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)

Biotechnology and Applied Biochemistry
Konanani RashamuseDean Brady

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 th...Continue Reading

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Citations

May 18, 2018·Chemical Communications : Chem Comm·Roger A Sheldon, Dean Brady
Nov 30, 2018·PLoS Computational Biology·Ryman ShokoHugh Patterton
Dec 7, 2018·Proceedings of the National Academy of Sciences of the United States of America·Gaku TokudaAndreas Brune
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Oct 5, 2020·International Journal of Biological Macromolecules·Raul Alcântara Teixeira LimaRicardo Henrique Krüger

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