Effect of Initial GnRH and Duration of Progesterone Insert Treatment on the Fertility of Lactating Dairy Cows

The study compared response to prostaglandin F2α (PG), synchrony of ovulation and pregnancy per AI (P/AI) in a 5‐ vs a 7‐day Ovsynch + PRID protocol and investigated whether the initial GnRH affects P/AI in lactating dairy cows. Two hundred and seventy‐six cows (500 inseminations) were assigned to one of four timed‐AI (TAI) protocols: (i) PRID‐7G; 100 μg GnRH im, and a progesterone‐releasing intravaginal device (PRID) for 7 days. At PRID removal, PG (500 μg of cloprostenol) was given im. Cows received the second GnRH treatment at 60 h after PRID removal and TAI 12 h later. (ii) PRID‐5G; as PRID‐7G except the duration of PRID, treatment was 5 days and PG was given twice (12 h apart). (iii) PRID‐7NoG; as PRID‐7G except the initial GnRH, treatment was omitted. (iv) PRID‐5NoG; as PRID‐7NoG except the duration of PRID, treatment was 5 days. Response to treatments and pregnancy status at 32 and 60 days after TAI was determined by ultrasonography. The percentage of cows ovulating before TAI was greatest in PRID‐7G (17.1%), and the percentage of cows that did not have luteal regression was greatest in PRID‐5G (9.5%). The overall P/AI at 32 and 60 days did not differ among TAI protocols. However, during resynchronization, cows subjected to the 5‐day protocols had greater (p < 0.05) P/AI (45.3% vs 33.6%) than cows subjected to the 7‐day protocols. Pregnancy loss between 32 and 60 days tended (p = 0.10) to be greater in cows that did not receive initial GnRH (14.8%) compared to those that received GnRH (8.2%). In conclusion, the PRID‐5G protocol resulted in fewer cows responding to PG, but P/AI did not differ among TAI protocols. A 5‐day protocol resulted in more P/AI in resynchronized cows, and cows that did not receive initial GnRH tended to experience more pregnancy losses.     

Isothermal titration calorimetry study of pectin-ionic surfactant interactions

Isothermal titration calorimetry (ITC) was used to measure enthalpy changes resulting from injection of anionic (sodium dodecyl sulfate, SDS) or cationic (dodecyl trimethylammonium bromide, DTAB) surfactants into aqueous 1 wt % pectin solutions (30, 60, or 90% methoxylated). In the absence of pectin, the critical micelle concentrations (cmc) determined by ITC were 14.7 mM for DTAB and 7.7 mM for SDS. Binding of DTAB to pectin was endothermic and was attributed to electrostatic attraction between the cationic surfactant and anionic biopolymer. Binding of SDS to pectin was exothermic and was attributed to hydrophobic interactions. Pectin reduced the cmc of SDS, probably because of long-range electrostatic repulsion between the molecules. Above a particular concentration, which depended on pectin and surfactant type, both ionic surfactants promoted pectin aggregation (monitored by turbidity increase). This study demonstrates the potential of ITC for providing valuable information about interactions between polysaccharides and amphiphiles.     

Production and characterization of O/W emulsions containing cationic droplets stabilized by lecithin-chitosan membranes

Oil-in-water emulsions containing cationic droplets stabilized by lecithin-chitosan membranes were produced using a two-stage process. A primary emulsion was prepared by homogenizing 5 wt % corn oil with 95 wt % aqueous solution (1 wt % lecithin, 100 mM acetic acid, pH 3.0) using a high-pressure valve homogenizer. This emulsion was diluted with aqueous chitosan solutions to form secondary emulsions with varying compositions: 1 wt % corn oil, 0.2 wt % lecithin, 100 mM acetic acid, and 0-0.04 wt % chitosan (pH 3.0). The particle size distribution, particle charge, and creaming stability of the primary and secondary emulsions were measured. The electrical charge on the droplets increased from -49 to +54 mV as the chitosan concentration was increased from 0 to 0.04 wt %, which indicated that chitosan adsorbed to the droplet surfaces. The mean particle diameter of the emulsions increased dramatically and the emulsions became unstable to creaming when the chitosan concentration exceeded 0.008 wt %, which was attributed to charge neutralization and bridging flocculation effects. Sonication, blending, or homogenization could be used to disrupt flocs formed in secondary emulsions containing droplets with high positive charges, leading to the production of emulsions with relatively small particle diameters (approximately 1 microm). These emulsions had good stability to droplet aggregation at low pH (< or =5) and ionic strengths (<500 mM). The interfacial engineering technology utilized in this study could lead to the creation of food emulsions with improved stability to environmental stresses.     

Consistency and solubility changes in herring (Clupea harengus) light muscle homogenates as a function of pH

Fish muscle proteins can be isolated from a variety of low-value raw materials by solubilization in either acid or base. If the consistency of the resulting solution is sufficiently low, it is possible to recover most of the solubilized proteins and remove most of the lipids by centrifugation. Lipid removal should greatly stabilize the isolated proteins. In a previous investigation into the use of herring for production of these protein isolates, it was observed that this species had particularly high consistency values when the proteins were solubilized. This study was undertaken to determine the consistencies obtained with herring light muscle tissue over the pH range covered by the two processes, from about pH 2.7 to 10.8. Protein solubility was compared to consistency of the resultant solutions. Maximum consistencies of the homogenates, approximately 220 and approximately 175 mPa.s, were obtained at pH values of approximately 3.5 and 10.5, respectively. Consistency began to increase approximately when solubilization began. Storage of homogenates at pH 2.7 decreased the consistency over a 10 min time period. The magnitude of the consistency peaks at both acid and alkaline pH values increased when using ice-stored as well as frozen-stored herring, especially in the acid range. Protein solubility at pH <4 and pH >/=10.8 slightly decreased after post-mortem storage of the herring muscle. It is suggested that the observed changes in consistency result from the expansion and solvation of protein aggregates which eventually dissociate into smaller units, perhaps even monomers.     

