Tyrosol is a phenolic compound found in olive oil and wines. The health benefits of tyrosol have attracted considerable attention. Because the tyrosol extraction from plants poses a major obstacle, biosynthesizing this compound using microbial hosts is of interest. In this study, the phenylpyruvate decarboxylase gene ARO10 and the aromatic amino acid aminotransferase gene ARO8 were introduced into Escherichia coli to generate two recombinant tyrosol producers. Deleting the prephenate dehydratase gene pheA and the phenylacetaldehyde dehydrogenase gene feaB improved the tyrosol production. Under the optimal fermentation conditions, a recombinant strain overexpressing ARO10 gene produced 4.15 mM tyrosol from 1% (w/v) glucose during a 48 h shake flask cultivation. Furthermore, when tyrosine was used as the substrate, the recombinant strain co-overexpressing ARO8 and ARO10 genes displayed a higher tyrosol yield, in which 8.71 mM tyrosol was produced from 10 mM tyrosine. This investigation suggests that microbial tyrosol production has application potential.

In this study, we investigated the effects of the different critical genes in the three modules on tyrosol production in Escherichia coli. Coexpression of the yahK and ARO10 genes increased the yield of tyrosol by 10% compared to that of the control. Tyrosol production by E. coli BFPT1 and E. coli BFPA1 was higher by 15.0% and 17.8% than that by the control, respectively, via coordinated expression of key genes from modules 2 and 3. The tyrosol yield of E. coli BFPE2 was 58.3% higher than that of the control (reaching 5.72 mM) when the expression levels of the key genes aroA and tyrA* from module 2 were balanced. The tyrosol yield of E. coli BFPG1 was increased by 52.6% (reaching 5.8 mM) compared to the control via coexpression of modules 1, 2, and 3. This work suggested that microbial production of tyrosol in E. coli has potential for industrial applications.