Title |
Characterization of biphenyl biodegradation, and regulation of biphenyl catabolism in alcaligenes xylosoxydans |
Author |
Lee, Na Ri · On, Hwa Young · Jeong, Min Seon¹ · Kim, Chi Kyung² · Park, Young Keun³ · Ka, Jong Ok⁴· Min, Kyung Hee * |
Address |
Department of Biology, Sookmyung Women's University; ¹Department of Food Science & Technology, Yeungnam University; ²Department of Microbiology, Chungbuk University; ³Department of biology, Korea University; ⁴Department of Agriculture of Life Science, Seoul National University |
Bibliography |
Journal of Microbiology, 35(2),141-148, 1997,
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DOI |
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Key Words |
Biphenyl degradation, dioxygenase, catechol, salicylate, Alcaligenes xtylosoxydans |
Abstract |
Alcaligenes xylosoxydans strain SMN3 capable of utilizing biphenyl grew not only on phenol, and benzoate, but also on salicylate. Catabolisms of biphenyl and salicylate appear to be interrelated since benzoate is a common metabolic intermediate of these compounds. Enzyme levels in the excatechol 2,3-dioxygenas which is meta-cleavage enzyme of catechol, but did not induce catechol 1, 2-dioxygenase. All the oxidative enzymes of biphenyl and 2,3-dihydroxybiphenyl (23DHBP) were induced when the cells were grown on biphenyl and salicylate, respectively. Biphenyl and salicylate could be a good inducer in the oxidation of biphenyl and 2, 3-dihydroxybiphenyl. The two enzymes for the degradation of biphenyl and salicylate were induced after growth on either biphenyl or salicylate, suggesting the presence of a common regulatory element. However, benzoate could not induce the enzymes responsible for the oxidation of these compounds. Biphenyl and salicylate were good inducers for indigo formation due to the activity of biphenyl dioxygenase. These results suggested that indole oxidation is a property of bacterial dioxygenase that form cis-dihydrodiols from aromatic hydrocarbon including biphenyl. |
Download PDF |
Eng_350211_141-148p.pdf |