Amount Of P-nitrophenol Research Articles

Synthesis of enzymes connected with mycoparasitism by ectomycorrhizal fungi

The production of enzymes involved in mycoparasitism by several strains of ectomycorrhizal fungi: Amanita muscaria (16-3), Laccaria laccata (9-12), L. laccata (9-1), Suillus bovinus (15-4), S. bovinus (15-3), S. luteus (14-7) on different substrates such as colloidal chitin, mycelia of Trichoderma harzianum, T. virens and Mucor hiemalis was examined. Chitinases and beta-1,3-glucanases were assayed spectrophotometrically by measuring the amount of reducing sugars releasing from suitable substrate by means of Miller's method. Beta-glucosidases were determined by measuring the amount of p-nitrophenol released from p-nitrophenyl-beta-D-glucopyranoside. It was observed that A. muscaria (16-3) and L. laccata (9-12) biosynthesized the highest activity of enzymes in contrast to the strains of S. bovinus and S. luteus. The mycelium of T. harzianum turned out to be the best substrate for the induction of beta-1,3-glucanases and beta-glucosidases for both strains of L. laccata, although the difference in the induction of chitinases in the presence of mycelia of different species of Trichoderma was not indicated.

Solvation ofp-Nitrophenol at a Water/Alkane Interface: The Role of Ionic Strength and Salt Identity

Second harmonic generation (SHG), a surface specific, nonlinear optical spectroscopy, was used to study the interfacial solvation of a neutral surfactant, p-nitrophenol (PNP), adsorbed to the water/cyclohexane interface in the presence of simple salts at varying salt concentrations. The purpose of this work was to determine what relationship (if any) exists between interfacial polarity and bulk solution ionic strength. Data show an apparent red shift in SHG spectra with an increase in salt anion size from fluoride to chloride to bromide at 1 M salt concentrations. A spectral red shift of the PNP electronic excitation implies an increase in local polarity. Within experimental limits, however, these observed interfacial spectral shifts mimic shifts in absorbance spectra observed for PNP in bulk electrolyte solutions. Given the similarities between bulk and surface behavior, we conclude that observed shifts in SHG spectra may be attributed to effects similar to those found in bulk solution. Additionally, the surface adsorption of PNP to the water/cyclohexane interface was studied to determine the surface distribution of PNP and the conjugate base, p-nitrophenoxide (PNP(-)), for a 10 mM PNP solution. PNP adsorption is favored over PNP(-) adsorption by a factor of 10, giving rise to an equilibrium surface distribution that is an order of magnitude greater than that found in bulk solution. These findings indicate that the amount of PNP(-) at the surface in an aqueous solution of 10 mM PNP is negligible.

Facile formation of water-insoluble cyclodextrin/Nafion composite films on solid surfaces

The water-insoluble poly- β-cyclodextrin (poly-CD)/Nafion composite film was easily prepared by casting a mixed solution of poly-CD and Nafion onto substrate plates. FT-IR measurements showed that the 50/50 wt% poly-CD/Nafion composite film remained stable on the glass and quartz substrates after immersion in water for more than 3 h, while a pure poly-CD film was almost completely dissolved by immersion within 1 h. The film stability was also evaluated from the amount of p-nitrophenol ( p-NP) inclusion in the film, which was determined from the decrease in UV–vis absorbance of the p-NP solution into which the film was immersed. The composition dependence of the inclusion amount showed that the film was stable up to 50 wt% CD, but became less stable with further increase in the CD concentration in the film. From the isotherms for the inclusion of p-NP and 1-naphthoate (1-Naph) into the film, the inclusion (stability) constants were determined to be 3.7 × 10 3 M −1 and 1.9 × 10 2 M −1 , respectively. These results show that the selective inclusion of CD is retained after preparation of the composite film.

Adsorption Capacities of Activated Carbons Derived from Rice Straw and Water Hyacinth in the Removal of Organic Pollutants from Water

Two activated carbons were prepared from unconventional raw materials, i.e. rice straw (RS) and water hyacinth (WH), using the same activation scheme, i.e. impregnation with 50 vol% H3 PO4 followed by pyrolysis at 500°C. The porosity characteristics of the samples were determined via nitrogen adsorption studies at -196°C from which the various parameters were evaluated. WH carbon showed a more developed porosity relative to RS, although both carbons were apparently of low quality. The capacities of both samples towards the removal from aqueous solution of five organic sorbates were tested. These were phenol (P), p-nitrophenol (PNP), p-nitroaniline (PNA), Methylene Blue (MB) and Congo Red (CR). The adsorption of the two dyes (MB and CR) was a function of the pore dimensions, whereas phenol uptake was greatly reduced because of the acidic oxygen functional groups on the carbon surface. The amount of PNP taken up corresponded exactly with the specific surface area as estimated from nitrogen isotherm measurem...

Detection of ouabain-insensitive H(+)-transporting, K(+)-stimulated p-nitrophenylphosphatase activity in rat gastric glands by cerium-based cytochemistry.

