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

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

The phenoloxidase system responsible for the sclerotization of cockroach ootheca is found to be present as an inactive form in the left colleterial gland of Periplaneta americana. The supernatant fraction obtained by centrifugation of the milky white secretions contained the inactive phenoloxidase which required both sodium dodecyl sulfate (SDS) and the insoluble sediment for exhibiting enzyme activity. Bovine serum albumin could replace the sediment in the activation process. Proteins separated from the supernatant fraction by molecular sieve chromatography on Sephadex G-25 did not require either albumin or the sediment, but required SDS for exhibiting the phenoloxidase activity. Among the detergents tested, SDS (anionic) and cetylpyridinium chloride (cationic) activated the phenoloxidase, but CHAPS (zwitterionic) or nonionic detergents failed to activate the enzyme. The activation caused by SDS occurred well below the critical micellar concentration of SDS indicating that SDS is causing the activation by binding to the protein and altering its conformation. Chloroform-methanol extracts of vestibulum or right gland could replace SDS confirming the presence of endogenous activator(s) of phenoloxidase system. A variety of exogenously added lipids could activate the latent enzyme, among which linoleate, oleate, laurate, linolenate, phosphatidylethanolamine, and phosphatidylglycerol proved to be the effective activators of the latent phenoloxidase. Partially purified phenoloxidase was found to be extremely labile and lost its activity on a) freezing and thawing, b) dialysis, and c) heating for 10 min at 55 degrees C. It exhibited a pH optimum of 7 and was inhibited drastically by phenylthiourea and diethyldithiocarbamate. It readily oxidized a number of o-diphenols such as 3,4-dihydroxybenzylalcohol, 3,4-dihydroxyphenethyl alcohol, catechol, N-acetyldopamine, N-acetylnorepinephrine, dopa, dopamine, etc., but failed to oxidize both 3,4-dihydroxybenzoic acid and 3,4-dihydroxybenzaldehyde. It neither converted the typical laccase substrate syringaldazine to its quinone methide product, nor oxidized the p-diphenols, hydroquinone and methylhydroquinone. Therefore, the enzyme participating in the quinone tanning of cockroach ootheca appears to be a typical o-diphenol oxidase and not a laccase as previously thought.
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PMID:On the latency and nature of phenoloxidase present in the left colleterial gland of the cockroach Periplaneta americana. 213 24

Graphite (GE) or printed graphite electrode (PGE) based biosensors containing recombinant fungal laccase Polyporus pinsitus (rPpL), and Myceliophthora thermophila (rMtL) were developed. The enzymes were immobilized using bovine serum albumin and glutaraldehyde. At pH 5.5 and -0.1 V, the calibration graphs of GE based biosensors were hyperbolic if pyrocatechol was used. The concentration of substrate that results in 50% of steady-state response (EC(50)) was 0.7 mM and sensitivity (S) was 3.8 mA/M. The sensitivity increased up to 4 A/M if larger amount of rPpL was used. The sensitivity of biosensors changed little during 9 days of exploitation, but decreased at longer time. The PGE based biosensors were mounted into the flow-through cell and calibrated under kinetic regime. EC(50) of the biosensors containing rPpL varied from 0.6 to 4.0 mM and sensitivity varied from 0.11 to 1.9 mA/M. The response of biosensor containing thermostable laccase rMtL was less, but response saturated at larger pyrocatechol concentration. The sensitivity changed little during 6 days. Both type of biosensors responded also to 1-naphthol, o-phenylenediamine, guaiacol, o-anizidine, benzidine. The experiments demonstrate recombinant laccases application to biosensor engineering and their use to phenol and related compound determination under steady-state and flow-through regimes.
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PMID:Amperometric biosensors based on recombinant laccases for phenols determination. 1248 79

Stability characteristics of the laccases of the basidiomycetes Coriolus hirsutus and Coriolus zonatus were measured comparatively at temperatures 25 and 40 degrees C in the presence of various effectors (proteins, salts, polyalcohols, polyacids, and polyelectrolytes). Stabilization effects of cations on the laccases from C. hirsutus and C. zonatus decreased in the descending series Cu2+ > Mg2+ > Ca2+ and Ca2+ > Mg2+ > Mn2+, respectively. Tween 20 caused insignificant stabilization of the two enzymes. The C. zonatus laccase was also insignificantly stabilized as a result of treatment with bovine serum albumin. The enzymatic activity of the laccase preparations from C. hirsutus and C. zonatus was conserved virtually completely after vacuum drying (84 and 93%, respectively). The most effective stabilizer of the C. hirsutus laccase was found to be dextran (17 kD). Dry preparations treated with this agent conserved up to 95% of the enzymatic activity. The most effective stabilizer of the C. zonatus was polyacrylic acid (102% of the initial activity).
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PMID:[Comparative stability assessment of laccases from the basidiomycetes Coriolus hirsutus and Coriolus zonatus in the presence of effectors]. 1459 68

