ArticleApplied and environmental microbiology2011
Comparison of family 9 cellulases from mesophilic and thermophilic bacteria.
Article in Applied and environmental microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 62 citations in OpenAlex.
- Cellulase secretion by engineered Pseudomonas putida enables growth on cellulose oligomers.Applied microbiology and biotechnology · 2025Article
- Cellulolytic and Ethanologenic Evaluation ofACS omega · 2024Article
- Diversity of Cellulolytic Microorganisms Associated with the Subterranean TermiteJournal of fungi (Basel, Switzerland) · 2023Article
- Some characters of bacterial cellulases in goats' rumen elucidated by metagenomic DNA analysis and the role of fibronectin 3 module for endoglucanase function.Animal bioscience · 2021Article
- Parallel molecular mechanisms for enzyme temperature adaptation.Science (New York, N.Y.) · 2021Article
- Cellulolytic thermophilic microorganisms in white biotechnology: a review.Folia microbiologica · 2020Review
- Extremophile - An Adaptive Strategy for Extreme Conditions and Applications.Current genomics · 2020Review
- Origin, evolution, and divergence of plant class C GH9 endoglucanases.BMC evolutionary biology · 2018Article
- The Genome of a Thermo Tolerant, Pathogenic AlbinoFrontiers in microbiology · 2018Article
- Alkene hydrogenation activity of enoate reductases for an environmentally benign biosynthesis of adipic acid.Chemical science · 2017Article
- Polarity Alteration of a Calcium Site Induces a Hydrophobic Interaction Network and Enhances Cel9A Endoglucanase Thermostability.Applied and environmental microbiology · 2016Article
- Structure, activity, and stability of metagenome-derived glycoside hydrolase family 9 endoglucanase with an N-terminal Ig-like domain.Protein science : a publication of the Protein Society · 2015Article
- Significance of relative position of cellulases in designer cellulosomes for optimized cellulolysis.PloS one · 2015Article
- Article
- First thermostable endo-β-1,4-glucanase from newly isolated Xanthomonas sp. EC102.The protein journal · 2014Article
- Aspergillus niger β-glucosidase has a cellulase-like tadpole molecular shape: insights into glycoside hydrolase family 3 (GH3) β-glucosidase structure and function.The Journal of biological chemistry · 2013Article
- Endoglucanases: insights into thermostability for biofuel applications.Biotechnology for biofuels · 2013Article
- Plant carbohydrate binding module enhances activity of hybrid microbial cellulase enzyme.Frontiers in plant science · 2012Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cellulases containing a family 9 catalytic domain and a family 3c cellulose binding module (CBM3c) are important components of bacterial cellulolytic systems. We measured the temperature dependence of the activities of three homologs: Clostridium cellulolyticum Cel9G, Thermobifida fusca Cel9A, and C. thermocellum Cel9I. To directly compare their catalytic activities, we constructed six new versions of the enzymes in which the three GH9-CBM3c domains were fused to a dockerin both with and without a T. fusca fibronectin type 3 homology module (Fn3). We studied the activities of these enzymes on crystalline cellulose alone and in complex with a miniscaffoldin containing a cohesin and a CBM3a. The presence of Fn3 had no measurable effect on thermostability or cellulase activity. The GH9-CBM3c domains of Cel9A and Cel9I, however, were more active than the wild type when fused to a dockerin complexed to scaffoldin. The three cellulases in complex have similar activities on crystalline cellulose up to 60°C, but C. thermocellum Cel9I, the most thermostable of the three, remains highly active up to 80°C, where its activity is 1.9 times higher than at 60°C. We also compared the temperature-dependent activities of different versions of Cel9I (wild type or in complex with a miniscaffoldin) and found that the thermostable CBM is necessary for activity on crystalline cellulose at high temperatures. These results illustrate the significant benefits of working with thermostable enzymes at high temperatures, as well as the importance of retaining the stability of all modules involved in cellulose degradation.
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