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

Authors
Ko, Hyeok-JinBang, Won-GiKim, Kyoung HeonChoi, In-Geol
Issue Date
4월-2012
Publisher
SPRINGER
Keywords
p-Acetaminophenol; Aryl acylamidase; Bioconversion; Whole-cell catalysis
Citation
BIOTECHNOLOGY LETTERS, v.34, no.4, pp.677 - 682
Indexed
SCIE
SCOPUS
Journal Title
BIOTECHNOLOGY LETTERS
Volume
34
Number
4
Start Page
677
End Page
682
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/108848
DOI
10.1007/s10529-011-0811-5
ISSN
0141-5492
Abstract
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 35A degrees 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%.
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