ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • P. chlororaphis B23  (1)
  • 1985-1989  (1)
  • 1980-1984
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 45 (1989), S. 1066-1070 
    ISSN: 1420-9071
    Keywords: Acrylamide ; nitrile hydratase ; P. chlororaphis B23
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary 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.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...