Title of article :
Resolution of (R, S)-ethyl-2-(4-hydroxyphenoxy) propanoate using lyophilized mycelium of Aspergillus oryzae WZ007
Author/Authors :
Zheng، نويسنده , , Jian-Yong and Wu، نويسنده , , Jiayu and Zhang، نويسنده , , Yinjun and Wang، نويسنده , , Zhao، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2013
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 0.5 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.
Keywords :
(R)-Ethyl-2-(4-hydroxyphenoxy) propanoate , Lipase , RESOLUTION , Enantioselective hydrolysis , Aspergillus oryzae
Journal title :
Journal of Molecular Catalysis B Enzymatic
Journal title :
Journal of Molecular Catalysis B Enzymatic