Tyrosine phenol-lyase (TPL) is a valuable and cost-effective biocatalyst for the biosynthesis of L-tyrosine and its derivatives, which are valuable intermediates in the pharmaceutical industry. A TPL from Morganella morganii (Mm-TPL) was overexpressed in Escherichia coli and characterized. Mm-TPL was determined as a homotetramer with molecular weight of 52 kDa per subunit. Its optimal temperature and pH for β-elimination of L-tyrosine were 45 °C and pH 8.5, respectively. Mm-TPL manifested strict substrate specificity for the reverse reaction of β-elimination and ortho- and meta-substituted phenols with small steric size were preferred substrates. The enzyme showed excellent catalytic performance for synthesis of L-tyrosine, 3-fluoro-L-tyrosine, and L-DOPA with a yield of 98.1%, 95.1%, and 87.2%, respectively. Furthermore, the fed-batch bioprocess displayed space-time yields of 9.6 g L⁻¹ h⁻¹ for L-tyrosine and 4.2 g L⁻¹ h⁻¹ for 3-fluoro-L-tyrosine with a yield of 67.4 g L⁻¹ and 29.5 g L⁻¹, respectively. These results demonstrated the great potential of Mm-TPL for industrial application.

酪氨酸苯酚裂解酶（TPL）是用于L-酪氨酸及其衍生物生物合成的有价值和具有成本效益的生物催化剂，L-酪氨酸及其衍生物是制药工业中的重要中间体。来自摩根氏菌的TPL （Mm -TPL）在大肠杆菌中过表达并进行了表征。Mm- TPL被确定为同四聚体，分子量为每个亚基52kDa。消除β-酪氨酸的最佳温度和pH分别为45°C和pH 8.5。Mm -TPL对β消除和邻位和间位的逆反应表现出严格的底物特异性具有小的空间尺寸的取代的苯酚是优选的底物。该酶在合成L-酪氨酸，3-氟-L-酪氨酸和L-DOPA方面显示出优异的催化性能，产率分别为98.1％，95.1％和87.2％。此外，补料分批生物过程显示9.6克L-时空产率^-1  ħ ^-1对L-酪氨酸和4.2克L- ^-1  ħ ^-1 3-氟-L-酪氨酸与67.4克L-产率^-分别为1和29.5g L ^-1。这些结果证明了Mm -TPL在工业应用中的巨大潜力。