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dc.contributor.author Rashamuse, Konanani J
dc.contributor.author Tendai, WS
dc.contributor.author Mathiba, Kgama
dc.contributor.author Ngcobo, Thobile F
dc.contributor.author Mtimka, Sibongile
dc.contributor.author Brady, Dean
dc.date.accessioned 2018-09-25T10:33:43Z
dc.date.available 2018-09-25T10:33:43Z
dc.date.issued 2016-05
dc.identifier.citation Rashamuse, K.J., Tendai, W.S., Mathiba, K., Ngcobo, T.F., Mtimka, S. and Brady, D. 2016. Metagenomic mining of glycoside hydrolases from the hindgut bacterial symbionts of a termite (Trinervitermes trinervoides) and the characterization of a multimodular ß-1,4-xylanase (GH11). Biotechnology and Applied Biochemistry, pp 174-186 en_US
dc.identifier.issn 0885-4513
dc.identifier.uri http://www.ncbi.nlm.nih.gov/pubmed/26790627
dc.identifier.uri doi: 10.1002/bab.1480
dc.identifier.uri http://hdl.handle.net/10204/10419
dc.description Copyright: 2018. NCBI. Due to copyright restrictions, the attached PDF file only contains the abstract of the full text item. For access to the full text item, please consult the publisher's website. The definitive version of the work is published in Biotechnology and Applied Biochemistry, pp 174-186 en_US
dc.description.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 a-fucosidase (GH29). The GH11 (Xyl1) was of particular interest as it was discovered to be a multimodular ß-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. en_US
dc.language.iso en en_US
dc.publisher National Center for Biotechnology Information en_US
dc.relation.ispartofseries Workflow;17247
dc.subject Biomass en_US
dc.subject Glycoside hydrolases en_US
dc.subject Metagenomics en_US
dc.subject Termite hindgut en_US
dc.subject Xylanas en_US
dc.title Metagenomic mining of glycoside hydrolases from the hindgut bacterial symbionts of a termite (Trinervitermes trinervoides) and the characterization of a multimodular ß-1,4-xylanase (GH11) en_US
dc.type Article en_US


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