ArticleJournal of bacteriology2010
Comparative analyses of two thermophilic enzymes exhibiting both beta-1,4 mannosidic and beta-1,4 glucosidic cleavage activities from Caldanaerobius polysaccharolyticus.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 38 citations in OpenAlex.
- Biotechnological upgrading of palm kernel meal for poultry nutrition: Challenges and opportunities.Poultry science · 2026Review
- Atypical endo-β-1,4-mannanases are necessary for normal glucomannan synthesis in Arabidopsis.Plant physiology · 2026Article
- Cloning and Characterization of the Novel Endoglucanase Identified in Deep Subsurface Thermal Well of Biragzang (North Ossetia) by Metagenomic Analysis.Biomolecules · 2025Article
- Role of the CBM11, Fn3, and CBM3 Domains in Enhancing the Multifunctional Enzymatic Activities of Glycoside Hydrolase Family 5 fromJournal of microbiology and biotechnology · 2025Article
- Non-Catalytic Domains of Glycoside Hydrolase Family 5 fromJournal of microbiology and biotechnology · 2025Article
- Depolymerization and conversion of lignin to value-added bioproducts by microbial and enzymatic catalysis.Biotechnology for biofuels · 2021Review
- Thermophilic Degradation of Hemicellulose, a Critical Feedstock in the Production of Bioenergy and Other Value-Added Products.Applied and environmental microbiology · 2020Review
- Biochemical characterization of a thermostable endomannanase/endoglucanase from Dictyoglomus turgidum.Extremophiles : life under extreme conditions · 2018Article
- Insights into the roles of non-catalytic residues in the active site of a GH10 xylanase with activity on cellulose.The Journal of biological chemistry · 2017Article
- Enzymatic Mechanism for Arabinan Degradation and Transport in the Thermophilic Bacterium Caldanaerobius polysaccharolyticus.Applied and environmental microbiology · 2017Article
- Multidomain, Surface Layer-associated Glycoside Hydrolases Contribute to Plant Polysaccharide Degradation by Caldicellulosiruptor Species.The Journal of biological chemistry · 2016Article
- A review of the enzymatic hydrolysis of mannans and synergistic interactions between β-mannanase, β-mannosidase and α-galactosidase.World journal of microbiology & biotechnology · 2015Review
- Distinct roles for carbohydrate-binding modules of glycoside hydrolase 10 (GH10) and GH11 xylanases from Caldicellulosiruptor sp. strain F32 in thermostability and catalytic efficiency.Applied and environmental microbiology · 2015Article
- Structural and biochemical basis for mannan utilization by Caldanaerobius polysaccharolyticus strain ATCC BAA-17.The Journal of biological chemistry · 2014Article
- Xylan utilization in human gut commensal bacteria is orchestrated by unique modular organization of polysaccharide-degrading enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Structural and biochemical analyses of glycoside hydrolase family 26 β-mannanase from a symbiotic protist of the termite Reticulitermes speratus.The Journal of biological chemistry · 2014Article
- Molecular dynamics study of enhanced Man5B enzymatic activity.Biotechnology for biofuels · 2014Article
- Reconstitution of a thermostable xylan-degrading enzyme mixture from the bacterium Caldicellulosiruptor bescii.Applied and environmental microbiology · 2013Article
- Article
- Biochemical and structural insights into xylan utilization by the thermophilic bacterium Caldanaerobius polysaccharolyticus.The Journal of biological chemistry · 2012Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
The hydrolysis of polysaccharides containing mannan requires endo-1,4-beta-mannanase and 1,4-beta-mannosidase activities. In the current report, the biochemical properties of two endo-beta-1,4-mannanases (Man5A and Man5B) from Caldanaerobius polysaccharolyticus were studied. Man5A is composed of an N-terminal signal peptide (SP), a catalytic domain, two carbohydrate-binding modules (CBMs), and three surface layer homology (SLH) repeats, whereas Man5B lacks the SP, CBMs, and SLH repeats. To gain insights into how the two glycoside hydrolase family 5 (GH5) enzymes may aid the bacterium in energy acquisition and also the potential application of the two enzymes in the biofuel industry, two derivatives of Man5A (Man5A-TM1 [TM1 stands for truncational mutant 1], which lacks the SP and SLH repeats, and Man5A-TM2, which lacks the SP, CBMs, and SLH repeats) and the wild-type Man5B were biochemically analyzed. The Man5A derivatives displayed endo-1,4-beta-mannanase and endo-1,4-beta-glucanase activities and hydrolyzed oligosaccharides with a degree of polymerization (DP) of 4 or higher. Man5B exhibited endo-1,4-beta-mannanase activity and little endo-1,4-beta-glucanase activity; however, this enzyme also exhibited 1,4-beta-mannosidase and cellodextrinase activities. Man5A-TM1, compared to either Man5A-TM2 or Man5B, had higher catalytic activity with soluble and insoluble polysaccharides, indicating that the CBMs enhance catalysis of Man5A. Furthermore, Man5A-TM1 acted synergistically with Man5B in the hydrolysis of beta-mannan and carboxymethyl cellulose. The versatility of the two enzymes, therefore, makes them a resource for depolymerization of mannan-containing polysaccharides in the biofuel industry. Furthermore, on the basis of the biochemical and genomic data, a molecular mechanism for utilization of mannan-containing nutrients by C. polysaccharolyticus is proposed.
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