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Related Experiment Videos

Enantioselective biotransformations using rhodococci.

T M Beard1, M I Page

  • 1Department of Chemical and Biological Sciences, University of Huddersfield, Queensgate, UK.

Antonie Van Leeuwenhoek
|March 9, 1999
PubMed
Summary

This study highlights a Rhodococcus strain

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Area of Science:

  • Biocatalysis and Enzyme Engineering
  • Organic Chemistry
  • Microbial Biotechnology

Background:

  • Enzymes and whole cells are crucial for enantioselective biotransformations.
  • Efficient methods for producing enantiomerically pure compounds are in high demand.
  • Biocatalysis offers a sustainable alternative to traditional chemical synthesis.

Purpose of the Study:

  • To investigate the potential of a Rhodococcus strain for enantioselective biotransformation.
  • To evaluate the strain's nitrile hydratase and amidase activities.
  • To demonstrate the conversion of racemic alpha-amino amides to (S) alpha-amino acids.

Main Methods:

  • Screening of microbial strains for specific enzymatic activities.
  • Enzymatic assays to determine nitrile hydratase and amidase activity.
  • Bioconversion experiments using racemic alpha-amino amides and the selected Rhodococcus strain.

Main Results:

  • A Rhodococcus strain exhibiting both nitrile hydratase and amidase activity was identified.
  • The strain efficiently converted racemic alpha-amino amides to (S) alpha-amino acids with >98% enantiomeric excess (ee).
  • The enantioselective biotransformation was time-independent and effective for various alpha-substituents.

Conclusions:

  • The Rhodococcus strain is a potent biocatalyst for the enantioselective synthesis of (S) alpha-amino acids.
  • The high enantioselectivity and efficiency make this method suitable for industrial applications.
  • Understanding the pH-dependence suggests the substrate binds to the amidase enzyme in its neutral form.

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