Stability testing of ligninase and Mn‐peroxidase from <i>Phanerochaete chrysosporium</i>

Aitken, Michael D.; Irvine, Robert L.

doi:10.1002/bit.260341003

Cited by 69 publications

(25 citation statements)

References 39 publications

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“…The deactivation kinetic could be described satisfactorily by the model in Equation (32) (Aitken and Irvine, 1989). Furthermore, an additional estimation for the dissociation constant K m S2 of 2,506 µM was obtained indicating high substrate affinity.…”

Section: Furthermore Vamentioning

confidence: 74%

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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: Furthermore Vamentioning

confidence: 74%

“…16 and 17). In this context, Aitken and Irvine (1989) and Hu et al (1993) investigated deactivation kinetics of a LiP (and a MnP) from P. chrysosporium. Both working groups concluded that the lag phases, caused by E III formation, are additionally associated with enzyme deactivation via E III .…”

Section: Furthermore Vamentioning

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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“…2). Peroxidases might be inactivated in the presence of H2O2, with this inactivation depending on the concentration of H2O2 (1,25). Vyas and Molitoris (27) observed that RBBR decolorization by a crude P. ostreatus extract was maximal at a H2O2 concentration ranging from 132 to 154 µM.…”

Section: Optimal H2o2 Concentration and Ph Optimum For Rbbr Decolorizmentioning

confidence: 99%

“…Whereas MnP produced by P. chrysosporium showed maximal activity at a H2O2 concentration of 0.02 mM, with total loss of activity in the presence of 1 mM H2O2, the MnP of L. betulinus presented maximal activity at 0.2mM, with 95 and 60% of its activity being maintained in the presence of 1 and 10 mM H2O2, respectively. High stability in the presence of H2O2 is an important characteristic for the commercial application of ligninolytic enzymes (1,8).…”

Section: Optimal H2o2 Concentration and Ph Optimum For Rbbr Decolorizmentioning

confidence: 99%

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Biodegradation of remazol brilliant blue R by ligninolytic enzymatic complex produced by Pleurotus ostreatus

Machado¹,

Matheus²

2006

Braz. J. Microbiol.

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Pleurotus ostreatus ("shimeji") is produced in Brazil on a commercial scale using various lignocellulosic residues. Efforts have been made to reuse the culture residue to obtain products of greater aggregate value such as enzymes or in processes of bioremediation. We evaluated the Remazol brilliant blue R (RBBR) degradation potential of extracts from solid substrate colonized by P. ostreatus and extracts from residue of the "shimeji" mushroom yield. Colonized substrates and residue were provided by Toyobo do Brasil Ltda. Extraction was performed with sodium acetate buffer (50 mM, pH 4.6). RBBR decolorization was monitored at 592 nm and peroxidase and laccase activities were measured by monitoring the oxidation of ABTS. Horseradish peroxidase was used as reference. The time of growth of P. ostreatus influenced RBBR degradation and peroxidase and laccase activities. Concentration of 1 mM H2O2 and pH 4.0 were the best for RBBR decolorization. Complete RBBR decolorization was obtained with the addition of only one aliquot of 50 µL of 1 mM H2O2. The stability of the extracts was higher when they were kept under refrigeration than when stored frozen. The potential application of the ligninolytic complex derived from P. ostreatus and mushroom residue for xenobiotic degradation was demonstrated.

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Immobilization of manganese peroxidase fromLentinula edodes and its biocatalytic generation of MnIII-chelate as a chemical oxidant of chlorophenols

Grabski¹,

Grimek²,

Burgess

1998

Biotechnol. Bioeng.

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Manganese peroxidase (MnP) purified from commercial cultures of Lentinula edodes was covalently immobilized through its carboxyl groups using an azlactone‐functional copolymer derivatized with ethylenediamine and 2‐ethoxy‐1‐ethoxycarbonyl‐1,2‐dihydroquinoline (EEDQ) as a coupling reagent. The tethered enzyme was employed in a two‐stage immobilized MnP bioreactor for catalytic generation of chelated MnIII and subsequent oxidation of chlorophenols. Manganese peroxidase immobilized in the enzyme reactor (reactor 1) produced MnIII‐chelate, which was pumped into another chemical reaction vessel (reactor 2) containing the organopollutant. Reactor 1‐generated MnIII‐chelates oxidized 2,4‐dichlorophenol and 2,4,6‐trichlorophenol in reactor 2, demonstrating a two‐stage enzyme and chemical system. H2O2 and oxalate chelator concentrations were varied to optimize the immobilized MnP's oxidation of MnII to MnIII. Oxidation of 1.0 mM MnII to MnIII was initially measured at 78% efficiency under optimized conditions. After 24 h of continuous operation under optimized reaction conditions, the reactor still oxidized 1.0 mM MnII to MnIII with ∼69% efficiency, corresponding to 88% of the initial MnP activity. © 1998 John Wiley & Sons, Inc. Biotechnol Bioeng 60: 204–215, 1998.

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Stability testing of ligninase and Mn‐peroxidase from Phanerochaete chrysosporium

Cited by 69 publications

References 39 publications

Reaction Kinetics of Versatile Peroxidase for the Degradation of Lignin Compounds

Reaction Kinetics of Versatile Peroxidase for the Degradation of Lignin Compounds

Biodegradation of remazol brilliant blue R by ligninolytic enzymatic complex produced by Pleurotus ostreatus

Immobilization of manganese peroxidase fromLentinula edodes and its biocatalytic generation of MnIII-chelate as a chemical oxidant of chlorophenols

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