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- W1990843222 abstract "• Peroxidases enhanced the waste degradation of lignin-rich waste. • The enzyme-catalyzed reaction mechanism was identified. • Rate constants for enzyme-catalyzed an un-catalyzed reactions were estimated. Augmenting leachate before recirculation with peroxidase enzymes is a novel method to increase the available carbon, and therefore the food supply to microorganisms at the declining phase of the anaerobic landfill bioreactor operation. In order to optimize the enzyme-catalyzed leachate recirculation process, it is necessary to identify the reaction mechanisms and determine rate constants. This paper presents a kinetic model developed to ascertain the reaction mechanisms and determine the rate constants for enzyme catalyzed anaerobic waste degradation. The maximum rate of reaction ( V max ) for MnP enzyme-catalyzed reactors was 0.076 g TOC /g DS .day. The catalytic turnover number ( k cat ) of the MnP enzyme-catalyzed was 506.7 per day while the rate constant ( k ) of the un-catalyzed reaction was 0.012 per day." @default.
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- W1990843222 date "2014-06-01" @default.
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- W1990843222 title "Reaction mechanisms and rate constants of waste degradation in landfill bioreactor systems with enzymatic-enhancement" @default.
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- W1990843222 doi "https://doi.org/10.1016/j.biortech.2014.03.147" @default.
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