Systematic comparison of HEA and HEMA as initiators in enzymatic ring-opening polymerizations

Y. Xiao; M. Takwa; K. Hult; C.E. Koning; A. Heise; M. Martinelle

doi:10.1002/mabi.200800290

Systematic comparison of HEA and HEMA as initiators in enzymatic ring-opening polymerizations

Y. Xiao, M. Takwa, K. Hult, C.E. Koning, A. Heise, M. Martinelle

Research output: Contribution to journal › Article › Academic › peer-review

18 Citations (Scopus)

Abstract

Two initiators containing a cleavable ester bond were compared in the lipase-catalyzed ROP of CL and PDL. The results show that transesterification reactions are present at high rates throughout the enzymatic ROP and start at low conversion. HEA and HEMA displayed similar reaction efficiencies as initiators (acyl acceptors) in the enzymatic ROP. However, transacylation reactions on the HEA-initiated polyesters were found to be 15 times faster. While in both cases the amount of HEA- and HEMA-initiated polymers could be maximized by short reaction times, a well-defined (meth)acrylation by this approach was not possible. Our results show that transesterification reactions have to be considered when performing an enzyme-catalyzed ROP.

Original language	English
Pages (from-to)	713-720
Journal	Macromolecular Bioscience
Volume	9
Issue number	7
DOIs	https://doi.org/10.1002/mabi.200800290
Publication status	Published - 2009

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title = "Systematic comparison of HEA and HEMA as initiators in enzymatic ring-opening polymerizations",

abstract = "Two initiators containing a cleavable ester bond were compared in the lipase-catalyzed ROP of CL and PDL. The results show that transesterification reactions are present at high rates throughout the enzymatic ROP and start at low conversion. HEA and HEMA displayed similar reaction efficiencies as initiators (acyl acceptors) in the enzymatic ROP. However, transacylation reactions on the HEA-initiated polyesters were found to be 15 times faster. While in both cases the amount of HEA- and HEMA-initiated polymers could be maximized by short reaction times, a well-defined (meth)acrylation by this approach was not possible. Our results show that transesterification reactions have to be considered when performing an enzyme-catalyzed ROP.",

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AU - Xiao, Y.

AU - Takwa, M.

AU - Hult, K.

AU - Koning, C.E.

AU - Heise, A.

AU - Martinelle, M.

PY - 2009

Y1 - 2009

N2 - Two initiators containing a cleavable ester bond were compared in the lipase-catalyzed ROP of CL and PDL. The results show that transesterification reactions are present at high rates throughout the enzymatic ROP and start at low conversion. HEA and HEMA displayed similar reaction efficiencies as initiators (acyl acceptors) in the enzymatic ROP. However, transacylation reactions on the HEA-initiated polyesters were found to be 15 times faster. While in both cases the amount of HEA- and HEMA-initiated polymers could be maximized by short reaction times, a well-defined (meth)acrylation by this approach was not possible. Our results show that transesterification reactions have to be considered when performing an enzyme-catalyzed ROP.

AB - Two initiators containing a cleavable ester bond were compared in the lipase-catalyzed ROP of CL and PDL. The results show that transesterification reactions are present at high rates throughout the enzymatic ROP and start at low conversion. HEA and HEMA displayed similar reaction efficiencies as initiators (acyl acceptors) in the enzymatic ROP. However, transacylation reactions on the HEA-initiated polyesters were found to be 15 times faster. While in both cases the amount of HEA- and HEMA-initiated polymers could be maximized by short reaction times, a well-defined (meth)acrylation by this approach was not possible. Our results show that transesterification reactions have to be considered when performing an enzyme-catalyzed ROP.

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DO - 10.1002/mabi.200800290

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