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Carrier-free immobilized enzymes for biocatalysis

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Abstract

Methods for the preparation of carrier-free insoluble enzymes are reviewed. The technology of cross-linked enzyme aggregates has now been applied to a range of synthetically useful activities. Fusion proteins are also gaining momentum because they allow a relatively selective aggregation or even a specific self-assembly of the desired enzyme activity into insoluble particles in the absence of potentially denaturing chemicals required for precipitation and cross-linking. Recycling of insoluble protein particles for multiple rounds of batchwise reaction has been demonstrated in selected biotransformations. However, for application in a fully continuous biocatalytic process, low resistance to mechanical stress and high compressibility are issues for consideration on carrier-free enzyme particles.

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Acknowledgments

B.N. and J.N. acknowledge support from a project for scientific and technological co-operation between Austria and Slovakia (SK-AT-0024-08).

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  1. Institute of Biotechnology and Biochemical Engineering, Graz University of Technology, Petersgasse 12, 8010, Graz, Austria

    Ulrich Roessl & Bernd Nidetzky

  2. Institute of Chemistry, Center for Glycomics, Slovak Academy of Sciences, Dúbravská cesta 9, 84538, Bratislava, Slovak Republic

    Jozef Nahálka

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  1. Ulrich Roessl
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Correspondence to Bernd Nidetzky.

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Roessl, U., Nahálka, J. & Nidetzky, B. Carrier-free immobilized enzymes for biocatalysis. Biotechnol Lett 32, 341–350 (2010). https://doi.org/10.1007/s10529-009-0173-4

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