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

doi:10.1007/s10529-011-0811-5

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

Department of Biotechnology

Research output: Contribution to journal › Article › peer-review

5 Citations (Scopus)

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 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%.

Original language	English
Pages (from-to)	677-682
Number of pages	6
Journal	Biotechnology letters
Volume	34
Issue number	4
DOIs	https://doi.org/10.1007/s10529-011-0811-5
Publication status	Published - 2012 Apr

Keywords

Aryl acylamidase
Bioconversion
Whole-cell catalysis
p-Acetaminophenol

ASJC Scopus subject areas

Biotechnology
Bioengineering
Applied Microbiology and Biotechnology

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10.1007/s10529-011-0811-5

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

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 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%.",

keywords = "Aryl acylamidase, Bioconversion, Whole-cell catalysis, p-Acetaminophenol",

author = "Ko, {Hyeok Jin} and Bang, {Won Gi} and Kim, {Kyoung Heon} and Choi, {In Geol}",

note = "Funding Information: Acknowledgments We thank Joseph Song of Korea University for a critical review. This work is supported by the National Research Foundation (NRF) (No. 2009-0068606), the Pioneer Research Center Program (2011-0002327) and the Advanced Biomass R&D Center of Korea (2010-0029734) grants funded by the Korea Ministry of Education, Science and Technology.",

year = "2012",

month = apr,

doi = "10.1007/s10529-011-0811-5",

language = "English",

volume = "34",

pages = "677--682",

journal = "Biotechnology Letters",

issn = "0141-5492",

publisher = "Springer Netherlands",

number = "4",

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TY - JOUR

T1 - Production of p-acetaminophenol by whole-cell catalysis using Escherichia coli overexpressing bacterial aryl acylamidase

AU - Ko, Hyeok Jin

AU - Bang, Won Gi

AU - Kim, Kyoung Heon

AU - Choi, In Geol

N1 - Funding Information: Acknowledgments We thank Joseph Song of Korea University for a critical review. This work is supported by the National Research Foundation (NRF) (No. 2009-0068606), the Pioneer Research Center Program (2011-0002327) and the Advanced Biomass R&D Center of Korea (2010-0029734) grants funded by the Korea Ministry of Education, Science and Technology.

PY - 2012/4

Y1 - 2012/4

N2 - 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%.

AB - 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%.

KW - Aryl acylamidase

KW - Bioconversion

KW - Whole-cell catalysis

KW - p-Acetaminophenol

UR - http://www.scopus.com/inward/record.url?scp=84858004357&partnerID=8YFLogxK

U2 - 10.1007/s10529-011-0811-5

DO - 10.1007/s10529-011-0811-5

M3 - Article

C2 - 22130742

AN - SCOPUS:84858004357

VL - 34

SP - 677

EP - 682

JO - Biotechnology Letters

JF - Biotechnology Letters

SN - 0141-5492

IS - 4

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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