4-Chlorophenol biodegradation facilitator composed of recombinant multi-biocatalysts immobilized onto montmorillonite

Oh Sung Kwean; Su Yeon Cho; Jun Won Yang; Wooyoun Cho; Sungyoon Park; Yejee Lim; Min Chul Shin; Han Suk Kim; Joonhong Park; Han S. Kim

doi:10.1016/j.biortech.2018.03.066

4-Chlorophenol biodegradation facilitator composed of recombinant multi-biocatalysts immobilized onto montmorillonite

Oh Sung Kwean, Su Yeon Cho, Jun Won Yang, Wooyoun Cho, Sungyoon Park, Yejee Lim, Min Chul Shin, Han Suk Kim, Joonhong Park, Han S. Kim

Department of Civil and Environmental Engineering

Research output: Contribution to journal › Article

8 Citations (Scopus)

Abstract

A biodegradation facilitator which catalyzes the initial steps of 4-chlorophenol (4-CP) oxidation was prepared by immobilizing multiple enzymes (monooxygenase, CphC-I and dioxygenase, CphA-I) onto a natural inorganic support. The enzymes were obtained via overexpression and purification after cloning the corresponding genes (cphC-I and cphA-I) from Arthrobacter chlorophenolicus A6. Then, the recombinant CphC-I was immobilized onto fulvic acid-activated montmorillonite. The immobilization yield was 60%, and the high enzyme activity (82.6%) was retained after immobilization. Kinetic analysis indicated that the Michaelis-Menten model parameters for the immobilized CphC-I were similar to those for the free enzyme. The enzyme stability was markedly enhanced after immobilization. The immobilized enzyme exhibited a high level of activity even after repetitive use (84.7%) and powdering (65.8%). 4-CP was sequentially oxidized by a multiple enzyme complex, comprising the immobilized CphC-I and CphA-I, via the hydroquinone pathway: oxidative transformation of 4-CP to hydroxyquinol followed by ring fission of hydroxyquinol.

Original language	English
Pages (from-to)	268-275
Number of pages	8
Journal	Bioresource technology
Volume	259
DOIs	https://doi.org/10.1016/j.biortech.2018.03.066
Publication status	Published - 2018 Jul

Bibliographical note

Funding Information:
This research was supported by the Faculty Research Fund of Konkuk University 2017.

All Science Journal Classification (ASJC) codes

Bioengineering
Environmental Engineering
Renewable Energy, Sustainability and the Environment
Waste Management and Disposal

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@article{64a08cebb3104aa5ba3c58db026e143a,

title = "4-Chlorophenol biodegradation facilitator composed of recombinant multi-biocatalysts immobilized onto montmorillonite",

abstract = "A biodegradation facilitator which catalyzes the initial steps of 4-chlorophenol (4-CP) oxidation was prepared by immobilizing multiple enzymes (monooxygenase, CphC-I and dioxygenase, CphA-I) onto a natural inorganic support. The enzymes were obtained via overexpression and purification after cloning the corresponding genes (cphC-I and cphA-I) from Arthrobacter chlorophenolicus A6. Then, the recombinant CphC-I was immobilized onto fulvic acid-activated montmorillonite. The immobilization yield was 60%, and the high enzyme activity (82.6%) was retained after immobilization. Kinetic analysis indicated that the Michaelis-Menten model parameters for the immobilized CphC-I were similar to those for the free enzyme. The enzyme stability was markedly enhanced after immobilization. The immobilized enzyme exhibited a high level of activity even after repetitive use (84.7%) and powdering (65.8%). 4-CP was sequentially oxidized by a multiple enzyme complex, comprising the immobilized CphC-I and CphA-I, via the hydroquinone pathway: oxidative transformation of 4-CP to hydroxyquinol followed by ring fission of hydroxyquinol.",

