Etude de L’Acétonitrilase D’une Souche deBrevibacterium
- 1 November 1977
- journal article
- research article
- Published by Oxford University Press (OUP) in Agricultural and Biological Chemistry
- Vol. 41 (11) , 2183-2191
- https://doi.org/10.1080/00021369.1977.10862833
Abstract
The acetonitrilase from Brevibacterium R 312 has an activity between pH 5 and 10, with an optimum pH of 7, the optimum temperature is between 30° and 35°C. It is a thermolabile enzyme and the temperature denaturation starts at 35°C. The Michaelis constant is near 2,5.10−2 m. The enzyme is localized in the 180 000 g supernatant. It is an non adaptative enzyme.This publication has 2 references indexed in Scilit:
- In vivo and enzymatic conversion of toyocamycin to sangivamycin by Streptomyces rimosusArchives of Biochemistry and Biophysics, 1974
- The Aliphatic Amidases of Pseudomonas aeruginosaPublished by Elsevier ,1969