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Journal of Bacteriology, September 2001, p. 5441-5444, Vol. 183, No. 18
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.18.5441-5444.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Directed Evolution of Biphenyl Dioxygenase: Emergence of Enhanced Degradation Capacity for Benzene, Toluene, and Alkylbenzenes

Hikaru Suenaga, Mariko Mitsuoka, Yuko Ura, Takahito Watanabe, and Kensuke Furukawa*

Department of Biosciences and Biotechnology, Faculty of Agriculture, Kyushu University, Fukuoka 812-8581, Japan

Received 1 May 2001/Accepted 27 June 2001

Biphenyl dioxygenase (Bph Dox) catalyzes the initial oxygenation of biphenyl and related compounds. Bph Dox is a multicomponent enzyme in which a large subunit (encoded by the bphA1 gene) is significantly responsible for substrate specificity. By using the process of DNA shuffling of bphA1 of Pseudomonas pseudoalcaligenes KF707 and Burkholderia cepacia LB400, a number of evolved Bph Dox enzymes were created. Among them, an Escherichia coli clone expressing chimeric Bph Dox exhibited extremely enhanced benzene-, toluene-, and alkylbenzene-degrading abilities. In this evolved BphA1, four amino acids (H255Q, V258I, G268A, and F277Y) were changed from the KF707 enzyme to those of the LB400 enzyme. Subsequent site-directed mutagenesis allowed us to determine the amino acids responsible for the degradation of monocyclic aromatic hydrocarbons.

* Corresponding author. Mailing address: Department of Biosciences and Biotechnology, Faculty of Agriculture, Kyushu University, Fukuoka 812-8581, Japan. Phone: 81-92-642-2849. Fax: 81-92-642-2849. E-mail: kfurukaw{at}agr.kyushu-u.ac.jp.

Journal of Bacteriology, September 2001, p. 5441-5444, Vol. 183, No. 18
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.18.5441-5444.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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