Carbohydrate active enzyme domains from extreme thermophiles : components of a modular toolbox for lignocellulose degradation

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dc.contributor.author Botha, Jonathan
dc.contributor.author Mizrachi, Eshchar
dc.contributor.author Myburg, Alexander Andrew
dc.contributor.author Cowan, Don A.
dc.date.accessioned 2018-02-07T07:17:49Z
dc.date.issued 2018-01
dc.description Supplementary material 1 (XLSX 13 kb) en_ZA
dc.description Supplementary material 2 : Online Resource 2 CAZyme domains identified from extremely thermophilic organisms proteomes using HMMER analysis (PDF 44 kb) en_ZA
dc.description Supplementary material 3 (DOCX 80 kb) en_ZA
dc.description.abstract Lignocellulosic biomass is a promising feedstock for the manufacture of biodegradable and renewable bioproducts. However, the complex lignocellulosic polymeric structure of woody tissue is difficult to access without extensive industrial pre-treatment. Enzyme processing of partly depolymerised biomass is an established technology, and there is evidence that high temperature (extremely thermophilic) lignocellulose degrading enzymes [carbohydrate active enzymes (CAZymes)] may enhance processing efficiency. However, wild-type thermophilic CAZymes will not necessarily be functionally optimal under industrial pre-treatment conditions. With recent advances in synthetic biology, it is now potentially possible to build CAZyme constructs from individual protein domains, tailored to the conditions of specific industrial processes. In this review, we identify a ‘toolbox’ of thermostable CAZyme domains from extremely thermophilic organisms and highlight recent advances in CAZyme engineering which will allow for the rational design of CAZymes tailored to specific aspects of lignocellulose digestion. en_ZA
dc.description.department Forestry and Agricultural Biotechnology Institute (FABI) en_ZA
dc.description.department Genetics en_ZA
dc.description.embargo 2019-01-30
dc.description.librarian hj2018 en_ZA
dc.description.sponsorship The National Research Foundation (South Africa) en_ZA
dc.description.uri http://link.springer.com/journal/792 en_ZA
dc.identifier.citation Botha, J., Mizrachi, E., Myburg, A.A. et al. Carbohydrate active enzyme domains from extreme thermophiles: components of a modular toolbox for lignocellulose degradation. Extremophiles (2018) 22: 1-12. https://doi.org/10.1007/s00792-017-0974-7. en_ZA
dc.identifier.issn 1431-0651 (print)
dc.identifier.issn 1433-4909 (online)
dc.identifier.other 10.1007/s00792-017-0974-7
dc.identifier.uri http://hdl.handle.net/2263/63874
dc.language.iso en en_ZA
dc.publisher Springer en_ZA
dc.rights © Springer Japan KK 2017. The original publication is available at : http://link.springer.comjournal/792. en_ZA
dc.subject Carbohydrate active enzymes (CAZymes) en_ZA
dc.subject Lignocellulose en_ZA
dc.subject Extreme thermophiles en_ZA
dc.subject Synthetic biology en_ZA
dc.subject Protein domains en_ZA
dc.title Carbohydrate active enzyme domains from extreme thermophiles : components of a modular toolbox for lignocellulose degradation en_ZA
dc.type Postprint Article en_ZA


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