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 kinetics of potassium triiodide (KI(3)) formation during fungal laccase action was investigated in presence of methyl syringate (MS). The recombinant forms of Polyporus pinsitus (rPpL), Myceliophthora thermophila (rMtL), Coprinus cinereus (rCcL), and Rhizoctonia solani (rRsL) laccases were used. The triiodide formation rate reached 6.1, 5.5, 6.0, and 2.1 microM/min at saturated rPpL, rCcL, rRsL, and rMtL concentration, respectively, in acetate buffer solution pH 5.5 and in presence of 10 microM of MS and 1 mM of potassium iodide. The triiodide formation rate increased if pH decreased from 6.5 to 4.5. The scheme of laccase-catalysed iodide oxidation includes stadium of MS interaction with oxidized laccase with concomitant production of MS(ox). The reaction of MS(ox) with iodide produced triiodide. The turnover number of MS was 93 and 44 at pH 5.5 for rPpL and rMtL, respectively. The scheme also contained a stadium of reversible reduction of laccase active centre with the mediator explaining the different saturation rate of triiodide production. The fitting kinetic data revealed that the reversibility of the reaction increased for laccases containing lower redox potential of copper type I.
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PMID:Laccase-catalysed iodide oxidation in presence of methyl syringate. 1608 Jan 84

The kinetics of oxidation of 4-hydroxybiphenyl (4-HBP) catalyzed by laccase from Polyporus pinsitus was studied in the presence of methyl syringate (MS), which acts as an electron-transfer mediator. Measurements were performed in 0.05 M acetate buffer, pH 5.5, in the presence of 4-HBP, MS, and laccase. It is shown that the oxidation rate of the lowly reactive substrate 4-HBP significantly increases during synergistic action of the highly reactive substrate MS. Bimolecular kinetic constants of interaction between the oxidized form of laccase and MS, the former and 4-HBP, and the oxidized form of MS and 4-HBP were calculated. A kinetic scheme of the synergistic substrate action is suggested; based on this scheme, the dependence of the initial rate on reagent concentration is derived. Analyzing experimental data, we obtained kinetic constants close to those obtained by modeling the processes.
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PMID:Mediator-assisted laccase-catalyzed oxidation of 4-hydroxybiphenyl. 1673 35

Response surface methodology (RSM) was successfully applied to enzymatic bio-transformation of 1-naphthol. The experiments were conducted in a closed system containing acetone and sodium acetate buffer, with laccase enzyme. Laccase enzyme used as catalyst was derived from Trametes versicolor (ATCC 200801). The enzymatic bio-transformation rate of 1-naphthol, based on measurements of initial dissolved oxygen (DO) consumption rate in the closed system, was optimized by the application of RSM. The independent variables, which had been found as the most effective variables on the initial DO consumption rate by screening experiments, were determined as medium temperature, pH and acetone content. A quadratic model was developed through RSM in terms of related independent variables to describe the DO consumption rate as the response. Based on contour plots and variance analysis, optimum operational conditions for maximizing initial DO consumption rate, while keeping acetone content at its minimum value, were 301 K of temperature, pH 6 and acetone content of 7% to obtain 9.17 x 10(-3) mM DO/min for initial oxidation rate.
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PMID:An approach for prediction of optimum reaction conditions for laccase-catalyzed bio-transformation of 1-naphthol by response surface methodology (RSM). 1805 8

ABSTRACT Manganese (Mn) oxidation by the plant-pathogenic fungus Gaeumannomyces graminis var. tritici has been correlated with virulence in take-all disease. The mechanism of Mn oxidation has not, however, been investigated adequately. Research on bacteria and other fungi indicates that Mn oxidation is most often the result of the activity of multicopper oxidases. To determine if G. graminis var. tritici oxidizes Mn by similar means, the Mn oxidizing factor (MOF) produced by G. graminis var. tritici was characterized by cultural, spectrophotometric, and cellulose acetate electrophoresis methods. Based on our results, the MOF is an extracellular enzyme with an estimated molecular weight of 50 to 100 kDa. Electrophoresis and spectrophotometry indicate that the MOF is a multicopper oxidase with laccase activity.
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PMID:Evidence of a Multicopper Oxidase in Mn Oxidation by Gaeumannomyces graminis var. tritici. 1894 15

The effect of copper on the expression of genes encoding the ligninolytic enzymes laccase (lcs) and manganese peroxidase (mnp) in Ceriporiopsis subvermispora was evaluated. This metal increased transcript levels of lcs, mnp1 and mnp2. This finding was not unexpected in the case of lcs, since its promoter contains a putative ACE element. Originally characterized in the yeast Saccharomyces cerevisiae, ACE is the target sequence of the ACE1 copper-responsive transcription factor in this microorganism. Analysis of the promoter regions of mnp genes revealed the presence of formerly unnoticed ACE elements. Based on the ace1 gene from Phanerochaete chrysosporium, we isolated and characterized an ACE1-like transcription factor from C. subvermispora (Cs-ACE1) through complementation of a S. cerevisiae ace1Delta strain. Surprisingly, ACE1 factors from both basidiomycetes exhibit substantial differences, not only structurally but also in their ability to complement the aforementioned yeast strain. Specific binding of Cs-ACE1 to its cognate DNA sequence was confirmed by electrophoretic mobility-shift assays.
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PMID:Expression of genes encoding laccase and manganese-dependent peroxidase in the fungus Ceriporiopsis subvermispora is mediated by an ACE1-like copper-fist transcription factor. 1895 50

