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

Chem Commun (Camb). 2011 Jul 14;47(26):7392-4. doi: 10.1039/c1cc10865d. Epub 2011 May 23.

Abstract

Based on molecular modelling, the enzyme Candida antarctica lipase 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Catalytic Domain
  • Dioxanes / chemistry*
  • Fungal Proteins
  • Lipase / chemistry
  • Lipase / genetics*
  • Lipase / metabolism*
  • Models, Molecular
  • Mutagenesis, Site-Directed / methods*
  • Polymerization*

Substances

  • Dioxanes
  • Fungal Proteins
  • dilactide
  • Lipase
  • lipase B, Candida antarctica