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Int. J. Mol. Sci. 2012, 13(9), 11333-11342; doi:10.3390/ijms130911333

An Imprinted Cross-Linked Enzyme Aggregate (iCLEA) of Sucrose Phosphorylase: Combining Improved Stability with Altered Specificity

Centre of Expertise for Industrial Biotechnology and Biocatalysis, Department of Biochemical and Microbial Technology, Faculty of Biosciences Engineering, Ghent University, Coupure Links 653, Ghent B-9000, Belgium
Author to whom correspondence should be addressed.
Received: 28 August 2012 / Revised: 5 September 2012 / Accepted: 5 September 2012 / Published: 11 September 2012
(This article belongs to the Special Issue Enzyme Optimization and Immobilization)
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The industrial use of sucrose phosphorylase (SP), an interesting biocatalyst for the selective transfer of α-glucosyl residues to various acceptor molecules, has been hampered by a lack of long-term stability and low activity towards alternative substrates. We have recently shown that the stability of the SP from Bifidobacterium adolescentis can be significantly improved by the formation of a cross-linked enzyme aggregate (CLEA). In this work, it is shown that the transglucosylation activity of such a CLEA can also be improved by molecular imprinting with a suitable substrate. To obtain proof of concept, SP was imprinted with α-glucosyl glycerol and subsequently cross-linked with glutaraldehyde. As a consequence, the enzyme’s specific activity towards glycerol as acceptor substrate was increased two-fold while simultaneously providing an exceptional stability at 60 °C. This procedure can be performed in an aqueous environment and gives rise to a new enzyme formulation called iCLEA. View Full-Text
Keywords: sucrose phosphorylase; immobilization; imprinting; CLEA; glucosyl glycerol sucrose phosphorylase; immobilization; imprinting; CLEA; glucosyl glycerol

This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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De Winter, K.; Soetaert, W.; Desmet, T. An Imprinted Cross-Linked Enzyme Aggregate (iCLEA) of Sucrose Phosphorylase: Combining Improved Stability with Altered Specificity. Int. J. Mol. Sci. 2012, 13, 11333-11342.

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