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.     

Combined influence of NaCl and sucrose on heat-induced gelation of bovine serum albumin

The combined influence of a strongly interacting cosolvent (NaCl) and a weakly interacting cosolvent (sucrose) on the heat-induced gelation of bovine serum albumin (BSA) was studied. The dynamic shear rheology of 4 wt % BSA solutions containing 0 or 20 wt % sucrose and 0-200 mM NaCl was monitored as they were heated from 30 to 90 degrees C at 1.5 degrees C min(-)(1), held at 90 degrees C for 120 min, and then cooled back to 30 degrees C at -1.5 degrees C min(-)(1). The turbidity of the same solutions was monitored as they were heated from 30 to 95 degrees C at 1.5 degrees C min(-)(1) or held isothermally at 90 degrees C for 10 min. NaCl had a similar effect on BSA solutions that contained 0 or 20 wt % sucrose, with the gelation temperature decreasing and the final gel strength increasing with increasing salt concentration and the greatest changes occurring between 25 and 100 mM NaCl. Nevertheless, the presence of sucrose did lead to an increase in the gelation temperature and final gel strength and a decrease in the final gel turbidity. The impact of NaCl on gel characteristics was attributed primarily to its ability to screen electrostatic interactions between charged protein surfaces, whereas the impact of sucrose was attributed mainly to its ability to increase protein thermal stability and strengthen the attractive forces between proteins through a preferential interaction mechanism.     

Impact of lipid physical state on the oxidation of methyl linolenate in oil-in-water emulsions

The purpose of this research was to examine the influence of the physical state of lipids on iron-promoted oxidation of methyl linolenate in octadecane oil-in-water emulsions. Octadecane and methyl linolenate oil-in-water emulsions were prepared that contained droplets having the octadecane as either liquid or solid. The physical state of the octadecane was confirmed by a differential scanning calorimeter (DSC). The effect of the physical state of the lipid on oxidation rates was determined as a function of iron concentration (80 and 160 microM), pH (3.0 or 7.0), emulsifier type, and cooling rate. Oxidation of methyl linolenate was determined by lipid hydroperoxides and thiobarbituric acid reactive substances (TBARS). Emulsions containing solid octadecane had higher rates of lipid hydroperoxide and TBARS formation than those containing liquid octadecane. The rate at which the emulsions were cooled had no influence on oxidation rates. Oxidation rates in both emulsions increased with increasing iron concentration and decreasing pH. Oxidation rates were lowest in emulsions with cationic droplet membranes (dodecyl trimethylammonium bromide-stabilized), presumably due to the repulsion of iron from the oxidizable methyl linolenate in the emulsion droplet core. These results suggest that upon crystallization of octadecane, the liquid methyl linolenate migrated to the emulsion droplet surface, where it was more prone to oxidation because it was in closer contact with the iron ions in the aqueous phase.     

Properties of low-moisture viscoplastic materials consisting of oil droplets dispersed in a protein-carbohydrate-glycerol matrix: effect of oil concentration

The influence of oil concentration and baking on the properties of low-moisture composites consisting of oil droplets dispersed in a protein-carbohydrate-glycerol matrix was investigated. These composites were produced by blending canola oil, whey protein concentrate (WPC), corn syrup, and glycerol together using a high-speed mixer. The resulting system consisted of oil droplets dispersed in a polar matrix. Some composites were analyzed directly after preparation, while others were analyzed after being heated at 176 degrees C for 10 min to simulate baking. The "lightness" of the composites was greater before baking (higher L value), but the color was more intense after baking (higher a and b values). The lightness and color intensity of the composites decreased as the oil concentration increased, with the effects being more pronounced in the baked samples. The zeta potential of the oil droplets (measured after dilution at pH 6) was highly negative (approximately -40 mV), indicating that whey protein was adsorbed to the droplet surfaces. The mean particle diameter (measured after dilution at pH 6) increased appreciably after baking, which was attributed to droplet flocculation. The rheological properties of the unbaked and baked materials were characterized by squeezing flow viscometry, which showed that the measurements associated with consistency and yield stress increased with increasing oil concentration and with baking.     

Ability of lipid hydroperoxides to partition into surfactant micelles and alter lipid oxidation rates in emulsions

Lipid hydroperoxides are important factors in lipid oxidation due to their ability to decompose into free radicals. In oil-in-water emulsions, the physical location of lipid hydroperoxides could impact their ability to interact with prooxidants such as iron. Interfacial tension measurements show that linoleic acid, methyl linoleate, and trilinolein hydroperoxides are more surface-active than their non-peroxidized counterparts. In oil-in-water emulsion containing surfactant (Brij 76) micelles in the continuous phase, linoleic acid, methyl linoleate, and trilinolein hydroperoxides were solubilized out of the lipid droplets into the aqueous phase. Brij 76 solubilization of the different hydroperoxides was in the order of linoleic acid > trilinolein > or = methyl linoleate. Brij 76 micelles inhibited lipid oxidation of corn oil-in-water emulsions with greater inhibition of oxidation occurring in emulsions containing linoleic acid hydroperoxides. Surfactant solubilization of lipid hydroperoxides could be responsible for the ability of surfactant micelles to inhibit lipid oxidation in oil-in-water emulsions.     

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.