An esterase activity which hydrolyses palmitoyl-CoA was found in the membrane fraction of Acinetobacter calcoaceticus 69/V. Other tested strains of Acinetobacter also possessed this enzyme activity. The esterase is constitutive, fully active on the surface of intact cells and located on the outer me
Outer membrane vesiculation of acinetobacter calcoaceticus
โ Scribed by P. Borneleit; H.-P. Kleber; H. Binder
- Publisher
- John Wiley and Sons
- Year
- 1990
- Tongue
- English
- Weight
- 450 KB
- Volume
- 10
- Category
- Article
- ISSN
- 0138-4988
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๐ SIMILAR VOLUMES
Cells of Acinetobacter calcoaceticus strain 69-V contain an aminopeptidase that cleaves L-leucine amide, leucylglycine or leucine hydrazide with high efficiency. Leucine 4-nitroanilide and alanine hydrazide are hydrolyzed to less than 0.1 % and 1 %, resp. of leucine amide. Grown on acetate-NH; medi
The localization of hydrolytic enzymes, phosphatase, estcrase, lipase and palmitoyl-CoA hydrolase was analysed in the cytosol, cytoplasmic membrane, periplasmic fraction, outer membrane and culture supernatant in dependence on the growth rate of the bacteria. The unspecific phosphatase was found to
The hydrocarbon met a bol izi ng A cinetobacter calcoaceticus sp. 2CA2 reduces the surface tension of the culture broth during growth on liquid hydrocarbons. This activity, which is not evident during growth on soluble substrates, is associated with the whole cells. Removing the cells from the cultu