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At least 19 recordsLinked to original sources

PubMed1999

Rheological properties and characterization of polymerized whey protein isolates.

Whey protein polymers were formed by heating whey protein isolate solutions at 80 degrees C. Flow behaviors of whey protein polymers produced from different protein concentrations and heating times were comparable to various flow behaviors of hydrocolloids. Polymer formation was found to be a two-phase process. The initial protein concentration was a significant factor that determines the size and/or shape of the primary polymer in the first phase as shown by intrinsic viscosity. Heating time was a factor in determining the aggregation in the second phase as shown by apparent viscosity. Intrinsic viscosity of whey protein polymers was as high as 141.7 +/- 7.30 mL/g, compared to 5.04 +/- 0.20 mL/g for native whey proteins. The intrinsic viscosity and gel electrophoresis data suggested that disulfide bonds played an important role in whey polymer formation.

Colloids↗

PubMedDate not supplied

Preparation and evaluation of microspheres prepared from whey protein isolate.

Whey protein (WPI) microspheres were successfully produced containing hydrochlorothiazide, eosin, patent blue violet and sodium salicylate using a w/o emulsification method with glutaraldehyde cross linking. The release of these compounds from WPI microspheres occurred rapidly, with at least 70% of the incorporated material released for all systems within the first 20 min. Release of microsphere payload was essentially complete within 1 h. The degree of glutaraldehyde cross-linking was found to have no effect on the release profile for durations of cross-linking up to 24 h. Of a range of release equations examined, the experimental release data was best described by a biexponential equation and this agrees with the work of Tomlinson et al. (1984) for the release of drugs from albumin microspheres. Swelling of the microsphere systems was examined as this may contribute to the rapid release of drug from these systems.

Chemical Phenomena↗

PubMed2000

Effects of sugars on whey protein isolate gelation.

Whey protein isolate (WPI) gels were prepared from solutions containing ribose or lactose at pH values ranging from 6 to 9. The gels with added lactose had no color development, whereas the gels with added ribose were orange/brown. Lactose stabilized the WPI to denaturation, which increased the time and temperature required for gelation, thus decreasing the fracture modulus of the gel compared to the gels with added ribose and the gels with no sugar added. Ribose, however, favored the Maillard reaction and covalent cross-linking of proteins, which increased gel fracture modulus. The decreased pH caused by the Maillard reaction in the gels containing ribose occurred after protein denaturation and gelation, thus having little if any effect on the gelation process.

Calorimetry, Differential Scanning↗

PubMed2000

Formation of disulfide bonds in acid-induced gels of preheated whey protein isolate.

Cold gelation of whey proteins is a two-step process. First, protein aggregates are prepared by a heat treatment of a solution of native proteins in the absence of salt. Second, after cooling of the solution, gelation is induced by lowering the pH at ambient temperature. To demonstrate the additional formation of disulfide bonds during this second step, gelation of whey protein aggregates with and without a thiol-blocking treatment was studied. Modification of reactive thiols on the surface of the aggregates was carried out after the heat-treatment step. To exclude specific effects of the agent itself, different thiol-blocking agents were used. Dynamic light scattering and SDS-agarose gel electrophoresis were used to show that the size of the aggregates was not changed by this modification. The kinetics of gelation as determined by the development of pH and turbidity within the first 8 h of acidification were not affected by blocking thiol groups. During gelation, formation of large, covalently linked, aggregates occurred only in the case of unblocked WPI aggregates, which demonstrates that additional disulfide bonds were formed. Results of permeability and confocal scanning laser microscope measurements did not reveal any differences in the microstructure of networks prepared from treated or untreated whey protein aggregates. However, gel hardness was decreased 10-fold in gels prepared from blocked aggregates. Mixing different amounts of blocked and unblocked aggregates allowed gel hardness to be controlled. It is proposed that the initial microstructure of the gels is primarily determined by the acid-induced noncovalent interactions. The additional covalent disulfide bonds formed during gelation are involved in stabilizing the network and increase gel strength.

Acids↗

PubMed2006

Properties of whey protein isolates extruded under acidic and alkaline conditions.

