Production of p-acetaminophenol by whole-cell catalysis using Escherichia coli overexpressing bacterial aryl acylamidase.

Hyeok-Jin Ko, Won-Gi Bang, Kyoung Heon Kim, In-Geol Choi

Division of Biotechnology, College of Life Sciences and Biotechnology, Korea University, Anam-Dong, Seongbuk-Gu, Seoul, 136-713, Korea.

Biotechnology letters 2012 Apr

filter terms:

Aryl acylamidase (EC 3.5.1.13, AAA) acts on the amide bond between aryl and acyl groups. Whole cells of Escherichia coli overexpressing a novel bacterial AAA synthesized p-acetaminophenol (p-AAP) from p-aminophenol (p-AP, aryl compound) and acetate (acyl donor). Optimum conditions were pH 5.5 and 35°C with 100 mM p-AP and 600 mM sodium acetate in 100 mM sodium phosphate buffer including 1% (v/v) Triton X-100 for 60 h. 13.1 g p-AAP l(-1) was produced with a conversion yield of 87%.

Citation

Hyeok-Jin Ko, Won-Gi Bang, Kyoung Heon Kim, In-Geol Choi. Production of p-acetaminophenol by whole-cell catalysis using Escherichia coli overexpressing bacterial aryl acylamidase. Biotechnology letters. 2012 Apr;34(4):677-82