Novel biosensors based on laccase from Aspergillus oryzae and the ionic liquids (ILs) 1-n-butyl-3-methylimidazolium hexafluorophosphate (BMIPF(6)) and 1-n-butyl-3-methylimidazolium tetrafluoroborate (BMIBF(4)) were constructed for determination of rosmarinic acid by square-wave voltammetry. The laccase catalyzes the oxidation of rosmarinic acid to the corresponding o-quinone, which is electrochemically reduced back to rosmarinic acid at +0.2V vs. Ag/AgCl. The biosensor based on BMIPF(6) showed a better performance than that based on BMIBF(4). The best performance was obtained with 50:20:15:15% (w/w/w/w) of the graphite powder:laccase:Nujol:BMIPF(6) composition in 0.1mol L(-1) acetate buffer solution (pH 5.0). The rosmarinic acid concentration was linear in the range of 9.99 x 10(-7) to 6.54 x 10(-5)mol L(-1) (r=0.9996) with a detection limit of 1.88 x 10(-7)mol L(-1). The recovery study for rosmarinic acid in plant extract samples gave values from 96.1 to 105.0% and the concentrations determined were in agreement with those obtained using capillary electrophoresis at the 95% confidence level. The BMIPF(6)-biosensor demonstrated long-term stability (300 days; 920 determinations) and reproducibility, with a relative standard deviation of 0.56%.
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PMID:Biosensor based on laccase and an ionic liquid for determination of rosmarinic acid in plant extracts. 1908 43

To immobilize laccase (Lac) from Trametes versicolor that shows its maximum enzymatic activity in acidic aqueous solutions, the biopolymer chitosan (CS) was chemically modified with glutaraldehyde (GA) to form GA functionalized CS (GAfCS), which was then allowed to react with Lac to form a Lac-GAfCS composite that is robust in weakly acidic solutions (two-step protocol), as confirmed by quartz crystal microbalance and durability tests. The Lac-GAfCS-multiwalled carbon nanotubes (MWCNTs)/glassy carbon (GC) electrode exhibited good catalytic activity towards O(2) reduction in the presence of 2,2'-azinobis (3-ethylbenzothiazoline-6-sulfonate) diammonium salt (ABTS), and the pH-dependent enzymatic activity of the immobilized Lac towards O(2) reduction was examined. A glucose/air biofuel cell was fabricated, with the Lac-GAfCS-MWCNTs/GC electrode as the biocathode and a glucose oxidase (GOx)-GAfCS-MWCNTs/GC electrode as the bioanode in a Nafion membrane-separated acetate buffer solution (pH 5.0). The biofuel cell output a maximum power density of 9.6 microW/cm(2), an open-circuit cell voltage of 0.19V, and a short-circuit current density of 114 microA/cm(2), respectively, as measured with an electrochemical noise (ECN) apparatus. Furthermore, the Lac-GAfCS-MWCNTs/GC electrode was applied to determine catechol in Britton-Robinson buffer solution (pH 3.0), with a linear range of 0.1-50 microM and a limit of detection of 20 nM. In comparison with the direct use of GA for one-pot Lac-GA-CS or Lac-GA crosslinking to immobilize Lac, the use of macromolecular GAfCS in the proposed two-step protocol was proven to be less harmful to the enzymatic activity and thus more suitable for immobilizing the enzyme to construct the biofuel cell and biosensor. This work may be helpful for exploiting the popular biocompatible CS as an acid-resistant film matrix for many other biotechnology applications, and the proposed two-step crosslinking protocol is recommended for high-activity immobilization of other biomolecules.
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PMID:Biofuel cell and phenolic biosensor based on acid-resistant laccase-glutaraldehyde functionalized chitosan-multiwalled carbon nanotubes nanocomposite film. 1915 37