We report in this study that the sonication of laccase from Trametes villosa and bovine serum albumin promotes the formation of protein aggregates with high molecular weight. The formation of aggregates leads to the deactivation of the enzyme, fact that was confirmed by the analysis of the enzyme stability (half-life time) upon ultrasound treatment. This inactivation was mainly caused by the radicals formed by the cavitation phenomenon. It was verified that the addition of polyvinyl alcohol to laccase had a protecting effect against enzyme inactivation. The performance of laccase in the decolourization of indigo carmine was studied. It was observed that the best results were attained when the dye solution was treated with ultrasound and enzyme stabilized with polyvinyl alcohol, where more than 65% of decolourization was achieved. This value is remarkably higher than that attained for the enzyme alone, which was only able to decolourize 20% of the dye solution within 1h of treatment. These results have important implications for the exploitation of sonication in textile industry, where the pollution caused by the release of dyes into effluents is one of the major concerns.
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PMID:Stability and decolourization ability of Trametes villosa laccase in liquid ultrasonic fields. 1698 90

Laccase from the white rot fungus Coriolopsis polyzona was immobilized for the first time through the formation of cross-linked enzyme aggregates (CLEAs). Laccase CLEAs were produced by using 1000g of polyethylene glycol per liter of enzyme solution as precipitant and 200muM of glutaraldehyde as a cross-linking agent. These CLEAs had a laccase activity of 148Ug(-1) and an activity recovery of 60.2% when using 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) as substrate. CLEAs formed by co-aggregation with bovine serum albumin (BSA) as a stabilizer showed lower laccase activity and affinity for ABTS than those without BSA. The CLEAs co-aggregated with BSA showed higher residual activity against a protease, NaN(3), EDTA, methanol and acetone. The thermoresistance was higher for CLEAs than for free laccase and also higher for CLEAs co-aggregated with BSA than for simple CLEAs when tested at a pH of 3 and a temperature of 40 degrees C. Finally, laccase CLEAs were tested for their capacity to eliminate the known or suspected endocrine disrupting chemicals (EDCs) nonylphenol, bisphenol A and triclosan in a fluidized bed reactor. A 100-ml reactor with 0.5mg of laccase CLEAs operated continuously at a hydraulic retention time of 150min at room temperature and pH 5 could remove all three EDCs from a 5mgl(-1) solution.
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PMID:Preparation and characterization of cross-linked laccase aggregates and their application to the elimination of endocrine disrupting chemicals. 1788 20

Surface hydrophobicity (SH) of milk proteins treated physicochemically (by heating and Maillard reaction) or modified enzymatically (by transglutaminase, lactoperoxidase, laccase, and glucose oxidase) was assessed in relation to their techno-functional properties. Heat-treatment increased SH of whey protein isolate and decreased SH of sodium caseinate and bovine serum albumin. Maillard reaction of milk proteins caused time-depended decreases of SH. Only for total milk protein reacting with glucose and lactose elevated SH-values were detected. Protein modification with transglutaminase, laccase, and lactoperoxidase strongly increased the SH of whey protein isolate and total milk protein. Incubation with glucose oxidase elevated SH values of sodium caseinate, whey protein isolate, and total milk protein. When correlating SH with techno-functional properties, a positive correlation was observed between SH and foam formation, and a negative correlation was observed between SH and foam stability as well as emulsion stability. No clear correlation was detected between SH and emulsifying activity, surface tension, viscosity, and heat stability of enzymatically and physicochemically treated milk proteins.
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PMID:Surface hydrophobicity of physicochemically and enzymatically treated milk proteins in relation to techno-functional properties. 1816 64

Laccase from the white rot fungus strain Coriolopsis polyzona was immobilized covalently on the diatomaceous earth support Celite R-633 using different strategies. A first methodology involved the sequential activation of the support surface with gamma-aminopropyltriethoxysilane followed by the reaction of the functionalized surface with glutaraldehyde (GLU) or glyoxal (GLY) and the immobilization of laccase on the activated surface. Another strategy tested the simultaneous internal cross-linking of the protein with GLU or GLY and the immobilization of the laccase on the silanized surface. Finally, these two strategies were modified to test the impact of the concomitant addition of bovine serum albumin (BSA) as a stabilizing agent during the immobilization steps. The highest laccase activity and the greatest degree of activity recovery (tested using 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) as the substrate) were achieved by the sequential immobilization procedure using GLU as the cross-linking agent. The solid catalysts featuring internal cross-linking of the protein showed significantly higher stability against several denaturants. The Michaelis-Menten kinetic parameters with respect to ABTS revealed a higher affinity for this substrate in the case of the sequential procedure compared to the simultaneous approach. The biocatalyst formed using GLU in the sequential procedure was applied in a packed bed reactor for the continuous treatment of 5 mg l(-1) solutions of the endocrine disrupting chemicals (EDCs) nonylphenol (NP), bisphenol A (BPA) and triclosan (TCS) through repeated batch treatments. All of these EDCs could be eliminated at a contact time of less than 200 min by using, respectively, 3.75 units (U) of laccase activity for BPA and TCS and 1.88 U for NP. These performances of elimination were maintained over five consecutive treatment cycles using the same biocatalyst. This system could also remove these EDCs from 100 mg l(-1) solutions. The Michaelis-Menten kinetic parameters with respect to these chemicals showed a decreasing affinity of the solid biocatalyst for NP, TCS and BPA in that order.
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PMID:Immobilization of laccase from the white rot fungus Coriolopsis polyzona and use of the immobilized biocatalyst for the continuous elimination of endocrine disrupting chemicals. 1932 8