We employed a modification of our previously reported cerium-based cytochemical method for ouabain-sensitive, K-dependent p-nitrophenylphosphatase (Na-K ATPase) activity to detect ouabain-insensitive, K-stimulated p-nitrophenylphosphatase (K-pNPPase) activity in rat gastric glands. Biochemically, the enzyme activity of gastric glands incubated in a medium containing 50 mM Tricine buffer (pH 7.5), 50 mM KCl, 10 mM MgCl2, 2 mM CeCl3, 2 mM p-nitrophenylphosphate (pNPP), 2.5 mM levamisole, 10 mM ouabain, and 0.00015% Triton X-100, was optimal at pH 7.5-8.0 and decreased above pH 8.5. The amount of p-nitrophenol after incubation increased linearly in proportion to the amount of tissue in the medium. The enzyme activity was inhibited by omeprazole, sodium flouride (NaF), N-ethylmaleimide (NEM), and dicyclohexylcarbodiimide (DCCD). Heat-treated specimens had no enzyme activity. The enzyme activity increased with addition of K ions up to the concentration of 50 mM, and became constant above 50 mM. Cytochemically, the parietal cells of the gastric glands reacted positively for ouabain-insensitive K-pNPPase activity. Intense reaction was observed at the microvilli of the luminal surface and the intracellular canaliculi. The tubulovesicular system showed weak enzyme activity. The reaction products were found as fine, granular, electron-dense deposits in the cytoplasm just beneath the plasma membrane. The ouabain-insensitive K-pNPPase activity detected in this study appears, therefore, to be associated with that of H-transporting, K-stimulated adenosine triphosphatase (H-K ATPase).

THE ADSORPTION OF PHENOL ON ANION EXCHANGE RESINS IN THE PRESENCE OF p-NITROPHENOL

A Freundlich-type multicomponent adsorption isotherm based on the ideal adsorbed solution theory is used to examine the experimental data of the adsorption of phenol in the presence of p-nitrophenol. A good agreement between the experimental data and the predicted results is obtained. Moreover, when the adsorbed amount of p-nitrophenol is kept constant, the adsorption isotherm of phenol is linear, and the slope is dependent on the adsorbed amount of p-nitrophenol.

Preparation of non-reducing-end substituted p-nitrophenyl alpha-maltopentaoside (FG5P) as a substrate for a coupled enzymatic assay for alpha-amylases.

p-Nitrophenyl O-6-deoxy-6-[(2-pyridyl)amino]-alpha-D-glucopyranosyl-(1----4)-O-alpha-D - glucopyranosyl-(1----4)-O-alpha-D-glucopyranosyl-(1----4)-O-alpha-D- glucopyranosyl-(1----4)-alpha-D-glucopyranoside, FG5P, was prepared, taking advantage of the action of Bacillus macerans cyclodextrin glucanotransferase on a mixture of O-6-deoxy-6-[(2-pyridyl)-amino]-alpha-D-glucopyranosyl-(1----4)-O-alpha- D- glucopyranosyl-(1----4)-O-alpha-D-glucopyranosyl-(1----4)-O-alpha-D- glucopyranosyl-(1----4)-O-alpha-D-glucopyranosyl-(1----4)-D-glucose and p-nitrophenyl alpha-glucoside. The maltopentaose derivative is resistant to alpha-glucosidase and is suitable as a substrate for the alpha-amylase assay coupled with alpha-glucosidase in which the activity of alpha-amylase is determined by measuring the amount of p-nitrophenol liberated by alpha-glucosidase from p-nitrophenyl alpha-glucoside and p-nitrophenyl alpha-maltoside produced by the action of alpha-amylase. This alpha-amylase assay method was applied for determination of alpha-amylases in human serum.

Dual role of esterases in insecticide resistance in the green rice leafhopper

The role of esterases as related to insecticide resistance was studied in an organophosphorus (OP)-resistant strain of the green rice leafhopper. As judged by p-nitrophenyl acetate hydrolysis, 21, 5, and 74% of the esterase activity was located in nuclei/mitochondria, microsomes, and the soluble fraction, respectively. All the fractions were active in hydrolyzing malathion, paraoxon, and fenvalerate. Hydrolysis of malathion and fenvalerate increased with time while that of paraoxon reached a plateau within 15 min. Since a considerable amount of p-nitrophenol was detected in the paraoxon reaction at 0°C and at zero time, the formation of p-nitrophenol may be due to phosphorylation of the esterases rather than phosphorotriesterase action. The results suggest a dual role for esterases in resistance mechanisms; a catalyst for hydrolysis of malathion and fenvalerate, and a binding protein for the oxygen analogs of other OP insecticides, both of which would protect the intrinsic target, acetylcholinesterase, from inhibition. Chromatofocusing of the soluble fraction resolved five esterase peaks, I–V. These esterases were active toward the three general substrates as well as for the three insecticides tested, except for Peak I in which the overall activity was too low. Thin-layer agar gel electrophoresis showed that the chromatofocusing peaks I–V corresponded to the electrophoretic bands E 1–E 5, some of which were previously shown to be associated with OP resistance. The dual role of these esterases may explain the cross-resistance between malathion and other OP insecticides as well as synergism between OP and carbamate insecticides.