Biosensors based on hydrophobic ionic liquids (ILs) derived from the bis(trifluoromethylsulfonyl)imide [(CF(3)SO(2))(2)N(-) = Tf(2)N(-)] anion associated with three different imidazolium cations: 1-butyl-3-methylimidazolium (BMI x Tf(2)N), 1-decyl-3-methylimidazolium (DMI x Tf(2)N) and 1-tetradecyl-3-methylimidazolium (TDMI x Tf(2)N), along with laccase from Aspergillus oryzae, were constructed and optimized for determination of rutin. The laccase catalyzes the oxidation of rutin to the corresponding o-quinone, which is electrochemically reduced back to rutin. The best performance was obtained with 50:20:15:15% (w/w/w/w) as the graphite powder:laccase:Nujol:ILs composition in 0.1 mol L(-1) acetate buffer solution (pH 5.0). The parameters for the square-wave voltammetry experiments and scanning electron microscopy images of the biosensors were studied. Under the selected conditions, the cathodic peak current increased linearly in the rutin concentration ranges of 4.77x10(-6) to 4.62x10(-5) mol L(-1), 5.84x10(-6) to 5.36x10(-5) mol L(-1) and 5.84x10(-6) to 5.36x10(-5) mol L(-1) using the (I) BMI x Tf(2)N-laccase, (II) DMI x Tf(2)N-laccase and (III) TDMI x Tf(2)N-laccase, respectively. The rutin contents of commercial samples of pharmaceuticals were successfully determined by the biosensors and the results compared well with those obtained using the official method. The studies on rutin recovery from these samples gave values of 96.9-104.6%.
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PMID:Development of biosensors containing laccase and imidazolium bis(trifluoromethylsulfonyl)imide ionic liquid for the determination of rutin. 1934 64

Novel aerobic, Gram-negative bacteria with DNA G+C contents below 50 mol% were isolated from the culturable microbiota associated with the Mediterranean seagrass Posidonia oceanica. 16S rRNA gene sequence analyses revealed that they belong to the genus Marinomonas. Strain IVIA-Po-186 is a strain of the species Marinomonas mediterranea, showing 99.77 % 16S rRNA gene sequence similarity with the type strain, MMB-1(T), and sharing all phenotypic characteristics studied. This is the first description of this species forming part of the microbiota of a marine plant. A second strain, designated IVIA-Po-101(T), was closely related to M. mediterranea based on phylogenetic studies. However, it differed in characteristics such as melanin synthesis and tyrosinase, laccase and antimicrobial activities. In addition, strain IVIA-Po-101(T) was auxotrophic and unable to use acetate. IVIA-Po-101(T) shared 97.86 % 16S rRNA gene sequence similarity with M. mediterranea MMB-1(T), but the level of DNA-DNA relatedness between the two strains was only 10.3 %. On the basis of these data, strain IVIA-Po-101(T) is considered to represent a novel species of the genus Marinomonas, for which the name Marinomonas balearica sp. nov. is proposed. The type strain is IVIA-Po-101(T) (=CECT 7378(T) =NCIMB 14432(T)). A third novel strain, IVIA-Po-185(T), was phylogenetically distant from all recognized Marinomonas species. It shared the highest 16S rRNA gene sequence similarity (97.4 %) with the type strain of Marinomonas pontica, but the level of DNA-DNA relatedness between the two strains was only 14.5 %. A differential chemotaxonomic marker of this strain in the genus Marinomonas is the presence of the fatty acid C(17 : 0) cyclo. Strain IVIA-Po-185(T) is thus considered to represent a second novel species of the genus, for which the name Marinomonas pollencensis sp. nov. is proposed. The type strain is IVIA-Po-185(T) (=CECT 7375(T) =NCIMB 14435(T)). An emended description of the genus Marinomonas is given based on the description of these two novel species, as well as other Marinomonas species described after the original description of the genus.
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PMID:Taxonomic study of Marinomonas strains isolated from the seagrass Posidonia oceanica, with descriptions of Marinomonas balearica sp. nov. and Marinomonas pollencensis sp. nov. 1964 36

Novel and effective biosensors based on Ag or Au nanoparticles dispersed in ionic liquid (IL) 1-butyl-3-methylimidazolium hexafluorophosphate (BMI.PF(6)) and laccase (Lac) from Aspergillus oryzae immobilized in chitosan (Chi) chemically cross-linked with cyanuric chloride (CC) were constructed. This enzyme catalyzes the oxidation of luteolin to the corresponding o-quinone, which is electrochemically reduced back to luteolin at 0.35 V vs. Ag/AgCl. Square-wave voltammetry was used for the electrochemical determination of luteolin at the Lac-nanoparticles-BMI.PF(6) biosensors. The best performance was obtained with 50:20:15:15% (w/w/w/w) as the graphite powder:Chi-CC:Nujol:Ag-BMI.PF(6) or Au-BMI.PF(6) composition (Lac 0.29 units mL(-1)) in 0.1 M acetate buffer solution (pH 4.0) with frequency, pulse amplitude and scan increment at 50 Hz, 100 mV, and 5.0 mV, respectively. Under optimized conditions, the cathodic currents increased linearly for the luteolin concentration range of 0.099-5.825 microM with detection limits of 0.054 +/- 0.004 microM (Ag-BMI.PF(6)) and 0.028 +/- 0.002 microM (Au-BMI.PF(6)). These biosensors demonstrated high sensitivity, good repeatability and reproducibility, and long-term stability (13% decrease in response over 70 days). The recovery study for luteolin in chamomile tea samples gave values of 91.8-104.8%. The influence of Lac immobilized in Chi-CC and nanoparticles-BMI.PF(6) contributes to the excellent performance of the biosensors.
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PMID:Biosensor for luteolin based on silver or gold nanoparticles in ionic liquid and laccase immobilized in chitosan modified with cyanuric chloride. 1983 22


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