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Coprinus cinereus

APX, ascorbate peroxidase PJiP, Arthromyces ramosus peroxidase BPl, barley grain peroxidase CCP, C3dochrome c peroxidase CIP, Coprinus cinereus peroxidase EXAFS, extended X-ray absorption fine structure HRP, horseradish peroxidase HRP Z (where Z = A1-A3, B1-B3, Cl, C2, D, E1-E6, or N), a specific isoenzyme of horseradish peroxidase HS, high-spin lAA, indole-3-acetic acid LIP, hgnin peroxidase LS, low-spin PNP, the major cationic isoenzyme of peanut peroxidase WT, wild-type 5-c, five-coordinate 6-c, six-coordinate. [Pg.107]

Chemical modification of surface residues of HRP is one method which may offer some improvement in thermal or long-term stability of the enzyme. The -amino groups of the six surface Lys residues can be modified by reaction with carboxylic anhydrides and picryl sulfonic acid (296). In this example the number of sites modified was found to be more significant than the chemical nature of the modification, at least as a criterion for improved stability. Other methods explored include the use of bifunctional crosslinking reagents to couple surface sites on the enzyme (297). Future developments are likely to be concerned with the selection of site-directed mutants of HRP C that show enhanced thermal stability. Dramatic increases in thermal stability of up to 190-fold have been reported recently for mutants of Coprinus cinereus peroxidase (CIP) generated using a directed evolution approach (298). [Pg.150]

The same authors also investigated the kinetic resolution of racemic hydroperoxides with Coprinus peroxidase (CiP), isolated from the basidiomycete Coprinus cinereus... [Pg.337]

Morimoto, N., Suda, S., and Sagara, N. (1981). Effect of ammonia on fruit-body induction of Coprinus cinereus in darkness. Plant Cell Physiol. 22, 247-254. Morimoto, N., Suda, S., and Sagara, N. (1982). The effects of urea on the vegetative and reproductive growth of Coprinus stercorarius in pure culture. Trans. Mycol. Soc. Japan 23, 79-83. [Pg.96]

Ciaccio C, Rosati A, De Sanctis G et al (2003) Relationships of ligand binding, redox properties, and protonation in Coprinus cinereus peroxidase. J Biol Chem 278 18730-18737... [Pg.76]

Kim YH, Won K, Kwon JM et al (2005) Synthesis of polycardanol from a renewable resource using a fungal peroxidase from Coprinus cinereus. J Mol Catal B Enzym 34 33-38... [Pg.173]

An enzymatic method to remove dioxins from fishmeal has been investigated using Coprinus cinereus peroxidase, cloned and expressed in Aspergillus sp. and did not result in a major degradation of dioxins with only 10-15% reduction achieved [120]. [Pg.195]

The plug flow reactor has been mainly utilized for the removal of phenol in waste streams by HRP [76, 83] and Coprinus cinereus peroxidase [2]. According to Buchanan et al. [83], who modeled the kinetics of the HRP-aromatic substrate system and applied to PFR and CSTR, plug-flow configuration is recommended when working with low HRT, since considerably less enzyme would be required for equal phenol removal. However, for long HRTs, a multiple-stage CSTR would be more efficient than a PFR, due to the lower rate of enzyme inactivation. [Pg.262]

Masuda M, Sakurai A, Sakakibara M (2001) Effect of enzyme impurities on phenol removal by the method of polymerization and precipitation catalyzed by Coprinus cinereus peroxidase. Appl Microb Biotechnol 57 494 -99... [Pg.284]

Chang HC, Holland RD, Bumpus JA et al (1999) Inactivation of Coprinus cinereus peroxidase by 4-chloroaniline during turnover comparison with horseradish peroxidase and bovine lactoperoxidase. Chem Biol Interact 123 197-217... [Pg.312]

CPO Chloroperoxidase CPO nonheme chloroperoxidase LiP Lignin peroxidase LiPH2 Lignin peroxidase H2 isozyme MnP Manganese peroxidase CiP Coprinus cinereus peroxidase ARP Arthromyces ramosus peroxidase... [Pg.318]

Coprinus cinereus washing Pulp bleaching Cork treatment... [Pg.1377]

Fig. 3. Geometries of the type 1 copper sites of various blue copper proteins. The trigonal planar geometry is the type 1 site of laccase from Coprinus cinereus (PDB Code 1A65). The trigonal bipyramidal geometry shown is the copper site of azurin from Pseudomonas aeruginosa (PDB Code lAZU). The trigonal pyramidal/distorted tetrahedral sites are of the stellacyanin from Cucumis sativus (PDB Code IJER), NNSO site, and of the plastocyanin from Populus nigra (PDB Code IPLC) NNSS site. Fig. 3. Geometries of the type 1 copper sites of various blue copper proteins. The trigonal planar geometry is the type 1 site of laccase from Coprinus cinereus (PDB Code 1A65). The trigonal bipyramidal geometry shown is the copper site of azurin from Pseudomonas aeruginosa (PDB Code lAZU). The trigonal pyramidal/distorted tetrahedral sites are of the stellacyanin from Cucumis sativus (PDB Code IJER), NNSO site, and of the plastocyanin from Populus nigra (PDB Code IPLC) NNSS site.
Complex hetero-bifactorial faccordina to Kues. pers.com. ) A 1C, two subunits, multiple highly divergent alleles B 1C two subunits, multiple highly divergent alleles Schizophyllum commun, Coprinus cinereus... [Pg.218]

Three of the five crystal stmctures of eukaryotic MCOs archived in the PDB are of laccases from Coprinus cinereus... [Pg.996]

Horseradish peroxidase (HPO) has been reported to be threefold more stable at 80°C in 5-10% [bmim+][BF ] as compared to phosphate buffer [28], Okrasa et al. [29] reported the asymmetric oxidation of phenyl methyl- and 2-naphthyl methyl sulphides to sulphoxides catalysed by peroxidase from Coprinus cinereus in [bmim ] [PP6-] with 10% water [29], Although the enantioselectivity (63-92% ee) and yields (<32%) were similar to those in water, the reaction workup was easier because ionic liquids and the extraction solvent did not form emulsions. [Pg.173]

Similarly, Coprinus cinereus (CcP) peroxidase-catalyzed conversion of thioani-sole to sulfoxides has been studied in [BMIM] [PFJ in a biphasic reaction medium... [Pg.263]


See other pages where Coprinus cinereus is mentioned: [Pg.158]    [Pg.116]    [Pg.124]    [Pg.467]    [Pg.64]    [Pg.72]    [Pg.140]    [Pg.525]    [Pg.87]    [Pg.100]    [Pg.160]    [Pg.169]    [Pg.234]    [Pg.297]    [Pg.317]    [Pg.318]    [Pg.76]    [Pg.234]    [Pg.242]    [Pg.266]    [Pg.314]    [Pg.319]    [Pg.221]    [Pg.325]    [Pg.1762]    [Pg.303]   
See also in sourсe #XX -- [ Pg.173 , Pg.196 ]

See also in sourсe #XX -- [ Pg.682 , Pg.686 ]




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