L-tyrosine, one of the non-essential amino acids for human, is an important precursor for numerous high-value chemical products, such as phenylpropanoids. L-tyrosine is widely used in food, chemical, feed and pharmaceutical industries as the nutritional supplements and the raw materials for peptide hormones, antibiotics, L-DOPA, melanin, p-hydroxycinnamic acid. The tyrosine phenol lyase (TPL) derived from Rhodobacter capsulatus was expressed in Escherichia coli (named pET28a RcTPL) to promote the efficient production of L-tyrosine. Optimization of induction conditions, determination of enzyme activity and analysis of enzymatic properties were performed. The optimum catalytic pH of TPL determined by purified RcTPL was 8.5 and the optimum catalytic temperature was determined to be 40 ℃. Furthermore, enzyme activity of purified enzyme and whole-cell catalysis were analyzed. The enzyme activity and the specific enzyme activity of purified RcTPL was 0.29 U/mL and 0.29 U/mg, respectively. The enzyme activity of whole-cell catalysis was 0.41 U/g, while the titer of L-tyrosine was 0.30 g/L after reaction for 10 hours. The results showed that TPL from Rhodobacter capsulatus was successfully expressed in E. coli, which laid the foundation for further studies on increasing the expression level and improving the catalytic performance based on molecular transformation.