Isolation and screening of basidiomycetes with high peroxidative activity

Jong, Ed de; Vries, Floris P. De; Field, Jim A.; Zwan, R.P. van der; Bont, J.A.M. de

doi:10.1016/s0953-7562(09)80121-4

Cited by 104 publications

(50 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The ether was removed by evaporation, yielding a yellow oil of methyl 4-([1-t-butylsilyl]oxy)-benzoate, yield kinetic isotope effects for the overall and reductive half-reactions were determined. For this purpose, an improved method 96%; 1 H-NMR (CDCl 3 ) δ H ppm ϭ 0.3 (t, 6H, CH 3 After acidification with H2SO4, the solution was expropiophenone, LiAlD4, t-butyldimethylsilyl chloride, imidazole, D 2 O and AlCl 3 were from Aldrich. Glucose oxidase (grade tracted twice with 150 ml ether.…”

Section: Synthesis Of 4-[b-2 H 3 ]Methylphenolmentioning

confidence: 99%

“…The ether was removed by evaporation and, in the final step, the deuterated product was purified II) was from Boehringer. Vanillyl-alcohol oxidase from P. simplicissimum (ATCC 90172) was purified as described before by silica column chromatography (eluent: dichloromethane/ ethyl acetate, 4:1) yielding 1.37 g pure 4-[A-2 H 3 ]methylphenol [3,5]. Enzyme concentrations were calculated from the molar absorption coefficient of the oxidized flavin (ε 439 ϭ 12.…”

Section: Synthesis Of 4-[b-2 H 3 ]Methylphenolmentioning

confidence: 99%

“…otherwise. Oxygen consumption was measured with a Clark electrode [3]. Conversion of 4-ethylphenol and 4-propylphenol was followed by the increase of absorbance at 260 nm.…”

Section: Synthesis Of 4-[b-2 H 3 ]Methylphenolmentioning

confidence: 99%

“…The reaction mechanism of vanillyl-alcohol oxidase has unit containing an 8A-(N 3 -histidyl)-FAD molecule [3,4]. Vanilproperties in common with that of p-cresol methylhydroxylase lyl-alcohol oxidase is active with a wide range of para-substi- [7].…”

mentioning

confidence: 99%

See 3 more Smart Citations

Kinetic mechanism of vanillyl‐alcohol oxidase with short‐chain 4‐alkylphenols

Fraaije

Heuvel

Roelofs

et al. 1998

European Journal of Biochemistry

View full text Add to dashboard Cite

The kinetic mechanism of vanillyl-alcohol oxidase with 4-methylphenol, 4-ethylphenol, 4-propylphenol and their CA-deuterated analogs has been studied at pH 7.5 and 25°C. Conversion of 4-methylphenol is extremely slow (0.005 s Ϫ1 ) while the enzyme is largely in the reduced form during turnover. 4-Ethylphenol and 4-propylphenol are readily converted while the enzyme is mainly in the oxidized form during turnover. The deuterium kinetic isotope effect for overall catalysis ranges between 7Ϫ10 whereas the intrinsic deuterium kinetic isotope effect for flavin reduction ranges over 9Ϫ10. With all three 4-alkylphenols, flavin reduction appeared to be a reversible process with the rate of reduction being in the same range as the rate for the reverse reaction. Keywords : alkylphenol; flavoprotein ; p-quinone methide ; kinetic isotope effect ; vanillyl-alcohol oxidase.Vanillyl-alcohol oxidase is a covalent flavoprotein isolated from Penicillium simplicissimum, a filamentous fungus capable of growing on a wide variety of aromatic compounds [1,2]. The enzyme is a rather stable homooctamer with each 65-kDa sub-The reaction mechanism of vanillyl-alcohol oxidase has unit containing an 8A-(N 3 -histidyl)-FAD molecule [3,4]. Vanilproperties in common with that of p-cresol methylhydroxylase lyl-alcohol oxidase is active with a wide range of para-substi- [7]. This bacterial flavocytochrome converts a wide range of tuted phenolic compounds [5], but the physiological function of 4-alkylphenols first into 4-hydroxybenzyl alcohols and subsethe enzyme is not fully understood. Based on induction experiquently into 4-hydroxybenzaldehydes. In contrast to vanillyl-alments, 4-(methoxymethyl)phenol has been proposed to represent cohol oxidase, flavin reoxidation in p-cresol methylhydroxylase the physiological substrate [2]. A detailed kinetic study with this involves the transfer of electrons to a tightly bound cytochrome phenolic methylether has pointed to a ternary complex mechasubunit [8]. nism in which flavin reduction is the rate-limiting step in cataly-The crystal structure of vanillyl-alcohol oxidase has recently sis [6]. The reaction of vanillyl-alcohol oxidase with 4-(methbeen solved at 2.5 Å resolution [9]. Each vanillyl-alcohol oxioxymethyl)phenol involves the initial formation of a binary dase monomer consists of two domains : one creates a binding complex of reduced enzyme and the p-quinone methide of site for the ADP moiety of the FAD molecule, while the other 4-(methoxymethyl)phenol. This complex then reacts with modomain covers the active center which is located between the lecular oxygen, reoxidizing the flavin, and after water addition two domains. The structure shows that the isoalloxazine ring of of the p-quinone methide, the products 4-hydroxybenzaldehyde the flavin makes a covalent bond with His422. Furthermore, the and methanol are formed (Eqn 1).active site is located in the interior of the protein and contains an Correspondence to W. J. H. van Berkel, Department of Biochemis-anion-binding pocket facilitating the depr...

