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Biotransformations with peroxidases

W Adam1, M Lazarus, C R Saha-Möller

  • 1Institute of Organic Chemistry, University of Würzburg, Germany. Adam@chemie.uni-wuerzburg.de

Advances in Biochemical Engineering/Biotechnology
|February 6, 1999
PubMed
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Enzymes, as chiral catalysts, enable the synthesis of optically active compounds. This review highlights recent advances in peroxidase-catalyzed reactions for preparing enantiomerically pure molecules, crucial for pharmaceuticals and agrochemicals.

Area of Science:

  • Biocatalysis
  • Organic Chemistry
  • Green Chemistry

Background:

  • Enzymes are chiral catalysts essential for asymmetric synthesis.
  • Producing enantiomerically pure compounds is vital for pharmaceuticals and agrochemicals.
  • Developing environmentally friendly synthetic processes remains a key challenge.

Purpose of the Study:

  • To review recent advances in peroxidase-catalyzed transformations.
  • To emphasize the preparative applications of these enzymatic reactions.
  • To showcase enzymes as sustainable catalysts for asymmetric synthesis.

Main Methods:

  • Summarizing literature on peroxidase-catalyzed reactions.
  • Focusing on selective oxidations of electron-rich substrates.
  • Highlighting enantioselective synthesis of valuable compounds.

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Main Results:

  • Peroxidases catalyze diverse selective oxidations, including hydroxylation, oxyfunctionalization, epoxidation, and halogenation.
  • Enzymatic reduction of hydroperoxides offers enantioselective pathways.
  • Recent advances demonstrate significant progress in preparative applications.

Conclusions:

  • Enzymes offer an environmentally acceptable approach to synthesizing enantiomerically pure compounds.
  • Peroxidase-catalyzed reactions provide efficient and selective methods for organic synthesis.
  • The review underscores the growing importance and applicability of biocatalysis in industry.