Involvement of catalytic amino acid residues in enzyme-catalyzed polymerization for the synthesis of polyesters

Y. Suzuki, S. Taguchi, T. Saito, K. Toshima, S. Matsumura, Y. Doi

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

Recently, a variety of aliphatic polyesters have been synthesized using hydrolases such as lipases and PHB depolymerases, and the reaction mechanism for these enzyme-catalyzed polymerization has been discussed. In this paper, we have studied the involvement of the catalytic amino acid residues of the hydrolase in enzyme-catalyzed polymerization with an extracellular PHB depolymerase from Alcaligenes faecalis T1. A wild-type PHB depolymerase and three kinds of site-specific mutants (catalytic amino acids were substituted) were prepared and their polymerization activities for the ring-opening polymerization of (R)-β-butyrolactone (BL) were compared. BL was polymerized at 80 °C in bulk by the wild-type enzyme to yield polymers consisting of cyclic and linear structures in a high monomer conversion. In contrast, none of the mutant enzymes showed obvious polymerization activity. These results have clearly demonstrated that the catalytic triad is indeed responsible for the enzyme-catalyzed polymerization of BL.

Original languageEnglish
Pages (from-to)541-544
Number of pages4
JournalBiomacromolecules
Volume2
Issue number2
DOIs
Publication statusPublished - 2001 Aug 15

ASJC Scopus subject areas

  • Bioengineering
  • Biomaterials
  • Polymers and Plastics
  • Materials Chemistry

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