BACTERIAL SHORT-CHAIN ACYL-COA OXIDASE - PRODUCTION, PURIFICATION ANDCHARACTERIZATION

Citation
H. Sztajer et al., BACTERIAL SHORT-CHAIN ACYL-COA OXIDASE - PRODUCTION, PURIFICATION ANDCHARACTERIZATION, Applied microbiology and biotechnology, 39(6), 1993, pp. 708-713
Citations number
22
Categorie Soggetti
Biothechnology & Applied Migrobiology
ISSN journal
01757598
Volume
39
Issue
6
Year of publication
1993
Pages
708 - 713
Database
ISI
SICI code
0175-7598(1993)39:6<708:BSAO-P>2.0.ZU;2-D
Abstract
An Arthrobacter nicotianae strain has been found to produce an inducib le acyl coenzyme A (CoA) oxidase. Nine times more butyryl-CoA oxidase activity, compared to palmitoyl-CoA oxidase, was found in the cell ext ract. The addition of flavin adenine dinucleotide (FAD) caused an incr ease in acyl-CoA oxidase activity and thermal stability. The purified enzyme exhibited a relative molecular mass of 50000 on sodium dodecyl sulphate-polyacrylamide gel electrophoresis and 100000 under non-denat uring conditions. Acyl-CoA oxidase from Arthrobacter nicotianae is hig hly specific towards short-chain fatty acids. The fastest O2 uptake wa s observed with butyryl-CoA as substrate. The enzyme is inhibited by s ilver and mercury salts.