Botha, JonathanMizrachi, EshcharMyburg, Alexander AndrewCowan, Don A.2018-02-072018-01Botha, 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/s00792-017-0974-7.1431-0651 (print)1433-4909 (online)10.1007/s00792-017-0974-7http://hdl.handle.net/2263/63874Supplementary material 1 (XLSX 13 kb)Supplementary material 2 : Online Resource 2 CAZyme domains identified from extremely thermophilic organisms proteomes using HMMER analysis (PDF 44 kb)Supplementary material 3 (DOCX 80 kb)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© Springer Japan KK 2017. The original publication is available at : http://link.springer.comjournal/792.Carbohydrate active enzymes (CAZymes)LignocelluloseExtreme thermophilesSynthetic biologyProtein domainsPostprint Article