A crystalline silicon surface can be made biocompatible and chemically stable by a self-assembled biofilm of proteins, the hydrophobins (HFBs) purified from the fungus Pleurotus ostreatus. The protein-modified silicon surface shows an improvement in wettability and is suitable for immobilization of other proteins. Two different proteins were successfully immobilized on the HFBs-coated chips: the bovine serum albumin and an enzyme, a laccase, which retains its catalytic activity even when bound on the chip. Variable-angle spectroscopic ellipsometry (VASE), water contact angle (WCA), and fluorescence measurements demonstrated that the proposed approach in silicon surface bioactivation is a feasible strategy for the fabrication of a new class of hybrid devices.
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PMID:Bioactive modification of silicon surface using self-assembled hydrophobins from Pleurotus ostreatus. 1976 45

Initial acceptance of Cibacron Blue 3G-A based matrices has made dye-ligand affinity chromatography an attractive proposition. This prompted the synthesis and search for new dye structures. A systematic library of 96 affinity resins was generated using novel analogs of Cibacron Blue 3G-A and also by varying spacer lengths for immobilization. The library was tested in a batch binding and elution mode using seven different proteins--four Aspergillus enzymes namely, NADP-glutamate dehydrogenase, laccase, glutamine synthetase and arginase, bovine pancreatic trypsin and the two serum proteins human serum albumin and immunoglobulin G. Unique binding patterns were observed for each of them indicating that the library displayed discriminatory interactions. The significance of spacer length in the interaction with proteins was discernable. Trypsin interacted best with affinity resins that had no spacer. It was possible to resolve IgG and HSA from a mixture using a combination of resins. There was a good spread of HSA binding capacity in the 96 affinity resins. While some showed better HSA binding capacity than the commercial CB3GA-based matrix, a few with lower capacity were also observed. Subsequent to an initial screen, one affinity resin (CR-017) could be used to enrich Aspergillus terreus NADP-GDH from crude cell extracts. The efficacy of this dye-affinity resin was rationalized by characterizing NADP-GDH inhibition kinetics with the corresponding free dye ligand. In the sum, the library provides a set of dye-ligand affinity matrices with a potential for use in high throughput screening for protein purification.
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PMID:Discriminatory protein binding by a library of 96 new affinity resins: a novel dye-affinity chromatography tool-kit. 1976 65

Metal electrodes covered with organic (mono)layers containing pi-delocalized structures have many potential applications, for example, in construction of bioelectronic elements with high efficiency of electron transfer. In this contribution, a silver surface was modified with mixed monolayers formed from sodium 2-mercaptoethanesulfonate (MES) and four model (stable and easily available) aromatic thiols with strong basic properties: 4,6-diamino-2-mercaptopyrimidine (APY), 1H-1,2,4-triazole-3-thiol (HTR), 4-methyl-1,2,4-triazole-3-thiol (MTR), and 3-amino-1,2,4-triazole-5-thiol (ATR). The structure of the formed monolayers was determined from surface-enhanced Raman scattering (SERS) measurements. These studies showed that, despite significant differences in the molecular structures, MES is a very promising candidate for making mixed monolayers with mercapto-derivative aromatic bases that are relatively homogeneous (without large one-component domains) in broad pH range. At high pH, in a one-component ATR monolayer, a significant amount of molecules are in the anionic form and adopt a flat orientation versus the metal surface. At the same pH, in mixed ATR+MES monolayers, a significantly larger part of ATR molecules than for the respective one-component monolayer is adsorbed in the neutral form with the aromatic ring(s) oriented perpendicularly to the metal surface. Also in the mixed APY+MES and HTR+MES monolayers, a significantly smaller part of HTR or APY molecules than for the respective one-component HTR and APY monolayers is deprotonated. The structure of the MTR monolayer practically does not depend on the pH of the surrounding solution. Increase of the ratio of acidic dissociation and reorientation of ATR molecules from the perpendicular to the parallel orientation is also observed during storage of the respective one-component and mixed monolayers in water, phosphorus buffers, and in the solutions of model peptides (bovine serum albumin or laccase). In some cases, the reorientation of ATR molecules forming the linkage monolayer when immersed in the peptide solution is very large. Significant spectral changes during soaking in water and solutions of model peptides has also been observed for APY monolayers. All studied mixed monolayers practically prevent the direct adsorption of peptides on the metal surface for at least 30 min.
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PMID:Raman characterization of monolayers formed from mixtures of sodium 2-mercaptoethanesulfonate and various aromatic mercapto-derivative bases. 2035 51


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