Efficient biocatalytic production of d-4-hydroxyphenylglycine by whole cells of recombinant Ralstonia pickettii |
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Authors: | H. Yu S. Yang W. Jiang Y. Yang |
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Affiliation: | 1.Laboratory of Molecular Microbiology, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences,Chinese Academy of Sciences,Shanghai,P.R. China;2.Graduate University of the Chinese Academy of Sciences,Beijing,P.R. China |
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Abstract: | The first establishment of a homologous expression system in the host Ralstonia pickettii CGMCC1596 using the compatible broad-host-range plasmid pWB5 is described. When whole cells of the recombinant strain R. pickettii MMYY01 (CGMCC1596/pYY05) were used as the biocatalyst to transform dl-4-hydroxyphenylhydantoin (dl-HPH) to d-4-hydroxyphenylglycine (d-HPG), the conversion rate reached 94 % in first 9 h, at a production rate of 2.8 g L−1 h−1, with the rapid reduction of the intermediate [N-carbamoyl-2-(4-hydroxyphenyl)glycine], compared with 80 % in >50 h at a rate of 0.5 g L−1 h−1 for the CGMCC1596. The stability of the recombinant plasmid pYY05 is sufficient for its application in industrial batch fermentation. An alternative strategy for the conversion of dl-HPH to d-HPG by resting CGMCC1596 cells and heterologous DCase expressed by E. coli is discussed. |
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