Functional metagenomics unveils a multifunctional glycosyl hydrolase from the family 43 catalysing the breakdown of plant polymers in the calf rumen.
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Your vote was cast
Thank you for your feedback
Thank you for your feedback
Vieites, José María
Nechitaylo, Taras Y
Chernikova, Tatyana N
Reva, Oleg N
Golyshina, Olga V
Golyshin, Peter N
MetadataShow full item record
AbstractMicrobial communities from cow rumen are known for their ability to degrade diverse plant polymers at high rates. In this work, we identified 15 hydrolases through an activity-centred metagenome analysis of a fibre-adherent microbial community from dairy cow rumen. Among them, 7 glycosyl hydrolases (GHs) and 1 feruloyl esterase were successfully cloned, expressed, purified and characterised. The most striking result was a protein of GH family 43 (GHF43), hereinafter designated as R_09-02, which had characteristics very distinct from the other proteins in this family with mono-functional β-xylosidase, α-xylanase, α-L-arabinase and α-L-arabinofuranosidase activities. R_09-02 is the first multifunctional enzyme to exhibit β-1,4 xylosidase, α-1,5 arabinofur(pyr)anosidase, β-1,4 lactase, α-1,6 raffinase, α-1,6 stachyase, β-galactosidase and α-1,4 glucosidase activities. The R_09-02 protein appears to originate from the chromosome of a member of Clostridia, a class of phylum Firmicutes, members of which are highly abundant in ruminal environment. The evolution of R_09-02 is suggested to be driven from the xylose- and arabinose-specific activities, typical for GHF43 members, toward a broader specificity to the glucose- and galactose-containing components of lignocellulose. The apparent capability of enzymes from the GHF43 family to utilise xylose-, arabinose-, glucose- and galactose-containing oligosaccharides has thus far been neglected by, or could not be predicted from, genome and metagenome sequencing data analyses. Taking into account the abundance of GHF43-encoding gene sequences in the rumen (up to 7% of all GH-genes) and the multifunctional phenotype herein described, our findings suggest that the ecological role of this GH family in the digestion of ligno-cellulosic matter should be significantly reconsidered.
CitationFunctional metagenomics unveils a multifunctional glycosyl hydrolase from the family 43 catalysing the breakdown of plant polymers in the calf rumen. 2012, 7 (6):e38134 PLoS ONE
AffiliationCSIC, Institute of Catalysis, Madrid, Spain. firstname.lastname@example.org
The following license files are associated with this item:
- Biochemical and kinetic characterization of GH43 β-D-xylosidase/α-L-arabinofuranosidase and GH30 α-L-arabinofuranosidase/β-D -xylosidase from rumen metagenome.
- Authors: Zhou J, Bao L, Chang L, Zhou Y, Lu H
- Issue date: 2012 Jan
- High genetic diversity and different distributions of glycosyl hydrolase family 10 and 11 xylanases in the goat rumen.
- Authors: Wang G, Luo H, Meng K, Wang Y, Huang H, Shi P, Pan X, Yang P, Diao Q, Zhang H, Yao B
- Issue date: 2011 Feb 3
- Metagenomic insights into the fibrolytic microbiome in yak rumen.
- Authors: Dai X, Zhu Y, Luo Y, Song L, Liu D, Liu L, Chen F, Wang M, Li J, Zeng X, Dong Z, Hu S, Li L, Xu J, Huang L, Dong X
- Issue date: 2012
- Isolation and characterization of novel multifunctional recombinant family 26 glycoside hydrolase from Mehsani buffalo rumen metagenome.
- Authors: Patel AB, Patel AK, Shah MP, Parikh IK, Joshi CG
- Issue date: 2016 Mar-Apr
- Characterization of novel lignocellulose-degrading enzymes from the porcupine microbiome using synthetic metagenomics.
- Authors: Thornbury M, Sicheri J, Slaine P, Getz LJ, Finlayson-Trick E, Cook J, Guinard C, Boudreau N, Jakeman D, Rohde J, McCormick C
- Issue date: 2019