Characterization of highly active tyrosine ammonia lyase and its application in biosynthesis of p -coumaric acid

• Published in: Sheng wu gong cheng xue bao = Chinese journal of biotechnology Vol. 38; no. 12; p. 4553
• Main Authors: Huang, Yawen, Jiang, Xiaolong, Chen, Wujiu, Zhang, Guimin, Wang, Qinhong
• Format: Journal Article
• Language: Chinese
• Published: China 25.12.2022
• Subjects: Ammonia-Lyases - chemistry; Ammonia-Lyases - genetics; Coumaric Acids; Escherichia coli - genetics; Tyrosine; gene mining; tyrosine ammonia lyase; whole cell catalysis; p-coumaric acid
• ISSN: 1872-2075

-coumaric acid is one of the aromatic compounds that are widely used in food, cosmetics and medicine due to its properties of antibacterium, antioxidation and cardiovascular disease prevention. Tyrosine ammonia-lyase (TAL) catalyzes the deamination of tyrosine to -coumaric acid. However, the lack of highly active and specific tyrosine ammonia lyase limits cost-effective microbial production of -coumaric acid. In order to improve biosynthesis efficiency of -coumaric acid, two tyrosine ammonia-lyases, namely Fc-TAL2 derived from and Fs-TAL derived from , were selected and characterized. The optimum temperature (55 ℃) and pH (9.5) for Fs-TAL and Fc-TAL2 are the same. Under optimal conditions, the specific enzyme activity of Fs-TAL and Fc-TAL2 were 82.47 U/mg and 13.27 U/mg, respectively. Structural simulation and alignment analysis showed that the orientation of the phenolic hydroxyl group of the conserved Y50 residue on the inner lid loop and its distance to the substrate were the main reasons accounting for th