show abstract

Section: Synthesis Of 4-[b-2 H 3 ]Methylphenolmentioning

confidence: 99%

Section: Synthesis Of 4-[b-2 H 3 ]Methylphenolmentioning

confidence: 99%

“…otherwise. Oxygen consumption was measured with a Clark electrode [3]. Conversion of 4-ethylphenol and 4-propylphenol was followed by the increase of absorbance at 260 nm.…”

Section: Synthesis Of 4-[b-2 H 3 ]Methylphenolmentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Kinetic mechanism of vanillyl‐alcohol oxidase with short‐chain 4‐alkylphenols

Fraaije

Heuvel

Roelofs

et al. 1998

European Journal of Biochemistry

View full text Add to dashboard Cite

show abstract

“…However, many white-rot fungi, including a number of aggressive lignin degraders, seem to operate without expressing LiP activity [11][12][13]. Laccase (EC 1.10.3.2) is another phenoloxidase that white-rot fungi often produce in conjunction with LiP, MnP or both [14,15]. However, the role played by laccase in lignin degradation has remained obscure since the low redox potential of this enzyme appeared to make it incapable of oxidizing non-phenolic lignin constituents [16].…”

Section: Introductionmentioning

confidence: 99%

A fungal metabolite mediates degradation of non‐phenolic lignin structures and synthetic lignin by laccase

et al. 1996

View full text Add to dashboard Cite

Lignin peroxidase is generally considered to be a primary catalyst for oxidative depolymerization of fignin by white-rot fungi. However, some white-rot fungi lack lignin peroxidase. Instead, many produce laccase, even though the redox potentials of known laccases are too low to directly oxidize the non-phenolic components of lignin. Pycnoporus cinnabarinus is one example of a laccase-producing fungus that degrades lignin very efficiently. To overcome the redox potential barrier, P.cinnabarinus produces a metabolite, 3-hydroxyanthranilate that can mediate the oxidation of nowphenolic substrates by laccase. This is the first description of how laccase might function in a biological system for the complete depolymerization of lignin.

show abstract

Degradation and Transformation of Aquatic Humic Substances by Laccase-producing FungiCladosporium cladosporioides andPolyporus versicolor

Claus

Filip²

1998

Acta hydrochim. hydrobiol.

View full text Add to dashboard Cite

Isolation and screening of basidiomycetes with high peroxidative activity

Cited by 104 publications

References 28 publications

Kinetic mechanism of vanillyl‐alcohol oxidase with short‐chain 4‐alkylphenols

Kinetic mechanism of vanillyl‐alcohol oxidase with short‐chain 4‐alkylphenols

A fungal metabolite mediates degradation of non‐phenolic lignin structures and synthetic lignin by laccase

Degradation and Transformation of Aquatic Humic Substances by Laccase-producing FungiCladosporium cladosporioides andPolyporus versicolor

Contact Info

Product

Resources

About