Whey proteins have wide acceptance and use in many products due to their beneficial nutritional properties. To further increase the amount of whey protein isolates (WPI) that may be added to products such as extruded snacks and meats, texturization of WPI is necessary. Texturization changes the folding of globular proteins to improve interaction with other ingredients and create new functional ingredients. In this study, WPI pastes (60% solids) were extruded in a twin-screw extruder at 100 degrees C with 4 pH-adjusted water streams: acidic (pH 2.0 +/- 0.2) and alkaline (pH 12.4 +/- 0.4) streams from 2 N HCl and 2 N NaOH, respectively, and acidic (pH 2.5 +/- 0.2) and alkaline (pH 11.5 +/- 0.4) electrolyzed water streams; these were compared with WPI extruded with deionized water. The effects of water acidity on WPI solubility at pH 7, color, microstructure, Rapid Visco Analyzer pasting properties, and physical structure were determined. Alkaline conditions increased insolubility caused yellowing and increased pasting properties significantly. Acidic conditions increased solubility and decreased WPI pasting properties. Subtle structural changes occurred under acidic conditions, but were more pronounced under alkaline conditions. Overall, alkaline conditions increased denaturation in the extruded WPI resulting in stringy texturized WPI products, which could be used in meat applications.

Buffers↗

PubMed2005

Improvement of functional properties of whey protein isolate through glycation and phosphorylation by dry heating.

Whey protein isolate (WPI) was glycated with maltopentaose (MP) through the Maillard reaction, and the MP-conjugated WPI (MP-WPI) was then phosphorylated by dry heating in the presence of pyrophosphate. Glycation occurred efficiently, and the sugar content of WPI increased approximately 19.9% through the Maillard reaction. The phosphorylation of MP-WPI was enhanced with an increase in the dry-heating time from 1 to 5 d, and the phosphorus content of WPI increased approximately 1.05% by dry heating at pH 4.0 and 85 degrees C for 5 d in the presence of pyrophosphate. The electrophoretic mobility of WPI increased with an increase in the phosphorylation level. The stability of WPI against heat-induced insolubility at pH 7.0 was improved by conjugation with MP alone, and further improved by phosphorylation. Although the emulsifying activity of WPI was barely affected by glycation and phosphorylation, the emulsifying stability of phosphorylated MP-WPI (5 d), was 2.2 times higher than that of MP-WPI. Gelling properties such as hardness, resiliency, and water-holding capacity of heat-induced WPI gel were markedly improved, and the gel was rendered transparent by phosphorylation. The calcium phosphate-solubilizing ability of WPI was enhanced by phosphorylation. These results suggested that phosphorylation by dry heating in the presence of pyrophosphate after conjugation with MP is a useful method for improving the functional properties of WPI.

Calcium Phosphates↗

PubMed2005

Substitution of casein by beta-casein or of whey protein isolate by alpha-lactalbumin does not affect mineral balance in growing rats.

Bovine milk protein fractions that enable modification of the protein composition and amino acid profile of infant formulas to mimic those of human milk have recently become available. To determine the effects on protein quality and mineral bioavailability of replacing casein by beta-casein and of whey protein isolate by alpha-lactalbumin, 4 groups of growing rats were fed for 3 wk diets containing 10% protein as 1) casein (control); 2) beta-casein; 3) casein:whey (40:60); or 4) beta-casein:alpha-lactalbumin (40:60). Protein quality, determined as protein efficiency ratio (PER), net protein utilization (NPU), biological value (BV) and protein digestibility (PD), as well as body weight gain, were higher (P < 0.05) with consumption of the whey-adapted diets [casein:whey (40:60); beta-casein:alpha-lactalbumin (40:60)] compared with the casein diets (casein; beta-casein); however, there were no differences between the 2 casein diets or between the 2 whey-adapted diets. Apparent absorption of minerals (Ca, P, Fe, Zn) from the whey-adapted diets was higher than that from the casein diets (P < 0.05); but again, no differences were observed when casein or whey protein isolate were replaced by beta-casein or alpha-lactalbumin, respectively. Thus, substitution of casein by beta-casein or of whey protein isolate by alpha-lactalbumin does not affect protein quality or mineral bioavailability as determined in growing rats.

Absorption↗

PubMed2000

Enchancing effect of patented whey protein isolate (Immunocal) on cytotoxicity of an anticancer drug.

