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

Abstract

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
Chapter1
Pages3-23
Volume2
ISBN (Electronic)978-0-429-07964-1
Publication statusPublished - 1998
MoE publication typeA3 Part of a book or another research book

Fingerprint

Trichoderma
structure-activity relationships
cellulose
solubilization
enzymes
lignocellulose
degradation
organisms
enzymatic hydrolysis
crystals
polymers
culture media
history
glucose

Cite this

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). LondonBristol: Taylor & Francis.
Koivula, Anu ; Linder, Markus ; Teeri, Tuula. / Structure-function relationships in Trichoderma cellulolytic enzymes. Trichoderma and Gliocladium. editor / Gary E. Harman ; C.P. Kubicek. Vol. 2 LondonBristol : Taylor & Francis, 1998. pp. 3-23
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Koivula, A, Linder, M & Teeri, T 1998, Structure-function relationships in Trichoderma cellulolytic enzymes. in GE Harman & CP Kubicek (eds), Trichoderma and Gliocladium. vol. 2, Taylor & Francis, LondonBristol, pp. 3-23.

Structure-function relationships in Trichoderma cellulolytic enzymes. / Koivula, Anu; Linder, Markus; Teeri, Tuula.

Trichoderma and Gliocladium. ed. / Gary E. Harman; C.P. Kubicek. Vol. 2 LondonBristol : Taylor & Francis, 1998. p. 3-23.

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

TY - CHAP

T1 - Structure-function relationships in Trichoderma cellulolytic enzymes

AU - Koivula, Anu

AU - Linder, Markus

AU - Teeri, Tuula

PY - 1998

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N2 - 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).

AB - 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).

M3 - Chapter or book article

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BT - Trichoderma and Gliocladium

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Koivula A, Linder M, Teeri T. Structure-function relationships in Trichoderma cellulolytic enzymes. In Harman GE, Kubicek CP, editors, Trichoderma and Gliocladium. Vol. 2. LondonBristol: Taylor & Francis. 1998. p. 3-23