Structure-function relationships in Trichoderma cellulolytic enzymes

Anu Koivula, Markus Linder, Tuula Teeri

Research output: Chapter in Book/Report/Conference proceedingChapter or book articleScientificpeer-review


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).
Original languageEnglish
Title of host publicationTrichoderma and Gliocladium
EditorsGary E. Harman, C.P. Kubicek
Place of PublicationLondonBristol
PublisherTaylor & Francis
ISBN (Electronic)978-0-429-07964-1
Publication statusPublished - 1998
MoE publication typeA3 Part of a book or another research book

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