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

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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.

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Acknowledgements

The authors wish to thank the National Research Foundation (South Africa) for financial support.

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Authors and Affiliations

  1. Department of Genetics, Centre for Microbial Ecology and Genomics, University of Pretoria, Private Bag X20, Pretoria, 0028, South Africa

    Jonathan Botha & Don A. Cowan

  2. Department of Genetics, University of Pretoria, Private Bag X20, Pretoria, 0028, South Africa

    Jonathan Botha, Eshchar Mizrachi, Alexander A. Myburg & Don A. Cowan

  3. Forestry and Agricultural Biotechnology Institute (FABI), University of Pretoria, Private Bag X20, Pretoria, 0028, South Africa

    Eshchar Mizrachi & Alexander A. Myburg

  4. Genomics Research Institute (GRI), University of Pretoria, Private Bag X20, Pretoria, 0028, South Africa

    Jonathan Botha & Don A. Cowan

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  1. Jonathan Botha
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  2. Eshchar Mizrachi
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  3. Alexander A. Myburg
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  4. Don A. Cowan
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Correspondence to Don A. Cowan.

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Communicated by S. Albers.

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Online Resource 2 CAZyme domains identified from extremely thermophilic organisms proteomes using HMMER analysis (PDF 44 kb)

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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 22, 1–12 (2018). https://doi.org/10.1007/s00792-017-0974-7

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  • DOI: https://doi.org/10.1007/s00792-017-0974-7

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