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Molecular engineering of the cellulosome complex for affinity and bioenergy applications.

Authors
  • Nordon, Robert E
  • Craig, Scott J
  • Foong, Frances C
Type
Published Article
Journal
Biotechnology Letters
Publisher
Springer-Verlag
Publication Date
Apr 01, 2009
Volume
31
Issue
4
Pages
465–476
Identifiers
DOI: 10.1007/s10529-008-9899-7
PMID: 19116695
Source
Medline
License
Unknown

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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