Bioconversion of L-Tyrosine into Coumaric Acid by Tyrosine Ammonia-Lyase Heterologue of Produced in KT2440.

Curr Issues Mol Biol

Biological Chemistry Laboratory, Chemistry Institute, Pontificia Universidad Católica de Valparaíso, Valparaíso 2340025, Chile.

Published: September 2024

AI Article Synopsis

  • Coumaric acid is important for various industries but traditional production methods are not very efficient.
  • This study explores improving coumaric acid production by using a genetically engineered strain of bacteria (KT2440) that expresses a specific enzyme (TAL) to convert L-tyrosine into coumaric acid.
  • The researchers achieved successful integration of the TAL gene and optimized production through a pH shift during fermentation, resulting in a significant yield of coumaric acid (1381 mg/L), showcasing the potential for sustainable production methods.

Article Abstract

Coumaric acid (-CA) is a valuable compound with applications in food additives, cosmetics, and pharmaceuticals. However, traditional production methods are often inefficient and unsustainable. This study focuses on enhancing -CA production efficiency through the heterologous expression of tyrosine ammonia-lyase (TAL) from in KT2440. TAL catalyzes the conversion of L-tyrosine into -CA and ammonia. We engineered KT2440 to express TAL in a fed-batch fermentation system. Our results demonstrate the following: (i) successful integration of the TAL gene into KT2440 and (ii) efficient bioconversion of L-tyrosine into -CA (1381 mg/L) by implementing a pH shift from 7.0 to 8.5 during fed-batch fermentation. This approach highlights the viability of KT2440 as a host for TAL expression and the successful coupling of fermentation with the pH-shift-mediated bioconversion of L-tyrosine. Our findings underscore the potential of genetically modified for sustainable -CA production and encourage further research to optimize bioconversion steps and fermentation conditions.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11430055PMC
http://dx.doi.org/10.3390/cimb46090603DOI Listing

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