Density Dependent Grazing In Estuarine Water Quality Models

The objective of this study is to examine the influence different zooplankon grazing rate relationships have on water quality eutrophication model results in a tidal estuary. The water quality model being used includes phytoplankton and both dissolved and particulate constituents as state variables. It includes zooplankton grazing of the phytoplankton, where excretions from the latter increase the particulate constituents. The phytoplankton and particulate constituents also undergo settling. When applied to an existing estuary, the model results are different for a first order zooplankton grazing rate formulation than for a second order zooplankton grazing rate formulation.Constituents enter the estuary as wastewater discharges, freshwater river inflows, exchanges between the sediment and water interface, and exchange across the tidal boundary. The water quality model is coupled with a three-dimensional time varying hydrodynamic and transport model that allows accurate computation of the tidal velocity field transporting the constituents from their sources throughout the estuary. Comparisons of model results between the first order and the second order density dependent zooplankton grazing relationships allow determining which of the two processes best describe water quality behavior for the estuary being examined. The second order density dependent zooplankton grazing relationship performs best in application.     

Detection of polycyclic aromatic hydrocarbon levels in milk collected near potential contamination sources

Polycyclic aromatic hydrocarbons (PAHs), mainly formed by incomplete anthropogenic organic matter combustion, are ubiquitous in the environment. To assess milk PAH contamination sources, milk samples were collected from the tank milk at farms located near potential contaminating emission sources such as cementworks, steelworks, and motorways. PAH analyses were carried out by gas chromatography coupled to mass spectrometry. Eight PAHs were identified in milk: naphthalene, acenaphthylene, acenaphthene, fluorene, anthracene, fluoranthene, pyrene, and benzo[a]anthracene. For all potential contaminating sources, these eight PAHs were detected with similar profiles and at low concentrations except for fluorene and naphthalene, for which source-molecule interaction is pointed out.     

Role of continuous phase protein on the oxidative stability of fish oil-in-water emulsions

Whey protein isolate (WPI), soy protein isolate (SPI), and sodium caseinate (CAS) can inhibit lipid oxidation when they produce a positive charge at the interface of emulsion droplets. However, when proteins are used to stabilize oil-in-water emulsions, only a fraction of them actually absorb to the emulsion droplets, with the rest remaining in the continuous phase. The impact of these continuous phase proteins on the oxidative stability of protein-stabilized emulsions is not well understood. WPI-stabilized menhaden oil-in-water emulsions were prepared by high-pressure homogenization. In some experiments WPI was removed from the continuous phase of the emulsions through repeated centrifugation and resuspension of the emulsion droplets (washed emulsion). Unwashed emulsions were more oxidatively stable than washed emulsions at pH 7.0, suggesting that continuous phase proteins were antioxidative. The oxidative stability of emulsions containing different kinds of protein in the continuous phase decreased in the order SPI > CAS > WPI, as determined by both hydroperoxide and headspace propanal formation. Iron-binding studies showed that the chelating ability of the proteins decreased in the order CAS > SPI > WPI. The free sulfhydryls of both WPI and SPI were involved in their antioxidant activity. This research shows that continuous phase proteins could be an effective means of protecting omega-3 fatty acids from oxidative deterioration.     

Lipid oxidation in corn oil-in-water emulsions stabilized by casein,whey protein isolate,and soy protein isolate

Proteins can be used to produce cationic oil-in-water emulsion droplets at pH 3.0 that have high oxidative stability. This research investigated differences in the physical properties and oxidative stability of corn oil-in-water emulsions stabilized by casein, whey protein isolate (WPI), or soy protein isolate (SPI) at pH 3.0. Emulsions were prepared with 5% corn oil and 0.2-1.5% protein. Physically stable, monomodal emulsions were prepared with 1.5% casein, 1.0 or 1.5% SPI, and > or =0.5% WPI. The oxidative stability of the different protein-stabilized emulsions was in the order of casein > WPI > SPI as determined by monitoring both lipid hydroperoxide and headspace hexanal formation. The degree of positive charge on the protein-stabilized emulsion droplets was not the only factor involved in the inhibition of lipid oxidation because the charge of the emulsion droplets (WPI > casein > or = SPI) did not parallel oxidative stability. Other potential reasons for differences in oxidative stability of the protein-stabilized emulsions include differences in interfacial film thickness, protein chelating properties, and differences in free radical scavenging amino acids. This research shows that differences can be seen in the oxidative stability of protein-stabilized emulsions; however, further research is needed to determine the mechanisms for these differences.     

