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Purification and characterization of 2,3-dihydroxybiphenyl 1,2-dioxygenase from Comamonas sp SMN4

Authors
Lee, NLee, JMMin, KHKwon, DY
Issue Date
Aug-2003
Publisher
KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY
Keywords
dihydroxybiphenyl dioxygenase; bphC; Comamonas; biphenyl degradation; binding affinity; substrate specificity
Citation
JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.13, no.4, pp 487 - 494
Pages
8
Journal Title
JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
Volume
13
Number
4
Start Page
487
End Page
494
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/16176
ISSN
1017-7825
1738-8872
Abstract
2,3-Dihydroxybiphenyl 1,2-dioxygenase (23DBDO), an enzyme of the biphenyl biodegradation pathway encoded by the bphC gene of Comamonas sp. SMN4, was expressed and purified using column chromatographies. SDS-PAGE of purified 23DBDO showed a single band with a molecular mass of 32 kDa, which was consistent with the data from the gel filtration chromatography (GFC). The purified enzyme exhibited a maximum 23DBDO activity at pH 9.0 and was stable at pH 8.0. The enzyme showed maximum activity at 40degreesC and maintained activity at 30degreesC for 24 h. Kinetic parameters represented by Michaelis-Menten constants such as K-m and V-max values for various substrates were determined by Lineweaver-Burk plots: The purified enzyme 23DBDO from Comamonas sp. SMN4 had the highest catalytic activity for 2,3-dihydroxybiphenyl and 3-methylcatechol, and had very poor activity with catechol and 4-methylcatechol.
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