Resolution of (R, S)-ethyl-2-(4-hydroxyphenoxy) propanoate using lyophilized mycelium of Aspergillus oryzae WZ007

Abstract

• The kinetic resolution of ( R , S )-EHPP by Aspergillus oryzae WZ007 lipase is proposed. • The key biocatalytic process parameters were optimized. • The optical purity of ( R )-EHPP was up to >99% and the conversion was above 49%. 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 0.5 mol/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.