Production and characterization of oil-in-water emulsions containing droplets stabilized by beta-lactoglobulin-pectin membranes

Oil-in-water emulsions containing droplets stabilized by beta-lactoglobulin (beta-Lg)-pectin membranes were produced using a two-stage process. A primary emulsion containing small droplets (d(32) approximately 0.3 microm) was prepared by homogenizing 10 wt % corn oil with 90 wt % aqueous solution (1 wt % beta-Lg, 5 mM imidazole/acetate buffer, pH 3.0) using a high-pressure valve homogenizer. The primary emulsion was then diluted with pectin solutions to produce secondary emulsions with a range of pectin concentrations (5 wt % corn oil, 0.45 wt % beta-Lg, 5 mM imidazole/acetate buffer, 0-0.22 wt % pectin, pH 3.0). The electrical charge on the droplets in the secondary emulsions decreased from +33 +/- 3 to -19 +/- 1 mV as the pectin concentration was increased from 0 to 0.22 wt %, which indicated that pectin adsorbed to the droplet surfaces. The mean particle diameter of the secondary emulsions was small (d(32) < 1 microm) at relatively low pectin concentrations (<0.04 wt %), but increased dramatically at higher pectin concentrations (e.g., d(32) approximately 13 microm at 0.1 wt % pectin), which was attributed to charge neutralization and bridging flocculation effects. Emulsions with relatively small mean particle diameters (d(32) approximately 1.2 microm at 0.1 wt % pectin) could be produced by disrupting flocs formed in secondary emulsions containing highly negatively charged droplets, for example, by sonication, blending, or homogenization. The particles in these emulsions probably consisted of small flocs containing a number of protein-coated droplets bound together by pectin molecules. These emulsions had good stability to further particle aggregation up to relatively high ionic strengths (< or =500 mM NaCl) and low pH (pH 3). The interfacial engineering technology used in this study could lead to the creation of food emulsions with improved physicochemical properties or stability.     

Disorders of the pharynx.

Pharyngeal disorders are complex and difficult to treat. Disorders that lead to anatomic derangement, such as trauma and neoplasia, can significantly affect the function of this organ. Pharyngeal dysfunction can manifest as dysphagia, persistent palatal displacement, or exercise intolerance. Secondary complications are serious and life threatening and include aspiration pneumonia, weight loss, and death. Pharyngeal disorders that are only recognizable during strenuous exercise are difficult to diagnose and are treated with limited success, even though they are responsible for significant economic losses with performance animals.     

Degradation of the herbicide flamprop-methyl in soil

The degradation of the wild oat herbicide flamprop-methyl [methyl DL -N-benzoyl-N-(3-chloro-4-fluorophenyl)alaninate] in four soils has been studied under laboratory conditions using ¹⁴C-1abelled samples. The flamprop-methyl underwent degradation more rapidly than its analogue flamprop-isopropyl. However, similar degradation products were formed, namely the corresponding carboxylic acid and 3-chloro-4-fluoroaniline. The latter compound occurred mainly as ‘bound’ forms although evidence was obtained of limited ring-opening to give [¹⁴C]carbon dioxide. The time for depletion of 50% of the applied herbicide was approximately 1-2 weeks in sandy loam, clay and medium loam soils and 2-3 weeks in a peat soil.     

Detection of Escherichia coli strains producing cytotoxic necrotizing factor type two (CNF2) by enzyme-linked immunosorbent assay

Sheep and rabbit antisera were produced against lysates of E. coli strain 711 (pVir). This K-12 strain carries the Vir plasmid which codes for Cytotoxic Necrotizing Factor type 2 (CNF2). Immunoglobulin G (IgG) fractions of both immune sera were subsequently purified by a two-step precipitation method. To increase the specificity for CNF2, the sheep IgG preparation was extensively adsorbed against both a sonicated extract of isogenic K-12 strain 711 and intact phenol-treated cells of vaccine strain 711 (pVir). An enzyme-linked immunosorbent assay (ELISA) was developed to detect clinical isolates of E. coli producing CNF2, using the final preparations of rabbit and sheep IgG in a double sandwich technique. The results obtained with this CNF2-ELISA were compared to those obtained with the conventional HeLa cell cytotoxicity assay. The testing of 133 E. coli strains (49 CNF2 positive strains and 84 negative strains) resulted in no false-negative and no false-positive. Therefore, the CNF2-ELISA offers a good alternative to the HeLa cell culture assay for the detection of CNF2-producing strains where facilities for and experience with cell cultures is lacking.