Engineering dioxygenases for efficient degradation of environmental pollutants.
Dioxygenases have recently been engineered to improve their capabilities for environmental pollutant degradation. The techniques used to achieve this include in vitro DNA shuffling and subunit or domain exchanges between dioxygenases of different bacterial origins. Such evolved enzymes acquire novel and enhanced degradation capabilities of xenobiotic compounds, such as polychlorinated biphenyls, trichloroethylene and a variety of aromatic compounds. Hybrid strains in which the evolved genes are integrated into the chromosomal operons exhibit efficient degradation of xenobiotic chlorinated compounds.
Furukawa
K
K
Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University, Fukuoka, 812-8581, Japan. kfurukaw@agr.kyushu-u.ac.jp
D000595:Amino Acid Sequence; D001673:Biodegradation, Environmental; D001709:Biotechnology; D001713:Biphenyl Compounds / Q000378:metabolism; D049308:Dioxygenases; D004785:Environmental Pollutants / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D010105:Oxygenases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D015202:Protein Engineering; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013379:Substrate Specificity; D014241:Trichloroethylene / Q000378:metabolism
D001713:Biphenyl Compounds; D004785:Environmental Pollutants; D009097:Multienzyme Complexes; D011993:Recombinant Fusion Proteins; D014241:Trichloroethylene; D010105:Oxygenases; D049308:Dioxygenases; C038703:naphthalene dioxygenase; C108163:dioxin dioxygenase