To determine the enhancing effect of a whey protein isolate on the cytotoxicity of a potential anticancer drug, baicalein, the human hepatoma cell line Hep G2 was assigned to grow in different media for four days, and cell growth and apoptosis were investigated. The control group was grown in normal medium; the other three groups were grown in whey protein isolate (Immunocal) medium, baicalein medium, and a combination of Immunocal and baicalein. As indicated by 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl tetrazolium bromide assay, survival rate was significantly lower in cells grown in baicalein + Immunocal than in cells grown in baicalein alone. In contrast, there was no significant difference in survival rate of the cells grown in Immunocal. In the investigation of apoptosis, cells grown in baicalein + Immunocal showed a higher phosphatidylserine exposure, lower mitochondrial transmembrane potential, and nearly 13 times more cells undergoing apoptosis than cells grown in baicalein alone. We also demonstrated that Immunocal reduced glutathione (GSH) in Hep G2 cells by 20-40% and regulated the elevation of GSH, which was in response to baicalein. In conclusion, Immunocal seemed to enhance the cytotoxicity of baicalein by inducing more apoptosis; this increase in apoptotic cells may be associated with the depletion of GSH in Hep G2 cells. This is the first study to demonstrate, in vitro, that Immunocal may function as an adjuvant in cancer treatments.

Antineoplastic Agents↗

PubMedDate not supplied

Kinetics of cold-set diffusion-limited aggregations of denatured whey protein isolate colloids.

The CaCl2-induced cold-set aggregation kinetics of the denatured whey protein isolate (WPI) colloids has been investigated under dilute diffusion-limited cluster aggregation (DLCA) conditions, using small-angle light scattering. In particular, the structure factor, the scattered intensity at zero angle and the average radius of gyration have been measured for the aggregating system as a function of time. It is found that the fractal dimension of the clusters is df= 1.85, in the range typical of clusters aggregated under DLCA conditions. The aggregation kinetics in this transition region can be described by a power law relation in the initial stage of the aggregation, but the exponent of the power law is equal to 0.7, i.e., significantly larger than 1/df= 0.54, which is the typical value of the DLCA kinetics. Since it is found that the average gyration radius of the clusters has reached a value of 80 microm, leading to a cumulative volume fraction of clusters equal to 0.25, it is legitimate to expect that the process is in the region of transition from aggregation to gelation. This confirmed by the fact that, at the later stage of the aggregation, the growth of the average cluster size further accelerates with time and eventually becomes explosive, leading to gelation. The observed aggregation kinetics has been compared with that reported in the literature from DLCA Monte Carlo simulations, and a good agreement has been found with the data corresponding to the transition region from aggregation to gelation. Numerical simulations using the Smoluchowski kinetic model have also been carried out in order to support the experimental findings.

Biocompatible Materials↗

PubMed2005

Plasma lipid concentrations in preruminant calves fed whole milk with whey protein isolate.

The objective was to investigate the acute effects of retinol acetate added to whey protein isolate (WPI) on postprandial changes in plasma retinol (experiment 1) and the acute effects of milk fat added to WPI on triglyceride (TG), chylomicrons and very low density lipoprotein (VLDL), and fatty acid concentrations (experiment 2) in suckling calves at 1 and 6 wk of age. In experiment 1, 16 Holstein male calves were alloted to 2 equal groups. On the days of measurement, the calves were fed at 0900 h whole milk [4% of body weight (BW)] mixed with vitamin A acetate (500,000 IU) with or without WPI (0.04% of BW). At 1 wk of age, significantly higher postfeeding concentrations of plasma retinol were observed in the calves fed milk with WPI. At 6 wk of age, no differences in the plasma retinol concentrations were observed between 2 groups. On the days of measurement in experiment 2, 16 male calves were fed at 0900 h whole milk (4% of BW) with added milk fat prepared by centrifugation from whole milk (2% of BW) with or without WPI (0.04% of BW). The milk supplemented with fat was prepared on the day before the measurement. At 1 wk of age, significant higher postfeeding concentrations of plasma TG concentrations were obtained in the calves fed WPI than in the control calves, immediately after the meal or from 7 h later onward. Plasma chylomicrons and VLDL concentrations at 1 wk of age were significantly higher in the WPI-fed group than in the control group at 8 h postfeeding. In the calves with the WPI diet, plasma concentrations of myristic, palmitic, stearic, oleic, and linoleic acids at 1 wk of age were significantly higher than those in the control calves at 8 h after feeding. However, chylomicrons and VLDL, and fatty acid concentrations did not differ between the 2 groups after feeding at 6 wk of age. Results indicate that WPI increases plasma lipid concentration of preruminant calves only at 1 wk of age. These data are interpreted to indicate that WPI enhances mainly lipid uptake in the intestines of neonatal calves.

