Hydrolases Part I: Enzyme Mechanism, Selectivity and Control in the Synthesis of Well-Defined Polymers

Veld, Martijn A. J.; Palmans, Anja R. A.

doi:10.1007/12_2010_86

Martijn A. J. Veld³ &
Anja R. A. Palmans³

Part of the book series: Advances in Polymer Science ((POLYMER,volume 237))

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15 Citations

Abstract

Lipases are highly activity in the polymerization of a range of monomers. Both ring-opening polymerization of cyclic esters and polycondensation reactions of AA–BB and AB monomers have been investigated in great detail. This paper reviews the increased understanding in enzymatic strategies for the production of well-defined polymers. Major advantages of enzymatic catalysts are the relatively mild reaction conditions, and the often-observed excellent regio-, chemo-, and enantioselectivity that allow for the direct preparation of functional materials. However, as a result of the monomer activation mechanism, polymers of low polydispersity and low quantitative degree of endgroup functionality are difficult to attain. A wide variety of (co)polymers have been synthesized and explored in a variety of applications using lipase catalysts.

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Laboratory of Molecular Science and Technology, Eindhoven University of Technology, 513, 5600 MB, Eindhoven, The Netherlands
Martijn A. J. Veld & Anja R. A. Palmans

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Martijn A. J. Veld
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, Dept. Chemical Engineering & Chemistry, Eindhoven University of Technology, Eindhoven, 5600 MB, Netherlands
Anja R. A. Palmans
, School of Chemical Sciences, Dublin City University, Glasnevin, Dublin, 9, Ireland
Andreas Heise

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Veld, M.A.J., Palmans, A.R.A. (2010). Hydrolases Part I: Enzyme Mechanism, Selectivity and Control in the Synthesis of Well-Defined Polymers. In: Palmans, A., Heise, A. (eds) Enzymatic Polymerisation. Advances in Polymer Science, vol 237. Springer, Berlin, Heidelberg. https://doi.org/10.1007/12_2010_86

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DOI: https://doi.org/10.1007/12_2010_86
Published: 10 June 2010
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