other to form highly insoluble crystals. To meet the challenge of crystalline cellulose degradation, potent cellulolytic organisms, including Trichoderma, produce complex mixtures of enzymes all required for efficient solubilization of the substrate. Studies of the cellulolytic enzyme systems of Trichoderma species have a long history (for comprehensive coverage see BCguin and Aubert, 1994; Knowles et al., 1987; Montenecourt, 1983; Nevalainen and Penttilii, 1995; Reese et al., 1950; Teeri, 1997; Wood and McCrae, 1979; Wood and GarciaCampayo, 1990), and today T . reesei is probably the most extensively studied cellulolytic organism. Its many different cellulolytic enzymes are efficiently secreted into the culture medium and they act synergistically to bring about complete solubilization of the highly crystalline native cellulose (Fagerstam and Pettersson, 1980; Henrissat et al., 1985; Irwin et al., 1993; Medve et al., 1994; Nidetzky et al., 1993, 1994a; Wood and McCrae, 1972,1979).
|Title of host publication||Trichoderma and Gliocladium|
|Editors||Gary E. Harman, C.P. Kubicek|
|Place of Publication||LondonBristol|
|Publisher||Taylor & Francis|
|Publication status||Published - 1998|
|MoE publication type||A3 Part of a book or another research book|
Koivula, A., Linder, M., & Teeri, T. (1998). Structure-function relationships in Trichoderma cellulolytic enzymes. In G. E. Harman, & C. P. Kubicek (Eds.), Trichoderma and Gliocladium (Vol. 2, pp. 3-23). Taylor & Francis.