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Resolution of (R,S)-ethyl-2-(4-hydroxyphenoxy) propanoate using lyophilized mycelium ofAspergillus oryzaeWZ007

Authors
Journal
Journal of Molecular Catalysis B Enzymatic
1381-1177
Publisher
Elsevier
Publication Date
Volume
97
Identifiers
DOI: 10.1016/j.molcatb.2013.07.016
Keywords
  • (R)-Ethyl-2-(4-Hydroxyphenoxy) Propanoate
  • Aspergillus Oryzae
  • Lipase
  • Resolution
  • Enantioselective Hydrolysis

Abstract

Abstract The mycelium of Aspergillus oryzae WZ007 was successfully developed to kinetic resolution of (R, S)-ethyl-2-(4-hydroxyphenoxy) propanoate ((R, S)-EHPP) for production of (R)-ethyl-2-(4-hydroxyphenoxy) propanoate ((R)-EHPP). The key biocatalytic process parameters (pH, temperature, rotation speed and substrate concentration) were optimized. Under the optimum conditions, the optical purity of (R)-EHPP was improved up to >99% when the conversion was above 49%. A. oryzae WZ007 whole-cell lipase exhibited high reaction capacity, enantioselectivity and good reusability. The tolerable substrate concentration was 0.5mol/L, and dry mycelium of A. oryzae WZ007 maintains over 80% of its initial activity after eight repeating cycles. Therefore the enzymatic preparation of (R)-EHPP route was suitable for industrial application.

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