Cellulose hydrolysis by the cellulases from <i>Trichoderma reesei</i>: a new model for synergistic interaction

Nidetzky, Bernd; Steiner, Walter; Hayn, Marianne; Claeyssens, Marc

doi:10.1042/bj2980705

Cited by 217 publications

(155 citation statements)

References 20 publications

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“…2C), consistent with reported results (Nidetzky et al, 1994;Woodward et al, 1988). Predicted DS also increases with increasing reaction time (Fig.…”

Section: Endoglucanase-exoglucanase Synergysupporting

confidence: 91%

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A functionally based model for hydrolysis of cellulose by fungal cellulase

Zhang

Lynd

2006

Biotechnol. Bioeng.

204

158

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A new functionally based kinetic model for enzymatic hydrolysis of pure cellulose by the Trichoderma cellulase system is presented. The model represents the actions of cellobiohydrolases I, cellobiohydrolase II, and endoglucanase I; and incorporates two measurable and physically interpretable substrate parameters: the degree of polymerization (DP) and the fraction of b-glucosidic bonds accessible to cellulase, F a (Zhang and Lynd, 2004). Initial enzyme-limited reaction rates simulated by the model are consistent with several important behaviors reported in the literature, including the effects of substrate characteristics on exoglucanase and endoglucanase activities; the degree of endo/exoglucanase synergy; the endoglucanase partition coefficient on hydrolysis rates; and enzyme loading on relative reaction rates for different substrates. This is the first cellulase kinetic model involving a single set of kinetic parameters that is successfully applied to a variety of cellulosic substrates, and the first that describes more than one behavior associated with enzymatic hydrolysis. The model has potential utility for data accommodation and design of industrial processes, structuring, testing, and extending understanding of cellulase enzyme systems when experimental date are available, and providing guidance for functional design of cellulase systems at a molecular scale. Opportunities to further refine cellulase kinetic models are discussed, including parameters that would benefit from further study.

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“…2C), consistent with reported results (Nidetzky et al, 1994;Woodward et al, 1988). Predicted DS also increases with increasing reaction time (Fig.…”

Section: Endoglucanase-exoglucanase Synergysupporting

confidence: 91%

“…2C and D). The influence on the optimal exo/endo ratio by enzyme loading is in good agreement with experimental results (Nidetzky et al, 1994).…”

Section: Endoglucanase-exoglucanase Synergysupporting

confidence: 89%

A functionally based model for hydrolysis of cellulose by fungal cellulase

Zhang

Lynd

2006

Biotechnol. Bioeng.

204

158

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“…Examples of models in this category in the literature to date are based on endoglucanase and exoglucanase. Nidetzky et al (1994b) described saturation of the hydrolysis rate in terms of the concentration of a particular cellulase component, E i , as follows:…”

Section: Semimechanistic Modelsmentioning

confidence: 99%

Toward an aggregated understanding of enzymatic hydrolysis of cellulose: Noncomplexed cellulase systems

Zhang

Lynd

2004

Biotech & Bioengineering

1,658

1,284

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Information pertaining to enzymatic hydrolysis of cellulose by noncomplexed cellulase enzyme systems is reviewed with a particular emphasis on development of aggregated understanding incorporating substrate features in addition to concentration and multiple cellulase components. Topics considered include properties of cellulose, adsorption, cellulose hydrolysis, and quantitative models. A classification scheme is proposed for quantitative models for enzymatic hydrolysis of cellulose based on the number of solubilizing activities and substrate state variables included. We suggest that it is timely to revisit and reinvigorate functional modeling of cellulose hydrolysis, and that this would be highly beneficial if not necessary in order to bring to bear the large volume of information available on cellulase components on the primary applications that motivate interest in the subject. B

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“…Cellobiohydrolase I (CBHI) is the major family C glycoprotein secreted by the filamentous fungus Trichoderma reesei, where it operates in synergy with other exo-glucanases and endo-glucanases to achieve the degradation of cellulose [1]. CBHI is typically secreted in the order of several grams/litre, and many aspects of its structure and biology are well characterised.…”

Section: Abstract : Cellobiohydrolase I; Cellulase; Fungal Glycosylatmentioning

confidence: 99%

Modified glycosylation of cellobiohydrolase I from a high cellulase‐producing mutant strain of Trichoderma reesei

Harrison¹,

Nouwens²,

Jardine³

et al. 1998

European Journal of Biochemistry

141

142

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Cellobiohydrolase I is an industrially important exocellulase secreted in high yields by the filamentous fungus Trichoderma reesei. The nature and effect of glycosylation of CBHI and other cellulolytic enzymes is largely unknown, although many other structural and mechanistic aspects of cellulolytic enzymes are well characterised. Using a combination of liquid chromatography, electrospray mass spectrometry, solidphase Edman degradation, and monosaccharide analysis we have identified every site of glycosylation of CBHI from a high cellulase-producing mutant strain of T. reesei, ALKO2877, and characterised each site in terms of its modifying carbohydrate and site-specific heterogeneity. The catalytic core domain comprises three N-linked glycans which each consist of a single N-acetylglucosamine residue. Within the glycopeptide linker domain, all eight threonines are variably glycosylated with between at least one, and up to three, mannose residues per site. All serines in this domain are at least partially glycosylated with a single mannose residue. This linker region has also been shown to be sulfated by a combination of ion chromatography and collision-induced dissociation electrospray mass spectrometry. The sulfate is probably mannose-linked. The biological significance of N-linked single N-acetylglucosamine in the catalytic core, and mannose sulfation in the linker region, is not known. Keywords : cellobiohydrolase I; cellulase; fungal glycosylation; Trichoderma; N-acetylglucosamine.Cellobiohydrolase I (CBHI) is the major family C glycoprotein secreted by the filamentous fungus Trichoderma reesei, where it operates in synergy with other exo-glucanases and endo-glucanases to achieve the degradation of cellulose [1]. CBHI is typically secreted in the order of several grams/litre, and many aspects of its structure and biology are well characterised. Like most other fungal cellulolytic enzymes characterised, CBHI conforms to a well-defined multi-domain structure, typified by a relatively large catalytic (core) domain spatially removed from a smaller cellulose-binding domain (CBD) by a highly O-glycosylated linker domain [2]. Presumably, the CBD serves as a form of anchor, and the linker a form of torsional leash, providing the catalytic region with access to a wide range of potential (and perhaps otherwise inaccessible) sites [3]. Although the catalytic domain of CBHI by itself is sufficient for cellulose binding and full catalytic activity at low enzyme to cellulose ratios, a functional CBD with sufficient spatial separation from the catalytic region is necessary for cellulolytic activity at higher enzyme-to-cellulose ratios [3]. The importance of the linker domain in maintaining spatial orientation of catalytic Correspondence to N. H. Packer,

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Cellulose hydrolysis by the cellulases from Trichoderma reesei: a new model for synergistic interaction

Cited by 217 publications

References 20 publications

A functionally based model for hydrolysis of cellulose by fungal cellulase

A functionally based model for hydrolysis of cellulose by fungal cellulase

Toward an aggregated understanding of enzymatic hydrolysis of cellulose: Noncomplexed cellulase systems

Modified glycosylation of cellobiohydrolase I from a high cellulase‐producing mutant strain of Trichoderma reesei

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