Animal Nutritional Physiological Phenomena↗

PubMed1999

Dynamic interfacial rheology as a tool for the characterization of whey protein isolates gelation at the oil-water interface.

Heat-induced interfacial aggregation of a whey protein isolate (WPI), previously adsorbed at the oil-water interface, was studied by interfacial dynamic characteristics coupled with microscopic observation and image analysis of the drop after heat treatment. The experiments were carried out at temperatures ranging from 20 to 80 degrees C with different thermal regimes. During the heating period, competition exists between the effect of temperature on the film fluidity and the increase in mechanical properties associated with the interfacial gelation process. During the isothermal treatment, the surface dilational modulus, E, increases, and the phase angle, delta, decreases with time to a plateau value. The frequency dependence of E and delta is characteristic of viscoelastic films with increasing delta and decreasing E at lower frequencies. The effects of heat treatment depend on the conditions at which the gelation process takes place. Microscopic observation of gelled films gives complementary information on the effect of heat treatment on WPI adsorbed films.

Gels↗

PubMed2004

Antioxidant activity of a proanthocyanidin-rich extract from grape seed in whey protein isolate stabilized algae oil-in-water emulsions.

Algae oil-in-water emulsions stabilized with 0.2% whey protein isolate (WPI) at pH 3.0 and 7.0 were chosen to evaluate antioxidant activity of a proanthocyanidin-rich extract from grape seed. In this emulsion system, (+)-catechin and ascorbic acid (620 microM) were found to be prooxidative at pH 3.0 and ineffective at pH 7.0. Grape seed extract was not able to effectively inhibit both lipid hydroperoxides and propanal formation when added to the emulsion at 124 microM. However, increasing the concentration of the grape seed extract to 620 microM resulted in inhibition of both lipid hydroperoxide and propanal formation at pH 3.0 and 7.0. None of the antioxidants tested had any effect on the physical stability of the WPI-stabilized emulsion. The superior antioxidant activity of the grape seed extract is likely due to the presence of oligomeric procyanidins which are better antioxidants compared to their monomeric counterparts.

Aldehydes↗

PubMed2004

Electrostatic effects on the yield stress of whey protein isolate foams.

The mechanisms responsible for foam structure are of practical interest within the food industry. The yield stress (tau) of whey protein isolate (WPI) foams as affected by electrostatic forces was investigated by whipping 10% (w/v) protein solutions prepared over a range of pH levels and salt concentrations. Measurements of foam overrun and model WPI interfaces, i.e. adsorption kinetics as determined via dynamic surface tension and dilatational rheological characterization, aided data interpretation. Interfacial measurements were also made with the primary whey proteins, beta-lactoglobulin (beta-lg) and alpha-lactalbumin (alpha-la). Yield stress of WPI foams was dependent on pH, salt type and salt concentration. In the absence of salt, tau was highest at pH 5.0 and lowest at pH 3.0. The addition of NaCl and CaCl2 up to 400 mM significantly increased tau at pH 7.0 but not at pH 3.0. Furthermore, at pH 7.0, equivalent molar concentrations of CaCl2 as compared to NaCl increased tau to greater extents. Salts had minimal effects on tau at pH 5.0. Comparisons with interfacial rheological data suggested the protein's capacity to contribute towards tau was related to the protein's potential at forming strong, elastic interfaces throughout the structure. The dynamic surface tension data for beta-lg and alpha-la were similar to WPI, while the interfacial rheological data displayed several noticeable differences.

Adsorption↗

PubMed2000

Effect of soy and milk whey protein isolates and their hydrolysates on weight reduction in genetically obese mice.

