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

作者：De Winter Karel; Soetaert Wim; Desmet Tom^*

来源：International Journal of Molecular Sciences, 2012, 13(9): 11333-11342.

DOI：10.3390/ijms130911333

• sucrose phosphorylase
• immobilization
• imprinting
• CLEA
• glucosyl glycerol

The industrial use of sucrose phosphorylase (SP), an interesting biocatalyst for the selective transfer of alpha-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 alpha-glucosyl glycerol and subsequently cross-linked with glutaraldehyde. As a consequence, the enzyme%26apos;s specific activity towards glycerol as acceptor substrate was increased two-fold while simultaneously providing an exceptional stability at 60 degrees C. This procedure can be performed in an aqueous environment and gives rise to a new enzyme formulation called iCLEA.

• 出版日期2012-9