Abstract
In this paper an explanation is given of howPseudomonas (P.) chlororaphis B23 can accumulate so much acrylamide of such high purity. One reason is thatP. chlororaphis B23 exhibits much greater nitrile hydratase activity than amidase activity; the rate of formation of acrylamide through the nitrile hydratase reaction is at least 4000 times higher than its breakdown catalyzed by amidase. Furthermore, acrylonitrile, a powerful nucleophilic reagent, inactivates the active thiol residue of the amidase, whereas nitrile hydratase is not so susceptible to acrylonitrile. Thus acrylamide is produced but not transformed further. In addition, the nitrile hydratase purified fromP. chlororaphis B23 exhibits high resistance to a high concentration of acrylamide. Some other explanations, and the results of evaluation of theP. chlororaphis B23 enzyme as a catalyst for the production of acrylamide are discussed.
Published Version
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