Production of L-tyrosine using tyrosine phenol-lyase by whole cell biotransformation approach.

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ID: 63938
2019
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Abstract
L-tyrosine is an amino acid that has been widely used in the food, agriculture and pharmaceutical industries. In order to screen a tyrosine phenol-lyase (TPL) with excellent catalytic performance for L-tyrosine production, TPL genes from Citrobacter freundii (CfTPL), Erwinia herbicola (EhTPL) and Rhodobacter capsulatus (TutA) were codon-optimized and overexpressed in Escherichia coli. The results showed that EhTPL had the highest whole cell catalysis activity and tyrosine yield (3-fold that of CfTPL). The results of RT-qPCR and a stability analysis also revealed that EhTPL had a higher transcriptional level in whole cell catalysis, while CfTPL possessed greater stability. Conditions for the production by whole cell transformation were optimized in terms of reaction conditions and fed-batch strategy. Finally, the maximum production was obtained with a titer of 48.5 g·L by intermittent feeding with a conversion ratio of 75%.
Reference Key
xu2019productionenzyme Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Xu, Sha;Zhang, Yu;Li, Youran;Xia, Xiaole;Zhou, Jingwen;Shi, Guiyang;
Journal Enzyme and microbial technology
Year 2019
DOI
S0141-0229(19)30168-1
URL
Keywords
erwinia herbicola l-tyrosine tyrosine phenol-lyase whole cell biotransformation

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