Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

---

Query: EC:1.10.3.2 (laccase)
4,656 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Phenolic compounds originating from plant residue decomposition or microbial metabolism form humic-like polymers during oxidative coupling reactions mediated by various phenoloxidases or metal oxides. Xenobiotic phenols participating in these reactions undergo either polymerization or binding to soil organic matter. Another effect of oxidative coupling is dehalogenation, decarboxylation or demethoxylation of the substrates. To investigate these phenomena, several naturally occurring and xenobiotic phenols were incubated with various phenoloxidases (peroxidase, laccase, tyrosinase) or with birnessite (delta-MnO(2)), and monitored for chloride release, CO(2) evolution, and methanol or methane production. The release of chloride ions during polymerization and binding ranged between 0.2% and 41.4%. Using the test compounds labeled with 14C in three different locations (carboxyl group, aromatic ring, or aliphatic chain), it was demonstrated that 14CO(2) evolution was mainly associated with the release of carboxyl groups (17.8-54.8% of the initial radioactivity). Little mineralization of 14C-labeled aromatic rings or aliphatic carbons occurred in catechol, ferulic or p-coumaric acids (0.1-0.7%). Demethoxylation ranged from 0.5% to 13.9% for 2,6-dimethoxyphenol and syringic acid, respectively. Methylphenols showed no demethylation. In conclusion, dehalogenation, decarboxylation and demethoxylation of phenolic substrates appear to be controlled by a common mechanism, in which various substituents are released if they are attached to carbon atoms involved in coupling. Electron-withdrawing substituents, such as -COOH and -Cl, are more susceptible to release than electron-donating ones, such as -OCH(3) and -CH(3). The release of organic substituents during polymerization and binding of phenols may add to CO(2) production in soil.
...
PMID:Release of substituents from phenolic compounds during oxidative coupling reactions. 1273 92

The effect of the addition of the nonionic surfactant tributylphenyltetraethoxylate to culture media on pH and extracellular protein content, and on production of beta-glucosidase, xylanase, laccase, and manganese-dependent and -independent peroxidases by the edible fungus Pleurotus ostreatus was determined. The relationship between fermentation parameters and concentration of surfactant was assessed by multiple linear regression analysis, and the similarities and differences among the fermentation parameters were elucidated by principal component analysis. Calculations proved that except for xylanase all other cultivation parameters were significantly influenced by the surfactant, with the effect higher at higher surfactant concentrations. Surfactant increased the production of beta-glucosidase and inhibited laccase and manganese-dependent and -independent peroxidase activities.
...
PMID:Effect of tributylphenyltetraethoxylate on enzyme production of Pleurotus ostreatus. 1290 30

Penicillium funiculosum Thom. was consistently isolated from pineapple-infected fruitlet (black spots). Polyphenol oxidase, peroxidase, and laccase activities were determined in extracts from contiguous and infected fruitlets. Healthy fruitlets showed a rather high level of polyphenol oxidase (optimum pH 7.0), and this activity was tremendously increased (X 10) in contiguous infected fruitlets. Furthermore, infected fruitlets also exhibited laccase activity (optimum pH 4.0), while peroxidase was rather constant in both fruitlets. Browning reactions were attributed to qualitative and quantitative modifications of the enzymatic equipment (polyphenol oxidase and laccase) (p < 0.0001). In infected fruiltets, sucrose and L-malic acid were present at significantly lower amounts than in healthy ones, likely owing to fungal metabolism (p < 0.0001), whereas cell wall material was three times higher, which could be viewed as a defense mechanism to limit expansion of the mycelium.
...
PMID:Enzymatic browning and biochemical alterations in black spots of pineapple [Ananas comosus (L.) Merr.]. 1450 57

