Understanding How Diverse -Mannanases Recognise Heterogeneous Substrates.

  title={Understanding How Diverse -Mannanases Recognise Heterogeneous Substrates.},
  author={Louise E. Tailford and Val{\'e}rie M.-A. Ducros and James E. Flint and Shirley M. Roberts and Carl Morland and David L Zechel and Nicola L. Smith and Mads Eskelund Bj{\o}rnvad and Torben Vedel Borchert and Keith S Wilson and Gideon J. Davies and Harry J. Gilbert},
Structural and Biochemical Analyses of Glycoside Hydrolase Family 26 β-Mannanase from a Symbiotic Protist of the Termite Reticulitermes speratus*
Background: Symbiotic protists of the termite gut contribute to lignocellulosic biomass degradation. Results: A novel protistan β-mannanase efficiently degrades glucomannan and displaysExpand
Comparative Analyses of Two Thermophilic Enzymes Exhibiting both β-1,4 Mannosidic and β-1,4 Glucosidic Cleavage Activities from Caldanaerobius polysaccharolyticus
On the basis of the biochemical and genomic data, a molecular mechanism for utilization of mannan-containing nutrients by C. polysaccharolyticus is proposed and it is proposed that the CBMs enhance catalysis of Man5A. Expand
Understanding How the Complex Molecular Architecture of Mannan-degrading Hydrolases Contributes to Plant Cell Wall Degradation*
Background: The molecular architectures of cell wall degrading enzymes are complex. Results: The activity of mannanases and esterases and CBM function against cell walls are driven by substrateExpand
Les polymères de mannose en production animale. 2. Les enzymes de dégradation des mannanes dans l’alimentation des porcs et des volailles
Mannose-based polymers in livestock production : the glucomannan-degrading enzymes in swine and poultry feeds Enzymes capable of degrading mannans belong to several families, which are distinguishedExpand
Applications of Microbial β-Mannanases
  • A. Dawood, K. Ma
  • Medicine
  • Frontiers in Bioengineering and Biotechnology
  • 2020
This review summarizes the most recent studies reported on potential applications and bioengineering of β-mannanases to modify and optimize their key catalytic properties to cater to growing demands of commercial sectors. Expand
Characterization of two GH5 endoglucanases from termite microbiome using synthetic metagenomics
Describing two novel GH5 endoglucanases from an uncultured bacterium identified in termite gut microbiomes indicated that both enzymes possess a typical (β/α)8-barrel fold characteristic of GH5 family, with some differential features in the active site cleft. Expand
Expression, homology modeling and enzymatic characterization of a new β-mannanase belonging to glycoside hydrolase family 1 from Enterobacter aerogenes B19
The β-mannanase gene (Man1E), which encoded 731 amino acid residues, was cloned from Enterobacter aerogenes and heterologously expressed and characterized, laying the foundation for future application and molecular modification to improve its catalytic efficiency and substrate specificity. Expand
High-resolution structure of a modular hyperthermostable endo-β-1,4-mannanase from Thermotoga petrophila: The ancillary immunoglobulin-like module is a thermostabilizing domain.
Functional analysis showed that whereas the immunoglobulin-like domain does not have the carbohydrate-binding function, it stacks on the GH5 catalytic domain acting as a thermostabilizing domain and allowing operation at hyperthermophilic conditions. Expand
Spatially remote motifs cooperatively affect substrate preference of a ruminal GH26-type endo-β-1,4-mannanase
Results indicate a novel and complex mechanism for substrate recognition involving spatially remote motifs, distal negative subsites from the catalytic domain, and a surface-associated aromatic cluster from the ancillary domain. Expand
A surface-exposed GH26 β-mannanase from Bacteroides ovatus: Structure, role, and phylogenetic analysis of BoMan26B
The results suggested that BoMan26B performs the initial attack on galactomannan, generating oligosaccharides that after transport to the periplasm are processed by BoGal36A, which is implicated in saccharide transport. Expand