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Bacterial short-chain acyl-CoA oxidase: production, purification and characterization

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Abstract

An Arthrobacter nicotianae strain has been found to produce an inducible acyl coenzyme A (CoA) oxidase. Nine times more butyryl-CoA oxidase activity, compared to palmitoyl-CoA oxidase, was found in the cell extract. The addition of flavin adenine dinucleotide (FAD) caused an increase in acyl-CoA oxidase activity and thermal stability. The purified enzyme exhibited a relative molecular mass of 50 000 on sodium dodecyl sulphate-polyacrylamide gel electrophoresis and 100 000 under non-denaturing conditions. Acyl-CoA oxidase from Arthrobacter nicotianae is highly specific towards short-chain fatty acids. The fastest O2 uptake was observed with butyryl-CoA as substrate. The enzyme is inhibited by silver and mercury salts.

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To Professor Dr. Helmut Simon for his 65th birthday

Correspondence to: H. Sztajer

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Sztajer, H., Wagner, G. & Schmid, R.D. Bacterial short-chain acyl-CoA oxidase: production, purification and characterization. Appl Microbiol Biotechnol 39, 708–713 (1993). https://doi.org/10.1007/BF00164454

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  • DOI: https://doi.org/10.1007/BF00164454

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