Cloning and expression of an ether-bond-cleaving enzyme involved in the metabolism of polyethylene glycol
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Updated: Aug 15, 2026

Depolymerizable Olefinic Polymers Based on Fused-Ring Cyclooctene Monomers
Published on: December 16, 2022
Manabu Yamashita1, Akio Tani, Fusako Kawai
1Research Institute for Bioresources, Okayama University, 2-20-1 Chuo, Kurashiki, Okayama 710-0046, Japan.
Abstract:
A gene encoding an ether-bond-cleaving enzyme, diglycolic acid dehydrogenase (DGADH) from polyethylene glycol-utilizing Pseudonocardia sp. strain K1, was cloned and expressed in Escherichia coli. The deduced amino acid sequence had a high homology with superoxide dismutases (SODs) from various bacteria. The recombinant protein showed the same activities as those of DGADH from Pseudonocardia sp. strain K1, namely, SOD activity and ether-bond-cleaving activity.
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