Enzymatic Degradation of Ether-Alcohol Compounds

概要

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Alcaligenes sp. PE18,isolated as a strain utilizing polyethylene glycol 400,exhibited good growth with tri-, tetra-, and poly-ethylene glycols, but not with ethylene glycol, methoxy or ethoxy acetic acids, or ethanol. The dehydrogenase with activity towards ether-alcohols was purified from strain PE18 by ammonium sulfate fractionation and chromatographies on DEAE-cellulose, 10-Carboxydecyl Sephacryl S200,and Sephacryl S200 columns. It gave a single band of protein and enzyme activity on disc-gel electrophoresis, and required FAD, FMN, or NAD as a cofactor. The dehydrogenase could also link with phenazine methosulfate or 2,6-dichlorophenolindophenol, and catalyzed the formation of a 2,4-dinitrophenylhydrazine-positive compound, possibly an aldehyde. The enzyme has a wide substrate specificity with activity towards ethylene glycol-, diethylene glycol-, triethylene glycol-monoethyl and -monobutyl ethers, but not towards ethylene glycol, 1,3-propanediol, or n-alcohols.The reaction for cleavage of the ether bond was also investigated with cell-free extracts of mutant strain MA11 derived from Alcaligenes sp. PE18. The mutant could utilize methoxy and ethoxy acetic acids and split their ether linkages with consumption of oxygen in the presence of phenazine methosulfate.
社団法人日本生物工学会の論文
1981-10-25