利用重组色氨酸合成酶催化合成S-苯基-L-半胱氨酸,考察了反应温度、pH、底物摩尔比和底物浓度对色氨酸合成酶酶活的影响。最佳转化条件为:反应温度为37℃,pH=8,苯硫酚与L-丝氨酸的适宜底物摩尔比为1.2∶1,底物最适合浓度为400 mmol/L,反应达到平衡时间为16 h,底物L-丝氨酸摩尔转化率达到91%,苯硫酚与色氨酸合成酶活性位点Ser 235和Gly 233形成稳定的氢键。 The synthesis of S-phenyl-L-cysteine ​​by recombinant tryptophan synthase was investigated. The effects of reaction temperature, pH, substrate molar ratio and substrate concentration on tryptophan synthase activity were investigated. The optimal reaction conditions were as follows: the reaction temperature was 37 ℃, pH = 8, the appropriate substrate molar ratio of thiophenol and L-serine was 1.2:1, the optimum substrate concentration was 400 mmol / L, the reaction time was At 16 h, the molar conversion of L-serine was 91%, and the thiophenol and tryptophan synthase active sites Ser 235 and Gly 233 formed stable hydrogen bonds.