Mycena galopus is among the most important leaf litter decomposers in UK coniferous and angiosperm woodlands, having the potential to utilise all the major constituents of plant litter. Even so, the enzyme or combination of enzymes produced by M. galopus responsible for lignin depolymerisation was previously unknown. A range of media from liquid and semi-solid cultures to more natural substrata was tested to determine whether laccase was produced by an isolate of M. galopus, M9053. Malt extract liquid medium (MEL) with 2,5-xylidine favoured laccase production as compared with the same medium containing the inducers veratryl alcohol, veratryl aldehyde, veratric acid, homoveratric acid, vanillic acid or p-anisic acid. A semi-solid medium of cereal bran in phosphate buffer and a solid medium of Picea sitchensis F1 horizon needle litter were also not as effective as MEL with 2,5-xylidine as an inducer. Compared with six other isolates of the same species grown in MEL without inducers, M9053 exhibited rates of laccase activity fairly typical for M. galopus. An isolate from a dark coloured basidiome of M. galopus, but not var. nigra, exhibited the greatest activity while var. candida showed relatively low laccase activity. Marasmius androsaceus exhibited peak laccase production several days later than M. galopus. In addition, a manganese-dependent peroxidase that was responsible for 15% (in MEL culture fluid) and 39% (in needle litter extract III) of ligninolytic activity was produced by M9053. A further peroxidase was found to be the major ligninolytic constituent in MEL extracts (53%), and had a similar contribution to total activity (29%) as laccase (32%) in needle litter fraction III. Mycena galopus produced water- and buffer-extractable mannases and xylanases when grown on needle litter.
...
PMID:Enzyme production by Mycena galopus mycelium in artificial media and in Picea sitchensis F1 horizon needle litter. 1453 22

Increased manganese concentration during submerged cultivation of the ligninolytic white rot fungus Panus tigrinus 8/18 on N-limited mineral medium resulted in the induction of Mn-peroxidase and laccase. The Mn-peroxidase was purified with the purity factor RZ (A(406)/A(280)) = 4.3. The purified enzyme catalyzed H2O2-dependent oxidation of phenol oxidase substrates (aromatic amines, 2,2;-azinobis-(3-ethylbenzthiazolinesulfonic acid), hydroquinone, 2,6-dimethoxyphenol) without Mn2+, which is not typical for the usual Mn-peroxidases. Guaiacol and 2,4,6-trichlorophenol were not oxidized in the absence of Mn2+. Study of absorption spectra of the intermediates of the catalytic cycle revealed that this peroxidase is able to complete the redox cycle, reducing one-electron oxidized intermediate (Compound II) by Mn2+, as well as by an organic substrate (hydroquinone). This means that the enzyme is a "hybrid" Mn-peroxidase, different from the common Mn-peroxidases from ligninolytic fungi.
...
PMID:Hybrid Mn-peroxidase from the ligninolytic fungus Panus tigrinus 8/18. Isolation, substrate specificity, and catalytic cycle. 1460 47

White-rot fungi produce various isoforms of extracellular oxidases including laccase, Mn peroxidase and lignin peroxidase (LiP), which are involved in the degradation of lignin in their natural lignocellulosic substrates. This ligninolytic system of white-rot fungi (WRF) is directly involved in the degradation of various xenobiotic compounds and dyes. This review summarizes the state of the art in the research and prospective use of WRF and their enzymes (lignin-modifying enzymes, LME) for the treatment of industrial effluents, particularly dye containing effluents. The textile industry, by far the most avid user of synthetic dyes, is in need of ecoefficient solutions for its colored effluents. The decolorization and detoxification potential of WRF can be harnessed thanks to emerging knowledge of the physiology of these organisms as well as of the biocatalysis and stability characteristics of their enzymes. This knowledge will need to be transformed into reliable and robust waste treatment processes.
...
PMID:White-rot fungi and their enzymes for the treatment of industrial dye effluents. 1462 49

Ferroxidase activity was detected in a laccase-like multicopper oxidase (LMCO) produced in transgenic tobacco cells expressing an LMCO cDNA (Ltlacc2.2) cloned from yellow-poplar (Liriodendron tulipifera). This marks the first report of ferroxidase activity associated with a plant laccase and suggests that some members of this plant enzyme family may have physiological functions based on activities other than their more widely recognized phenoloxidase activity. Recent work with LMCOs from bacteria, yeast and mammals has shown that metal oxidase activities in these enzymes can be important for their primary physiological functions, With respect to ferroxidase activity in certain plant LMCOs, it is proposed that the high levels of LMCO expression in plant vascular tissues may reflect the need for high-efficiency iron uptake pumps in tissues that undergo lignification during normal development. Such iron uptake pumps would function to minimize levels of free iron so that reactive oxygen species do not reach toxic levels when H2O2 is generated for peroxidase-mediated monolignol coupling during lignin deposition.
...
PMID:Ferroxidase activity in a laccase-like multicopper oxidase from Liriodendron tulipifera. 1506 Oct 81

