| Abstract [eng] |
Investigation of Pyridine Degradation in Rhodococcus rhodochorus PY11 Strain Rhodococcus strains are capable of degrading wide range of natural and xenobiotic compounds due to their variety of catabolic enzymes. The aim of this work was to investigate the genes and enzymes responsible for degradation of pyridine in Rhodococcus rhodochrous PY11 strain. Firstly, we were trying to determine if pyridine inducible protein – hypothetical monooxygenase initiates first step of pyridine ring cleavage. E.coli and R. erythropolis SQ1 cells were transformed with recombinant plasmids carrying hypothetical monooxygenase and FMN reductase genes. The experiment of pyridine bioncorversion in E.coli and R. erythropolis SQ1 cells showed that they are uncapable to degrade pyridine. The results suggest that hypothetical monooxygenase is most likely not involved in initial reaction of pyridine cleavage. Pyridine inducable amidohydrolase from Rhodococcus rhodochrous PY11 strain was investigated as well. Recombinant amidohydrolase was expressed in E.coli and purified. Purified enzyme was added to reaction mixtures with different substrates. Unfortunately no products of reaction were obtained and hypothetical amidohydrolase function in pyridine degradation remains unclear. It was also revealed that pyridine activates expression of at least 21 of 22 investigated genes that might be involved in degradation of pyridine. |
