Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Coprinus cinereus peroxidase

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]

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]

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]

S. (2003) The structure of a mutant enzyme of Coprinus cinereus peroxidase provides an understanding of its increased thermostability. Acta Crys-tallogr.. Sect. D Biol. Crystallogr., 59, 997-1003. [Pg.21]

Bisphenol-A was polymerised by Coprinus cinereus peroxidase in an aqueous 2-propanol solution. Various polymerised products with different MW and hydroxyl values were synthesised depending on the reaction composition (the ratio of aqueous buffer to 2-propanol) [190]. [Pg.462]


See other pages where Coprinus cinereus peroxidase is mentioned: [Pg.124]    [Pg.64]    [Pg.72]    [Pg.169]    [Pg.297]    [Pg.317]    [Pg.79]    [Pg.79]    [Pg.80]    [Pg.84]    [Pg.196]    [Pg.156]    [Pg.424]   
See also in sourсe #XX -- [ Pg.150 ]




SEARCH



© 2024 chempedia.info