The role of carbohydrate binding module (CBM) at high substrate consistency: Comparison of Trichoderma reesei and Thermoascus aurantiacus Cel7A (CBHI) and Cel5A (EGII)

Costaouëc, Tinaïg Le; Pakarinen, Annukka; Várnai, Anikó; Puranen, Terhi; Viikari, Liisa

doi:10.1016/j.biortech.2013.05.079

Cited by 60 publications

(45 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The same conclusion has been reached previously by Viikari and co-workers (56 -58), who studied a number of systems and conditions including lignocellulosic substrates and long term experiments with significant conversion. These workers concluded that the increased probability of enzymes to find the substrate at high loads would compensate for the lower affinity of one-domain enzymes (56). This argument is along the lines of Le Chatelier's principle, which stipulates a shift toward the adsorbed form at high loads, and the results in Table 1 are compatible with this.…”

Section: Discussionsupporting

confidence: 80%

Temperature Effects on Kinetic Parameters and Substrate Affinity of Cel7A Cellobiohydrolases

Sørensen

Cruys-Bagger

Windahl

et al. 2015

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: Temperature concomitantly modulates kinetic and adsorption properties in heterogeneous enzyme catalysis. Results: Affinity-activity relationships for four Cel7A cellobiohydrolases are characterized over a broad temperature interval. Conclusion: Cellobiohydrolases are strongly activated by temperature at high, but not at low, substrate loads. Significance: Fundamental insight into cellulolytic mechanisms at high (industrially relevant) temperatures is gained.

show abstract

Section: Discussionsupporting

confidence: 80%

Temperature Effects on Kinetic Parameters and Substrate Affinity of Cel7A Cellobiohydrolases

Sørensen

Cruys-Bagger

Windahl

et al. 2015

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Lignin acts as a physical barrier that restricts the access of hydrolytic enzymes to cellulose and hemicellulose components of the plant cell wall. Moreover, it has been shown that cellulases have a tendency to bind lignin in a nonreversible manner (48)(49)(50)(51), thus limiting their availability in solution. Thermochemical pretreatment processes that are used for removal of the lignin component before cellulose degradation tend to be expensive, slow, and relatively inefficient.…”

Section: Discussionmentioning

confidence: 99%

Toward combined delignification and saccharification of wheat straw by a laccase-containing designer cellulosome

Davidi

Moraïs

Artzi

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Efficient breakdown of lignocellulose polymers into simple molecules is a key technological bottleneck limiting the production of plant-derived biofuels and chemicals. In nature, plant biomass degradation is achieved by the action of a wide range of microbial enzymes. In aerobic microorganisms, these enzymes are secreted as discrete elements in contrast to certain anaerobic bacteria, where they are assembled into large multienzyme complexes termed cellulosomes. These complexes allow for very efficient hydrolysis of cellulose and hemicellulose due to the spatial proximity of synergistically acting enzymes and to the limited diffusion of the enzymes and their products. Recently, designer cellulosomes have been developed to incorporate foreign enzymatic activities in cellulosomes so as to enhance lignocellulose hydrolysis further. In this study, we complemented a cellulosome active on cellulose and hemicellulose by addition of an enzyme active on lignin. To do so, we designed a dockerin-fused variant of a recently characterized laccase from the aerobic bacterium Thermobifida fusca. The resultant chimera exhibited activity levels similar to the wild-type enzyme and properly integrated into the designer cellulosome. The resulting complex yielded a twofold increase in the amount of reducing sugars released from wheat straw compared with the same system lacking the laccase. The unorthodox use of aerobic enzymes in designer cellulosome machinery effects simultaneous degradation of the three major components of the plant cell wall (cellulose, hemicellulose, and lignin), paving the way for more efficient lignocellulose conversion into soluble sugars en route to alternative fuels production.

show abstract

“…Várnai et al (2013) reported that a 10% substrate concentration led to an increase of glucose yield in comparison with a 1% substrate concentration when using cellulase core enzyme for hydrolysis of lignocellulose. Similarly, Le Costaouec et al (2013) demonstrated that the high substrate consistency resulted in higher hydrolysis yield when using cellulase hydrolysis of Avicel.…”

Section: Pulp Viscosity and Fock Reactivitymentioning

confidence: 95%

“…Várnai et al (2013) observed that increasing the substrate concentration during the enzymatic hydrolysis can increase the enzyme adsorption, thus improving the hydrolysis efficiency when studying the enzymatic hydrolysis of lignocellulose. Similarly, Le Costaouec et al (2013) found the increased cellulase adsorption onto Avicel at 20% Avicel concentration than at 10% Avicel concentration.…”

Section: Introductionmentioning

confidence: 92%

High consistency cellulase treatment of hardwood prehydrolysis kraft based dissolving pulp

Wang

Liu

Yang

et al. 2015

Bioresource Technology

View full text Add to dashboard Cite

The role of carbohydrate binding module (CBM) at high substrate consistency: Comparison of Trichoderma reesei and Thermoascus aurantiacus Cel7A (CBHI) and Cel5A (EGII)

Cited by 60 publications

References 34 publications

Temperature Effects on Kinetic Parameters and Substrate Affinity of Cel7A Cellobiohydrolases

Temperature Effects on Kinetic Parameters and Substrate Affinity of Cel7A Cellobiohydrolases

Toward combined delignification and saccharification of wheat straw by a laccase-containing designer cellulosome

High consistency cellulase treatment of hardwood prehydrolysis kraft based dissolving pulp

Contact Info

Product

Resources

About