ArticleThe Journal of biological chemistry2015
Temperature Effects on Kinetic Parameters and Substrate Affinity of Cel7A Cellobiohydrolases.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 59 citations in OpenAlex.
- Engineering natural Saccharomyces cerevisiae isolates for enhanced one-step cellulosic ethanol production.Applied microbiology and biotechnology · 2026Article
- Microbial chitinases in the plant holobiont: ecological roles and structural determinants.FEMS microbiology reviews · 2026Review
- Metabolic rearrangement enables adaptation of microbial growth rate to temperature shifts.Nature microbiology · 2025Article
- Impact of Synergy Partner Cel7B on Cel7A Binding Rates: Insights from Single-Molecule Data.The journal of physical chemistry. B · 2024Article
- Structural and functional characterization of a multi-domain GH92 α-1,2-mannosidase from Neobacillus novalis.Acta crystallographica. Section D, Structural biology · 2023Article
- Biogas Production Potential of Thermophilic Anaerobic Biodegradation of Organic Waste by a Microbial Consortium Identified with Metagenomics.Life (Basel, Switzerland) · 2022Article
- Analysis of fungal high-mannose structures using CAZymes.Glycobiology · 2022Article
- Ammonia-oxidizing archaea possess a wide range of cellular ammonia affinities.The ISME journal · 2022Article
- Physical constraints and functional plasticity of cellulases.Nature communications · 2021Article
- Enzymatic processing of lignocellulosic biomass: principles, recent advances and perspectives.Journal of industrial microbiology & biotechnology · 2020Review
- Substrate binding in the processive cellulase Cel7A: Transition state of complexation and roles of conserved tryptophan residues.The Journal of biological chemistry · 2020Article
- Removal ofBiotechnology for biofuels · 2020Article
- Activity of fungal β-glucosidases on cellulose.Biotechnology for biofuels · 2020Article
- Modeling the activity burst in the initial phase of cellulose hydrolysis by the processive cellobiohydrolase Cel7A.Biotechnology and bioengineering · 2019Article
- Systematic deletions in the cellobiohydrolase (CBH) Cel7A from the fungusThe Journal of biological chemistry · 2019Article
- Boosting of enzymatic softwood saccharification by fungal GH5 and GH26 endomannanases.Biotechnology for biofuels · 2018Article
- Inter-domain Synergism Is Required for Efficient Feeding of Cellulose Chain into Active Site of Cellobiohydrolase Cel7A.The Journal of biological chemistry · 2016Article
- Slow Off-rates and Strong Product Binding Are Required for Processivity and Efficient Degradation of Recalcitrant Chitin by Family 18 Chitinases.The Journal of biological chemistry · 2015Article
- Free Energy Diagram for the Heterogeneous Enzymatic Hydrolysis of Glycosidic Bonds in Cellulose.The Journal of biological chemistry · 2015Article
- A comparative biochemical investigation of the impeding effect of C1-oxidizing LPMOs on cellobiohydrolases.The Journal of biological chemistryArticle
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We measured hydrolytic rates of four purified cellulases in small increments of temperature (10-50 °C) and substrate loads (0-100 g/liter) and analyzed the data by a steady state kinetic model that accounts for the processive mechanism. We used wild type cellobiohydrolases (Cel7A) from mesophilic Hypocrea jecorina and thermophilic Rasamsonia emersonii and two variants of these enzymes designed to elucidate the role of the carbohydrate binding module (CBM). We consistently found that the maximal rate increased strongly with temperature, whereas the affinity for the insoluble substrate decreased, and as a result, the effect of temperature depended strongly on the substrate load. Thus, temperature had little or no effect on the hydrolytic rate in dilute substrate suspensions, whereas strong temperature activation (Q10 values up to 2.6) was observed at saturating substrate loads. The CBM had a dual effect on the activity. On one hand, it diminished the tendency of heat-induced desorption, but on the other hand, it had a pronounced negative effect on the maximal rate, which was 2-fold larger in variants without CBM throughout the investigated temperature range. We conclude that although the CBM is beneficial for affinity it slows down the catalytic process. Cel7A from the thermophilic organism was moderately more activated by temperature than the mesophilic analog. This is in accord with general theories on enzyme temperature adaptation and possibly relevant information for the selection of technical cellulases.
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