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

研究成果: Article査読

23 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)541-544
ページ数4
ジャーナルBiomacromolecules
2
2
DOI
出版ステータスPublished - 2001 8月 15

ASJC Scopus subject areas

  • バイオエンジニアリング
  • 生体材料
  • ポリマーおよびプラスチック
  • 材料化学

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