Reactor development for peroxidase catalyzed polymerization and precipitation of phenols from wastewater

Nicell, Jim A.; Bewtra, Jatinder K.; Biswas, Nihar; Taylor, Elmore H.

doi:10.1016/0043-1354(93)90127-4

Cited by 101 publications

(60 citation statements)

References 10 publications

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“…Free-radical products may also attack the peroxidase along with an inactivation process (Nicell et al, 1993) on the one hand or they act as an additional suitable substrate molecule (thus the radicals can be also considered as S (depending on their chemistry)) for maintaining the catalytic cycle on the other hand. The latter is partly applicable for the radical cation intermediates as discussed later in the text.…”

Section: Roomentioning

confidence: 99%

Reaction Kinetics of Versatile Peroxidase for the Degradation of Lignin Compounds

Busse¹

2013

American Journal of Biochemistry and Biotechnology

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The H 2 O 2 -dependent degradation of adlerol by a crude versatile peroxidase from Bjerkandera adusta, a new ligninolytic enzyme, was investigated. Adlerol (1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)-1,3-propanediol)) is a non-phenolic β-O-4 dimer whose structural architecture represents the most abundant unit (50-65%) of the valuable renewable biopolymer lignin. Lignin removel plays a key role in utilizing lignocellulosic biomass in biorefineries. Steady-state analyses in the µL scale showed saturation kinetics for both, H 2 O 2 and adlerol with quite sensitive response to H 2 O 2 . This was characterized through slow transient states (lag phases) prior steady-state and were enhanced by increasing H 2 O 2 concentration. The major reason for such phenomena was found to be an accumulation of compound III (E III ) via reaction of compound II (E II ) with H 2 O 2 ; instead with adlerol to the enzyme's ground state E 0 in order to restart another catalytic cycle. As result, the enzyme deviated from its normal catalytic cycle. A corresponding threshold was determined at ≥ 50 µM H 2 O 2 and an adlerol to H 2 O 2 ratio of 15:1 for the given conditions. Furthermore, E III did not represent a catalytical dead-end intermediate as it is generally described. By an additional decrease of the adlerol to H 2 O 2 ratio of ca. 3 at the latest, considerable irreversible enzyme deactivations occurred promoted through reaction of E III with H 2 O 2 . At a mL scale deactivation kinetics by H 2 O 2 were further examined in dependence on adlerol presence. The course followed a time-dependent irreversible deactivation (two step mechanism) and was diminished in the presence of adlerol. The deactivation could be sufficiently described by an equation similar to the Michaelis-Menten type, competitive inhibited by adlerol. Finally, first estimates of the kinetic parameters v max , K m S1 (S 1 : H 2 O 2 ), K m S2 (S 2 : adlerol), k i app and K i app were made. Moreover, the peroxidase reaction mechanism was reviewed and recommendations are given preventing permature enzyme losses.

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Section: Roomentioning

confidence: 99%

Reaction Kinetics of Versatile Peroxidase for the Degradation of Lignin Compounds

Busse¹

2013

American Journal of Biochemistry and Biotechnology

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“…3). As in other studies, (Klibanov et al, 1983, Maloney et al, 1986, Nicell et al, 1993, and Wu et al, 1993 2,4-DCP transformation was extremely fast; a maximum removal could be achieved within less than 15 min. According to Nicell et al, 1993, if peroxidase is used in excess, the number of catalytic turnovers is limited by the availability of substrate; whereas, excessive amount of H 2 O 2 may cause partial inactivation of the enzyme.…”

Section: Resultsmentioning

confidence: 59%

“…Horseradish peroxidase has not, however, been applied on an industrial scale, mainly due to the high cost of enzymatic treatment. It is demonstrated (Nakamoto &Machida, 1992 andNicell et al, 1993) that the reaction conditions can be optimized by application of various additives, such as gelatin or polyethene glycol, which prevent losses in enzymatic activity caused by adsorption of enzyme molecules on end-product polymers. The present study aims to test the usefulness of various small pieces of plants and algae (potato, sea lettuce and horseradish) compared to the purified horseradish peroxidase for decontamination of artificial polluted water with herbicide 2,4-DCP.…”

Section: Introductionmentioning

confidence: 99%

Peroxidase Catalyzed Decontamination of Water Polluted with 2,4-Dichlorophenols in Presence of Algae and Plant Materials

عبدالله¹

1999

mar

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ABSTRACT. Plants and algae were found useful in the decontamination of water polluted with chlorinated phenolic compounds. An artificial wastewater contaminated with up to 350 ppm herbicide 2,4-dichlorophenol (2,4-DCP), was successfully treated using horseradish, potato and Ulva sp. (sea lettuce), amended with H 2 O 2 . Horseradish -mediated provided up to 99% removal of 2,4-DCP from model solution, while, purified horseradish peroxidase provided up to 95%. Due to the apparent ease of application, the use of plant material may present a breakthrough in the enzyme treatment of contaminated water.

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“…Compound II oxidizes a second aromatic molecule, resulting in the release of a second free radical into the solution and returning the enzyme to its native state. The one-electron oxidation of aromatic substrate catalyzed by peroxidase is usually depicted by the following mechanism [21]: The effect of various concentrations of H 2 O 2 on phenol removal by jicama and luffa peroxidases is as illustrated in Fig. 2.…”

Section: Effect Of H 2 O 2 Concentrationmentioning

confidence: 99%

Comparison of two Agricultural Wastes for Phenol Removal Via Peroxidase-Catalyzed Enzymatic Approach

et al. 2016

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Abstract. Agricultural wastes of jicama and luffa skin peels were used as the source for peroxidase extraction. The extracted crude enzymes showed similar activities, 1.34U/mL and 1.22U/mL for jicama and luffa peroxidase respectively. These peroxidases were used to treat phenol under varying operating conditions of buffer pH, hydrogen peroxide concentration, enzyme volume and temperature. Jicama peroxidase demonstrated a phenol removal efficiency of approximately 90% at buffer pH 7, 1mM hydrogen peroxide using 1.5mL enzyme at 25 o C. Luffa peroxidase required a higher dosage of hydrogen peroxide, and exhibited a removal efficiency of 84% at 8mM with other operating conditions same as jicama peroxidase. Jicama peroxidase is sensitive to pH change and more susceptible to thermal denaturation. Luffa peroxidase showed a better stability in terms of temperature.

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Reactor development for peroxidase catalyzed polymerization and precipitation of phenols from wastewater

Cited by 101 publications

References 10 publications

Reaction Kinetics of Versatile Peroxidase for the Degradation of Lignin Compounds

Reaction Kinetics of Versatile Peroxidase for the Degradation of Lignin Compounds

Peroxidase Catalyzed Decontamination of Water Polluted with 2,4-Dichlorophenols in Presence of Algae and Plant Materials

Comparison of two Agricultural Wastes for Phenol Removal Via Peroxidase-Catalyzed Enzymatic Approach

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