An approach was developed to screening organic compounds for putative activity of redox mediators of oxidoreductases, including laccases and peroxidases, applicable for xenobiotic degradation. The study was carried out with a homogenous laccase preparation from the basidiomycete Trametes hirsuta and horse-radish root peroxidase. Compounds belonging to 1-phenyl-3-methylpyrazolones were selected. Spectroscopic and electrochemical investigation of two of the compounds, sodium 1-phenyl-2,3-dimethyl-4-aminopyrazolon 5n(4)-methanesulfonate (PPNa) and 1-(3'-sulfophenyl)-3-methylpyrazolone (SPP), was performed. Electrochemical oxidation of both PPNa and SPP gave rise to high-potential intermediates capable of oxidizing veratryl alcohol; a lignin-modeling compound. Kinetic indices of these compounds were determined in enzymatic reactions with the presence of laccase. It was shown that enzymatic oxidation of SPP by laccase produced high-potential intermediates capable of oxidizing veratryl alcohol to veratric acid. Veratryl alcohol did not oxidize during enzymatic oxidation of SPP by peroxidase. This points to a difference between the mechanisms of enzymatic oxidation of PPNa and SPP by laccase and peroxidase.
...
PMID:[Phenyl pyrazolones--novel oxidoreductase redox-mediators for degradation of xenobiotics]. 1512 93

White rot fungus Trametes gallica was studied for the production of lignocellulolytic enzymes: cellulase, xylanase, laccase, manganese-dependent peroxidase (MnP), and lignin peroxidase (LiP). The results demonstrated that low-nitrogen (2.2 mM N) and surface stationary cultivation favored production of extracellular MnP. MnP activity reached 118.1 UL(-1) while T. gallica was grown in a low-nitrogen culture containing phenylalanine. However, laccase levels observed in high-nitrogen (22 mM N) agitated cultures were much greater than those seen in low-nitrogen. The N source experiments seemed to reveal that NH4+ plays an important role in inducing MnP and laccase of the fungus. Results showed that T. gallica produces a series of the lignocellulolytic enzymes, and needs high N to produce all the enzymes during solid-state fermentation of wheat straw. This paper also presents a modified zymogram procedure to detect xylanase and laccase of T. gallica in polyacrylamide gel. Xylanase in crude enzyme of T. gallica was displayed by contacting protein gel strips with xylan substrate gels and by staining with iodine. By immersing the protein gel strips in o-tolidine solution, the blue-green zones representing laccase activity were visualized against a colorless background.
...
PMID:Production of lignocellulolytic enzymes by Trametes gallica and detection of polysaccharide hydrolase and laccase activities in polyacrylamide gels. 1516 96

Twenty-six species of aquatic hyphomycetes were isolated from woody sources (unidentified wood segments, leaf skeletons and neck of leaves and bark) in the North River Nile (Delta region). Alatospora acuminata, Anguillospora crassa, Flagellaspora penicillioides, Lunulospra curvula, Tetracladium marchalianum and Triscelophorus monosporus were the most common species. Temperature was the highest physico-chemical parameter affecting the aquatic hyphomycetes occurrence. Twelve species of hyphomycetes, isolated from woody substrates, were screened for their ability to produce extracellular lignocellulolytic enzymes on solid media. The enzymes tested included: endoglucanase, endoxylanase, beta-glucosidase, laccase, peroxidase, polyphenoloxidase, tyrosinase and beta-xylosidase. Three species, A. acuminata, F. penicillioides, T. monosporus, were positive for all tested enzymes. Also, A. longissima was positive for all enzymes except lignin-peroxidase. The ability to produce cellulase was 100% for all species while only, four species were positive for lignin-peroxidase. The ability of the species to produce other lignocellulotic enzyme ranged from 50% to 83%. Freshwater hyphomycetes have been shown to produce a rich array of enzymes able to degrade the polysaccharides of plant debris.
...
PMID:Lignocellulolytic enzyme production by aquatic hyphomycetes species isolated from the Nile's delta region. 1518 Jan 56


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>

---