author = "Kwean, {Oh Sung} and Cho, {Su Yeon} and Yang, {Jun Won} and Wooyoun Cho and Sungyoon Park and Yejee Lim and Shin, {Min Chul} and Kim, {Han Suk} and Joonhong Park and Kim, {Han S.}",

note = "Funding Information: This research was supported by the Faculty Research Fund of Konkuk University 2017.",

year = "2018",

month = jul,

doi = "10.1016/j.biortech.2018.03.066",

language = "English",

volume = "259",

pages = "268--275",

journal = "Bioresource Technology",

issn = "0960-8524",

publisher = "Elsevier Limited",

}

4-Chlorophenol biodegradation facilitator composed of recombinant multi-biocatalysts immobilized onto montmorillonite. / Kwean, Oh Sung; Cho, Su Yeon; Yang, Jun Won; Cho, Wooyoun; Park, Sungyoon; Lim, Yejee; Shin, Min Chul; Kim, Han Suk; Park, Joonhong; Kim, Han S.

In: Bioresource technology, Vol. 259, 07.2018, p. 268-275.

Research output: Contribution to journal › Article

TY - JOUR

T1 - 4-Chlorophenol biodegradation facilitator composed of recombinant multi-biocatalysts immobilized onto montmorillonite

AU - Kwean, Oh Sung

AU - Cho, Su Yeon

AU - Yang, Jun Won

AU - Cho, Wooyoun

AU - Park, Sungyoon

AU - Lim, Yejee

AU - Shin, Min Chul

AU - Kim, Han Suk

AU - Park, Joonhong

AU - Kim, Han S.

N1 - Funding Information: This research was supported by the Faculty Research Fund of Konkuk University 2017.

PY - 2018/7

Y1 - 2018/7

N2 - A biodegradation facilitator which catalyzes the initial steps of 4-chlorophenol (4-CP) oxidation was prepared by immobilizing multiple enzymes (monooxygenase, CphC-I and dioxygenase, CphA-I) onto a natural inorganic support. The enzymes were obtained via overexpression and purification after cloning the corresponding genes (cphC-I and cphA-I) from Arthrobacter chlorophenolicus A6. Then, the recombinant CphC-I was immobilized onto fulvic acid-activated montmorillonite. The immobilization yield was 60%, and the high enzyme activity (82.6%) was retained after immobilization. Kinetic analysis indicated that the Michaelis-Menten model parameters for the immobilized CphC-I were similar to those for the free enzyme. The enzyme stability was markedly enhanced after immobilization. The immobilized enzyme exhibited a high level of activity even after repetitive use (84.7%) and powdering (65.8%). 4-CP was sequentially oxidized by a multiple enzyme complex, comprising the immobilized CphC-I and CphA-I, via the hydroquinone pathway: oxidative transformation of 4-CP to hydroxyquinol followed by ring fission of hydroxyquinol.

AB - A biodegradation facilitator which catalyzes the initial steps of 4-chlorophenol (4-CP) oxidation was prepared by immobilizing multiple enzymes (monooxygenase, CphC-I and dioxygenase, CphA-I) onto a natural inorganic support. The enzymes were obtained via overexpression and purification after cloning the corresponding genes (cphC-I and cphA-I) from Arthrobacter chlorophenolicus A6. Then, the recombinant CphC-I was immobilized onto fulvic acid-activated montmorillonite. The immobilization yield was 60%, and the high enzyme activity (82.6%) was retained after immobilization. Kinetic analysis indicated that the Michaelis-Menten model parameters for the immobilized CphC-I were similar to those for the free enzyme. The enzyme stability was markedly enhanced after immobilization. The immobilized enzyme exhibited a high level of activity even after repetitive use (84.7%) and powdering (65.8%). 4-CP was sequentially oxidized by a multiple enzyme complex, comprising the immobilized CphC-I and CphA-I, via the hydroquinone pathway: oxidative transformation of 4-CP to hydroxyquinol followed by ring fission of hydroxyquinol.

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