Reversibility and binding kinetics of Thermobifida fusca cellulases studied through fluorescence recovery after photobleaching microscopy

Moran‐Mirabal, Jose M.; Bolewski, Jacob C.; Walker, Larry P.

doi:10.1016/j.bpc.2011.02.003

Cited by 43 publications

(37 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…1, B and C). Similarly labeled cellulases have previously been shown to retain their original activity on cellulose (8,9). This was confirmed for our labeled enzymes with activity assays.…”

Section: Methodssupporting

confidence: 63%

Binding and Movement of Individual Cel7A Cellobiohydrolases on Crystalline Cellulose Surfaces Revealed by Single-molecule Fluorescence Imaging

Jung¹,

Sethi²,

Gaiotto

et al. 2013

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: Molecular level mechanisms underlying cellulose hydrolysis by cellulases remain poorly understood. Results: The majority of cellobiohydrolase molecules on cellulose surfaces were stationary. Conclusion: There is a need for improved understanding of cellulose properties resulting in large fractions of stalled cellulases. Significance: Dynamic single-molecule imaging of cellulases provides insights on productive/nonproductive binding and surface diffusion on cellulose.

show abstract

“…1, B and C). Similarly labeled cellulases have previously been shown to retain their original activity on cellulose (8,9). This was confirmed for our labeled enzymes with activity assays.…”

Section: Methodssupporting

confidence: 63%

Binding and Movement of Individual Cel7A Cellobiohydrolases on Crystalline Cellulose Surfaces Revealed by Single-molecule Fluorescence Imaging

Jung¹,

Sethi²,

Gaiotto

et al. 2013

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Many earlier works have shown that the adsorbed population of both two-domain Cel7A and isolated CBM decreases with increasing temperature (42,43,50,52,53), and it follows that temperature-activity relationships on insoluble substrate may be seen as a balance between accelerated reaction steps on one hand and a shift toward less surface-adsorbed (potentially active) enzyme on the other hand. The results in Table 1 allow evaluation of these two contributions.…”

Section: Discussionmentioning

confidence: 99%

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

“…Newly developed atomic force [24,51,77] and fluorescence [78,79] microscopy techniques are likely to reveal whether such interactions, or at least the physical proximity of the synergistic partners on the cellulose surface, are necessary for some forms of synergism. In addition, by monitoring the interactions between cellulases and the substrate, highresolution microscopy studies may improve our understanding of substrate recalcitrance to digestion and the way syn ergistic mixtures are able to overcome recalcitrance.…”

Section: Future Perspectivementioning

confidence: 99%

Synergistic interactions in cellulose hydrolysis

2012

View full text Add to dashboard Cite

Cellulases acting on crystalline cellulose in synergistic mixtures have higher combined activities than the sum of their individual activities. The mechanisms by which different types of cellulases enhance each other's activities are complex and not completely understood, and the published data is often inconsistent. We discuss the role of the substrate and experimental factors in synergism experiments and consider the various modes of synergism that have been proposed. New oxidoreductase enzymes that participate in novel synergistic reactions are also discussed. Finally, we propose a general encompassing synergism model, based on the observations described in the review.

show abstract

Reversibility and binding kinetics of Thermobifida fusca cellulases studied through fluorescence recovery after photobleaching microscopy

Cited by 43 publications

References 31 publications

Binding and Movement of Individual Cel7A Cellobiohydrolases on Crystalline Cellulose Surfaces Revealed by Single-molecule Fluorescence Imaging

Binding and Movement of Individual Cel7A Cellobiohydrolases on Crystalline Cellulose Surfaces Revealed by Single-molecule Fluorescence Imaging

Temperature Effects on Kinetic Parameters and Substrate Affinity of Cel7A Cellobiohydrolases

Synergistic interactions in cellulose hydrolysis

Contact Info

Product

Resources

About