Involvement of Catalytic Amino Acid Residues in Enzyme-Catalyzed Polymerization for the Synthesis of Polyesters
- 6 April 2001
- journal article
- research article
- Published by American Chemical Society (ACS) in Biomacromolecules
- Vol. 2 (2) , 541-544
- https://doi.org/10.1021/bm015508o
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.Keywords
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