The nitrilase of Rhodococcus rhodochrous performs a one-step biotransformation of nitriles to their corresponding carboxylic acids. Application of a direct electric current moves the charged carboxylic acid towards an anode, across an anion exchange membrane, into a separate compartment. Cells encapsulated within alginate beads (2.9 mm diameter) for protection against the current biotransformed benzonitrile to benzoic acid with a 26% reduction in the biotransformation rate, from 0.054 mmol/min/g dcw with free cells to 0.040 mmol/min/g dcw with immobilised cells. When the electric current was applied, the biotransformation rate increased to 0.047 mmol/min/g dcw and product recovery increased from 19% to 79%
Nitrile hydrolysing enzymes have found wide use in the pharmaceutical industry for the production of...
The biotransformation of poorly water-soluble aromatic dinitriles is of scientific and industrial in...
SIGLEAvailable from British Library Document Supply Centre- DSC:DX187056 / BLDSC - British Library D...
The simultaneous enhancement of biotransformation coupled to product recovery, purification and conc...
The free and agar immobilized cells of Nocardia globerula NHB-2 having nitrilase (EC 3.5.5.1) a...
Whole cells of the bacterium Rhodococcus rhodochrous LL100-21, which had been grown on benzonitrile ...
The cyanomethyl benzonitrile compounds used for this study contain two cyano groups: a -CH(2)CN side...
Whole cells of Rhodococcus equi A4, a producer of nitrile hydratase and amidase activities, were imm...
A recombinant E. coli, expressing nitrilase from Acidovorax facilis 72W with dual-site expression pl...
SIGLEAvailable from British Library Document Supply Centre- DSC:DX184035 / BLDSC - British Library D...
Nitrilases are enzymes which catalyze the hydrolysis of nitriles to corresponding carboxylic acids. ...
International audienceTwo different electrochemical reduction processes for the removal of dimetrida...
Rhodococcus rhodochrous NCIMB 11216 grows on propionitrile or benzonitrile as the sole source of car...
The biohydration of acrylonitrile, propionitrile and benzonitrile catalysed by the NHase activity co...
AbstractNitrile metabolizing enzymes are of great industrial interest for the selective bio-transfor...
Nitrile hydrolysing enzymes have found wide use in the pharmaceutical industry for the production of...
The biotransformation of poorly water-soluble aromatic dinitriles is of scientific and industrial in...
SIGLEAvailable from British Library Document Supply Centre- DSC:DX187056 / BLDSC - British Library D...
The simultaneous enhancement of biotransformation coupled to product recovery, purification and conc...
The free and agar immobilized cells of Nocardia globerula NHB-2 having nitrilase (EC 3.5.5.1) a...
Whole cells of the bacterium Rhodococcus rhodochrous LL100-21, which had been grown on benzonitrile ...
The cyanomethyl benzonitrile compounds used for this study contain two cyano groups: a -CH(2)CN side...
Whole cells of Rhodococcus equi A4, a producer of nitrile hydratase and amidase activities, were imm...
A recombinant E. coli, expressing nitrilase from Acidovorax facilis 72W with dual-site expression pl...
SIGLEAvailable from British Library Document Supply Centre- DSC:DX184035 / BLDSC - British Library D...
Nitrilases are enzymes which catalyze the hydrolysis of nitriles to corresponding carboxylic acids. ...
International audienceTwo different electrochemical reduction processes for the removal of dimetrida...
Rhodococcus rhodochrous NCIMB 11216 grows on propionitrile or benzonitrile as the sole source of car...
The biohydration of acrylonitrile, propionitrile and benzonitrile catalysed by the NHase activity co...
AbstractNitrile metabolizing enzymes are of great industrial interest for the selective bio-transfor...
Nitrile hydrolysing enzymes have found wide use in the pharmaceutical industry for the production of...
The biotransformation of poorly water-soluble aromatic dinitriles is of scientific and industrial in...
SIGLEAvailable from British Library Document Supply Centre- DSC:DX187056 / BLDSC - British Library D...