Issue 26, 2011
From the journal:

Chemical Communications

Rational redesign of Candida antarcticalipase B for the ring opening polymerization of d,d-lactide†

Mohamad Takwa,a   Marianne Wittrup Larsen,a   Karl Hulta  and  Mats Martinelle*a  

* Corresponding authors

a Royal Institute of Technology, School of Biotechnology, Department of Biochemistry, AlbaNova University Centre, 106 91 Stockholm, Sweden
E-mail: matsm@biotech.kth.se
Fax: +46 8 55378468
Tel: +46 8 55378384

Abstract

Based on molecular modelling, the enzymeCandida antarcticalipase B was redesigned as a catalyst for the ring opening polymerization of D,D-lactide. Two mutants with 90-fold increased activity as compared to the wild-type enzyme were created. In a preparative synthesis of poly(D,D-lactide) the mutants greatly improved the rate and the degree of polymerization.

Graphical abstract: Rational redesign of Candida antarcticalipase B for the ring opening polymerization of d,d-lactide

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Article information

DOI
https://doi.org/10.1039/C1CC10865D
Article type
Communication
Submitted
14 Feb 2011
Accepted
04 May 2011
First published
23 May 2011

Chem. Commun., 2011,47, 7392-7394

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Rational redesign of Candida antarcticalipase B for the ring opening polymerization of D,D-lactide

M. Takwa, M. W. Larsen, K. Hult and M. Martinelle, Chem. Commun., 2011, 47, 7392 DOI: 10.1039/C1CC10865D

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