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Care A, Petroll K, Gibson ESY, et al. Solid-binding peptides for immobilisation of thermostable enzymes to hydrolyse biomass polysaccharides. Biotechnol Biofuels. 2017;10:29doi: 10.1186/s13068-017-0715-2.
Care, A., Petroll, K., Gibson, E. S. Y., Bergquist, P. L., & Sunna, A. (2017). Solid-binding peptides for immobilisation of thermostable enzymes to hydrolyse biomass polysaccharides. Biotechnology for biofuels, 1029. https://doi.org/10.1186/s13068-017-0715-2
Care, Andrew, et al. "Solid-binding peptides for immobilisation of thermostable enzymes to hydrolyse biomass polysaccharides." Biotechnology for biofuels vol. 10 (2017): 29. doi: https://doi.org/10.1186/s13068-017-0715-2
Care A, Petroll K, Gibson ESY, Bergquist PL, Sunna A. Solid-binding peptides for immobilisation of thermostable enzymes to hydrolyse biomass polysaccharides. Biotechnol Biofuels. 2017 Feb 02;10:29. doi: 10.1186/s13068-017-0715-2. eCollection 2017. PMID: 28184244; PMCID: PMC5289021.
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Biotechnol Biofuels. 2017 Feb 02;10:29. doi: 10.1186/s13068-017-0715-2. eCollection 2017.

Solid-binding peptides for immobilisation of thermostable enzymes to hydrolyse biomass polysaccharides.

Biotechnology for biofuels

Andrew Care, Kerstin Petroll, Emily S Y Gibson, Peter L Bergquist, Anwar Sunna

Affiliations

  1. Department of Chemistry and Biomolecular Sciences, Macquarie University, Sydney, Australia.
  2. ARC Centre of Excellence for Nanoscale BioPhotonics (CNBP), Macquarie University, Sydney, Australia.
  3. Department of Molecular Medicine & Pathology, Medical School, University of Auckland, Auckland, New Zealand.
  4. Biomolecular Discovery and Design Research Centre, Macquarie University, Sydney, Australia.

PMID: 28184244 PMCID: PMC5289021 DOI: 10.1186/s13068-017-0715-2

Abstract

BACKGROUND: Solid-binding peptides (SBPs) bind strongly to a diverse range of solid materials without the need for any chemical reactions. They have been used mainly for the functionalisation of nanomaterials but little is known about their use for the immobilisation of thermostable enzymes and their feasibility in industrial-scale biocatalysis.

RESULTS: A silica-binding SBP sequence was fused genetically to three thermostable hemicellulases. The resulting enzymes were active after fusion and exhibited identical pH and temperature optima but differing thermostabilities when compared to their corresponding unmodified enzymes. The silica-binding peptide mediated the efficient immobilisation of each enzyme onto zeolite, demonstrating the construction of single enzyme biocatalytic modules. Cross-linked enzyme aggregates (CLEAs) of enzyme preparations either with or without zeolite immobilisation displayed greater activity retention during enzyme recycling than those of free enzymes (without silica-binding peptide) or zeolite-bound enzymes without any crosslinking. CLEA preparations comprising all three enzymes simultaneously immobilised onto zeolite enabled the formation of multiple enzyme biocatalytic modules which were shown to degrade several hemicellulosic substrates.

CONCLUSIONS: The current work introduced the construction of functional biocatalytic modules for the hydrolysis of simple and complex polysaccharides. This technology exploited a silica-binding SBP to mediate effectively the rapid and simple immobilisation of thermostable enzymes onto readily-available and inexpensive silica-based matrices. A conceptual application of biocatalytic modules consisting of single or multiple enzymes was validated by hydrolysing various hemicellulosic polysaccharides.

Keywords: Biocatalytic modules; CLEAs; Enzyme immobilisation; Solid-binding peptide; Thermostable enzymes

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