Molecular engineering of the cellulosome complex for affinity and bioenergy applications |
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Authors: | Robert E Nordon Scott J Craig Frances C Foong |
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Institution: | (1) Graduate School of Biomedical Engineering, University of New South Wales, Sydney, 2052, NSW, Australia;(2) School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, NSW, Australia |
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Abstract: | The cellulosome complex has evolved to degrade plant cell walls and, as such, combines tenacious binding to cellulose with
diverse catalytic activities against amorphous and crystalline cellulose. Cellulolytic microorganisms provide an extensive
selection of domains; those with affinity for cellulose, cohesins and their dockerin binding partners that define cellulosome
stoichiometry and architecture, and a range of catalytic activities against carbohydrates. These robust domains provide the
building blocks for molecular design. This review examines how protein modules derived from the cellulosome have been incorporated
into chimaeric proteins to provide biosynthetic tools for research and industry. These applications include affinity tags
for protein purification, and non-chemical methods for immobilisation and presentation of recombinant protein domains on cellulosic
substrates. Cellulosomal architecture provides a paradigm for design of enzymatic complexes that synergistically combine multiple
catalytic subunits to achieve higher specific activity than would be obtained using free enzymes. Multimeric enzymatic complexes
may have industrial applications of relevance for an emerging carbon economy. Biocatalysis will lead to more efficient utilisation
of renewable carbon-fixing energy sources with the added benefits of reducing chemical waste streams and reliance on petroleum. |
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Keywords: | Biocatalysis Bioethanol Carbohydrate binding module Cellulosome Cohesin Dockerin Scaffoldin |
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