Cited by 27Enzyme Production and CharacterizationBiofuel production and bioconversionPolysaccharides and Plant Cell Walls

Metagenomic mining of glycoside hydrolases from the hindgut bacterial symbionts of a termite (Trinervitermes trinervoides) and the characterization of a multimodular β‐1,4‐xylanase (GH11)

Rashamuse, Konanani, Sanyika Tendai, Walter, Mathiba, Kgama, Ngcobo, Thobile, Mtimka, Sibongile, Brady, Dean·2017·Biotechnology and Applied Biochemistry

Abstract

In recent years, there have been particular emphases worldwide on the development and optimization of bioprocesses for the utilization of biomass. An essential component of the biomass processing conduit has been the need for robust biocatalysts as high-performance tools for both the depolymerization of lignocellulosic biomass and synthesis of new high-value bio-based chemical entities. Through functional screening of the metagenome of the hindgut bacterial symbionts of a termite, Trinervitermes trinervoides, we discovered open reading frames for 25 cellulases and hemicellulases. These were classified into 14 different glycoside hydrolase (GH) families: eight GH family 5; four GH9, two GH13, and one each in GH2, GH10, GH11, GH26, GH29, GH43, GH44, GH45, GH67, and GH94 families. Of these, eight were overexpressed and partially characterized to be shown to be endocellulases (GH5C, GH5E, GH5F, and GH5G), an exocellulase (GH5D), endoxylanases (GH5H and GH11), and an α-fucosidase (GH29). The GH11 (Xyl1) was of particular interest as it was discovered to be a multimodular β-1,4-xylanase, consisting of a catalytic domain and two carbohydrate-binding modules (CBMs). The CBM functions to selectively bind insoluble xylan and increases the rate of hydrolysis. The primary structure of GH11 showed a classical catalytic dyad of glutamic acid residues that generally forms part of the active site in GH11 enzyme family. This endoxylanase was optimal at pH 6 and 50 °C, and generated xylobiose and xylotriose from various xylan sources, including beechwood, birchwood, and wheat arabinoxylan. The catalytic ability of GH11 against natural substrate (e.g., wheat arabinoxylan) renders GH11 as a potential useful biocatalyst in the effective dismantling of complex plant biomass architecture.

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Crossref · 10.1002/bab.1480

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  • Sequencing techniques revealed a large variety of cellulose and hemicellulose hydrolysis related genes, enhancing understanding of cellulase richness.

    “By employing sequencing techniques, it become evident that there are a large variety of cellulose, hemicellulose hydrolysis related genes, which further enhances people's understanding of the richness of cellulase [83,84].”

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Authors
Rashamuse, K., Sanyika Tendai, W., Mathiba, K., Ngcobo, T., Mtimka, S., & Brady, D.
Affiliations
  • Council for Scientific and Industrial Research (ZA)
  • Biomanufacturing Centre CSIR Biosciences Pretoria South Africa
  • University of the Witwatersrand (ZA)
Corresponding author
Rashamuse, Konanani
Venue
Biotechnology and Applied Biochemistry
Publisher
Wiley
Published
2016-05-23
Volume
64
Issue
2
Pages
174-186
ISSN
  • 0885-4513 (ISSN-L)
  • 1470-8744
OpenAlex
W2396922342
Cited by
27
References
52
Citations by year
2026: 1 · 2025: 2 · 2024: 1 · 2023: 1 · 2022: 5 · 2021: 2 · 2020: 6 · 2019: 4 · 2018: 4 · 2017: 1
FWCI
2.61
Type
journal article
Language
en
Open access
closed
Locations
  • Biotechnology and Applied Biochemistry (publishedVersion)
  • PubMed (publishedVersion)
Funders
Department of Science and Technology, Ministry of Science and Technology, India
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
  • Physical Sciences › Engineering › Biomedical Engineering › Biofuel production and bioconversion
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Polysaccharides and Plant Cell Walls
Keywords
glycoside hydrolases, Trinervitermes trinervoides, β-1,4-xylanase, carbohydrate-binding module, endoxylanase, cellulase, hemicellulase, wheat arabinoxylan, xylobiose, xylotriose, biocatalysts
MeSH terms
Gastrointestinal Microbiome, Animals, Glycoside Hydrolases, Hydrolysis, Protein Conformation, Structure-Activity Relationship, Substrate Specificity, Symbiosis, Isoptera, Cellulases, Metagenomics

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