Enantioselective transesterification using immobilized <Emphasis Type="Italic">Aspergillus oryzae</Emphasis> overexpressing lipase |
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Authors: | M?Kaieda M?Nagayoshi S?Hama A?Kondo Email author" target="_blank">H?FukudaEmail author |
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Institution: | (1) Division of Molecular Science, Graduate School of Science and Technology, Kobe University, 1-1 Rokkoudai, Nada, Kobe, 657-8501, Japan;(2) Department of Chemical Science and Engineering, Faculty of Engineering, Kobe University, 1-1 Rokkoudai, Nada, Kobe, 657-8501, Japan |
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Abstract: | In the present study, we used gene manipulation to construct a recombinant Aspergillus oryzae strain overexpressing lipase and investigated its application to the optical resolution of chiral compounds. A. oryzae niaD300, which was derived from the wild-type strain RIB40, was used as the host strain. The tglA gene, which encodes a triacylglycerol lipase, was cloned from the A. oryzae niaD300 chromosomal genome, then reintroduced, with and without a secretion-signal sequence, into the genome and expressed under the control of the improved glaA promoter of plasmid pNGA142. The resulting recombinant strain overexpressing A. oryzae lipase was immobilized within biomass-support particles and used as a whole-cell biocatalyst. The immobilized lipase-overexpressing strain with secretion-signal sequence showed high activity and was used to selectively synthesize (R)-1-phenylethyl acetate from (RS)-1-phenylethanol and vinyl acetate. After 48 h reaction at 30°C with molecular sieve 4A, the yield and enantiomeric excess (%ee) of (R)-1-phenylethyl acetate reached approximately 90 and 95%ee, respectively. The whole-cell biocatalyst for optical resolution of chiral compounds produced in this study maintained its activity over 25 batch-reaction cycles. |
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