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Reference type: Journal
Authors: De Winter K, Soetaert W, Desmet T
Article Title: An Imprinted Cross-Linked Enzyme Aggregate (iCLEA) of Sucrose Phosphorylase: Combining Improved Stability with Altered Specificity.
Publication date: 2012
Journal: International Journal of Molecular Sciences
Volume: 13
Issue: (9)
Page numbers: 11333-11342.
DOI: 10.3390/ijms130911333

Abstract: The industrial use of sucrose phosphorylase (SP), an interesting biocatalyst for the selective transfer of a-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 a-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
Template and target information: bioimprinting


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