Expression of acylamidase gene in Rhodococcus erythropolis strains

The expression of a new acylamidase gene from R. erythropolis TA37 was studied in Rhodococcus erythropolis strains. This acylamidase, as a result of its unique substrate specificity, can hydrolyse N-substituted amides (4′-nitroacetanilide, N-isopropylacrylamide, N′N-dimethylaminopropylacrylamide). A...

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Bibliographic Details
Published in:Russian journal of genetics 2014, Vol.50 (9), p.1003-1007
Main Authors: Lavrov, K. V, Novikov, A. D, Ryabchenko, L. E, Yanenko, A. S
Format: Article
Language:English
Subjects:
amidase
amides
Animal Genetics and Genomics
Biomedical and Life Sciences
Biomedicine
genes
Human Genetics
Microbial Genetics and Genomics
promoter regions
Rhodococcus erythropolis
Short Communications
substrate specificity
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Summary:The expression of a new acylamidase gene from R. erythropolis TA37 was studied in Rhodococcus erythropolis strains. This acylamidase, as a result of its unique substrate specificity, can hydrolyse N-substituted amides (4′-nitroacetanilide, N-isopropylacrylamide, N′N-dimethylaminopropylacrylamide). A new expression system based on the use of the promoter region of nitrile hydratase genes from R. rhodochrous M8 was created to achieve constitutive synthesis of acylamidase in R. erythropolis cells. A fourfold improvement in the acylamidase activity of recombinant R. erythropolis cells as compared with the parent wild-type strain was obtained through the use of the new expression system.
ISSN:1022-7954
1608-3369
DOI:10.1134/S1022795414090087