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Abstract Rhodococcus erythropolis AJ270 metabolizes a wide range of nitriles via the two-step nitrile hydratase/amidase pathway. In this study, an amidase gene from R. erythropolis AJ270 was cloned and expressed in Escherichia coli BL21 (DE3). The activity reached the highest level of 22.04 U/ml in a complex auto-inducing medium using a simplified process of fermentation operation. The ...
An acetonitrile-utilising bacterium AJ270 has been isolated from soil, identified as a Rhodococcus sp. and shown to be distinct from all the recognised species of the genus. It grows well on 32 of 36 aliphatic, aromatic and hetero-aromatic nitriles tested and is capable of rapid growth on high concentrations (0.25-0.38 M) of acetonitrile, benzonitrile and 3-cyanopyridine. The nitrile ...
Nitrile hydratase (NHase, EC 4.2.1.84) from Rhodococcus sp. AJ270 was purified with 23.96% yield after sonication, ammonium sulfate fractionation, ion exchange, hydrophobic and gel-filtration column ...
The nitrile hydratase of Rhodococcus AJ270 is stable on storage for 18 months at − 20° C, has activity against a very broad range of nitriles and dinitriles and is able to catalyse regio-specific and stereo-specific nitrile biotransformations.
Rhodococcus erythropolis AJ270 metabolizes a wide range of nitriles via the two-step nitrile hydratase/amidase pathway. In this study, an amidase gene from R. erythropolis AJ270 was cloned and expressed in Escherichia coli BL21 (DE3). The activity reached the highest level of 22.04 U/ml in a complex auto-inducing medium using a simplified process of fermentation operation. The recombinant ...
An acetonitrile-utilising bacterium AJ270 has been isolated from soil, identified as a Rhodococcus sp. and shown to be distinct from all the recognised species of the genus. It grows well on 32 of 36 aliphatic, aromatic and hetero-aromatic nitriles tested and is capable of rapid growth on high concentrations (0.25-0.38 M) of acetonitrile, benzonitrile and 3-cyanopyridine. The nitrile hydratase ...
The crystal structure of Fe-type nitrile hydratase from Rhodococcus erythropolis AJ270 was determined at 1.3 Å resolution. The two cysteine residues (αCys 112 and αCys 114) equatorially coordinated to the ferric ion were post-translationally modified to cysteine sulfinic acids. A glutamine residue (αGln 90) in the active center gave double conformations. Based on the interactions among the ...
Abstract The nitrile metabolising strains AJ270, AJ300 and AJ115 were isolated from the same location. The strains have very similar nitrile metabolising profiles. Sequencing of the 16S rRNA gene indicates that strains AJ270 and AJ300 are novel strains of Rhodococcus erythropolis while strain AJ115 is a novel Microbacterium strain very closely related to Microbacterium oxydans and ...
Rhodococcus sp. AJ270, a nitrile hydratase/amidase-containing microorganism, were immobilized in alginate capsules. The influences of the bead size and the crosslinking agent on morphology and the biocatalytic activity of the cells were examined. In the presence of an organic co-solvent, such as methanol or acetone (5%), the encapsulated Rhodococcus sp. AJ270 has been found to catalyze ...
Abstract Rhodococcus sp. AJ270 is an efficient whole-cell system able to catalyze the stereoselective conversions of racemic α-substituted phenylacetonitriles and amides under very mild conditions into enantiopure carboxylic acids and derivatives. The nitrile hydratase involved generally has a broad substrate spectrum against phenylacetonitriles irrespective of the electronic nature of the α ...