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

Care, A; Petroll, K; Gibson, ESY; Bergquist, PL; Sunna, A

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

Care, A

Petroll, K Gibson, ESY Bergquist, PL Sunna, A

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Publisher:: BIOMED CENTRAL LTD
Publication Type:: Journal Article
Citation:: Biotechnol Biofuels, 2017, 10, (1), pp. 29
Issue Date:: 2017

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Field	Value	Language
dc.contributor.author	Care, A https://orcid.org/0000-0002-0035-7961
dc.contributor.author	Petroll, K
dc.contributor.author	Gibson, ESY
dc.contributor.author	Bergquist, PL
dc.contributor.author	Sunna, A
dc.date.accessioned	2022-03-25T04:51:24Z
dc.date.available	2017-01-19
dc.date.available	2022-03-25T04:51:24Z
dc.date.issued	2017
dc.identifier.citation	Biotechnol Biofuels, 2017, 10, (1), pp. 29
dc.identifier.issn	1754-6834
dc.identifier.issn	1754-6834
dc.identifier.uri	http://hdl.handle.net/10453/155567
dc.description.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.
dc.format	Electronic-eCollection
dc.language	eng
dc.publisher	BIOMED CENTRAL LTD
dc.relation.ispartof	Biotechnol Biofuels
dc.relation.isbasedon	10.1186/s13068-017-0715-2
dc.rights	info:eu-repo/semantics/openAccess
dc.subject	0904 Chemical Engineering, 1003 Industrial Biotechnology
dc.title	Solid-binding peptides for immobilisation of thermostable enzymes to hydrolyse biomass polysaccharides.
dc.type	Journal Article
utslib.citation.volume	10
utslib.location.activity	England
utslib.for	0904 Chemical Engineering
utslib.for	1003 Industrial Biotechnology
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Life Sciences
utslib.copyright.status	open_access	*
dc.date.updated	2022-03-25T04:51:18Z
pubs.issue	1
pubs.publication-status	Published online
pubs.volume	10
utslib.citation.issue	1

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.

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http://hdl.handle.net/10453/155567