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- W2016361282 abstract "Haloalkane dehalogenase is an enzyme capable of catalyzing the conversion of short-chained (C2–C8) aliphatic halogenated hydrocarbons to a corresponding primary alcohol. Because of its broad substrate specificity for mono-, di-, and trisubstituted halogenated hydrocarbons and cofactor independence, haloalkane dehalogenases are attractive biocatalysts for gas-phase bioremediation of pollutant halogenated vapor emissions. A solid preparation of haloalkane dehalogenase from Rhodococcus rhodochrous was used to catalyze the dehalogenation reaction of 1-chlorobutane or 1,3-dichloropropane delivered in the gas phase. For optimal gas-phase dehalogenase activity, a relative humidity of 100%, aw = 1, was desired. With a 50% reduction in the vapor-phase hydration level, an 80% decrease in enzymatic activity was observed. The enzyme kinetics for the gas-phase substrates obeyed an Arrhenius-“like” behavior and the solid haloalkane dehalogenase preparation was more thermally stable than its water-soluble equivalent. Triethylamine was added to the gaseous reaction environment in efforts to increase the rate of reaction. A tenfold increase in the dehalogenase activity for the vapor-phase substrates was observed with the addition of triethylamine. Triethylamine altered the electrostatic environment of haloalkane dehalogenase via a basic shift in local pH, thereby minimizing the effect of the pH-reducing reaction product on enzyme activity. Both organic phase and solid-state buffers were used to confirm the activating role of the altered ionization state. © 2000 John Wiley & Sons, Inc., Biotechnol Bioeng 69: 235–241, 2000." @default.
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- W2016361282 date "2000-01-01" @default.
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- W2016361282 title "Enzymatic dehalogenation of gas phase substrates with haloalkane dehalogenase" @default.
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- W2016361282 doi "https://doi.org/10.1002/1097-0290(20000805)69:3<235::aid-bit1>3.0.co;2-d" @default.
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