The effect on genetically obese mice of a milk whey protein isolate (WPI) and soy protein isolate (SPI) and their hydrolysates (WPI-H, SPI-H) on the rate of body fat disappearance was investigated. Male yellow KK mice were made obese by feeding with a high-fat diet containing 30% fat from 6 to 10 weeks of age. They were then fed with an energy-restricted low fat (5.0%) and high protein (35% WPI, WPI-H, SPI or SPI-H) diet for 2 weeks at the 60% level of energy intake by mice on laboratory feed. During the weight reduction period, the body weight of the WPI, WPI-H, SPI and SPI-H groups changed by -9.1, -9.1, -10.0 and -11.1 g/14 days, respectively, the reduction being significantly lower in the SPI-H group than in the WPI and WPI-H groups. The plasma total cholesterol level was significantly lower with the SPI diet, and the plasma glucose level was lower with the SPI and SPI-H diets than with the WPI and WPI-H diets. Although the body protein content was comparable in all the groups, the body fat content was significantly lower with the SPI diet than with the WPI diet, and was also significantly lower with the SPI-H diet than with the WPI and WPI-H diets. The weight of the perirenal fat pads was significantly lower with the SPI-H diet than with the WPI and WPI-H diets. These results indicate that SPI and SPI-H are suitable protein sources in an energy-restricted diet for treating obesity.

Adipose Tissue, Brown↗

PubMed2005

Interactions of whey proteins during heat treatment of oil-in-water emulsions formed with whey protein isolate and hydroxylated lecithin.

The interactions of proteins during the heat treatment of whey-protein-isolate (WPI)-based oil-in-water emulsions with and without added hydroxylated lecithin were studied by examining the changes in droplet size distribution and the quantity and type of adsorbed and unadsorbed proteins. Heat treatment at 90 degrees C of WPI emulsions resulted in an increase in total adsorbed protein; unadsorbed beta-lactoglobulin (beta-lg) was the main protein interacting with the adsorbed proteins during the first 10 min of heating, but after this time, unadsorbed alpha-lactalbumin (alpha-la) also associated with the adsorbed protein. In emulsions containing hydroxylated lecithin, the increase in total adsorbed protein during heat treatment was much lower and the unadsorbed beta-lg did not appear to interact with the adsorbed proteins during heating. However, the behavior of alpha-la during heat treatment of these emulsions was similar to that observed in the emulsions containing no hydroxylated lecithin. In the presence of NaCl, the particle size of the emulsion droplets and the quantities of adsorbed protein increased markedly during heating. Emulsions containing hydroxylated lecithin were less sensitive to the addition of NaCl. These results suggest that the binding of hydroxylated lecithin to unfolded monomers or intermediate products of beta-lg reduces the extent of heat-induced aggregation of beta-lg and consequently decreases the interactions between unadsorbed beta-lg and adsorbed protein. This was confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of heated whey protein and hydroxylated lecithin solutions.

Adsorption↗

PubMed1999

Adsorption of whey protein isolate at the oil-water interface as a function of processing conditions: a rheokinetic study.

In this paper we present surface dynamic properties (interfacial tension and surface dilational properties) of a whey protein isolate with a high content of beta-lactoglobulin (WPI) adsorbed on the oil-water interface as a function of adsorption time. The experiments were performed at constant temperature (20 degrees C), pH (5), and ionic strength (0.05 M). The surface rheological parameters and the interfacial tension were measured as a function of WPI concentration (ranging from 1 x 10(-)(1) to 1 x 10(-)(5)% w/w) and different processing factors (effect of convection and heat treatment). We found that the interfacial pressure, pi, and surface dilational modulus, E, increase and the phase angle, phi, decreases with time, theta, which should be associated with WPI adsorption. These phenomena have been related to diffusion of the protein toward the interface (at short adsorption time) and to the protein unfolding and/or protein-protein interactions (at long-term adsorption) as a function of protein concentration in solution and processing conditions.

Adsorption↗

PubMed2003

Effect of whey protein isolate on intracellular glutathione and oxidant-induced cell death in human prostate epithelial cells.

Cysteine is the rate-limiting amino acid for synthesis of the ubiquitous antioxidant glutathione (GSH). Bovine whey proteins are rich in cystine, the disulfide form of the amino acid cysteine. The objective of this study was to determine whether enzymatically hydrolyzed whey protein isolate (WPI) could increase intracellular GSH concentrations and protect against oxidant-induced cell death in a human prostate epithelial cell line (designated RWPE-1). Treatment of RWPE-1 cells with hydrolyzed WPI (500 microg/ml) significantly increased intracellular GSH by 64%, compared with control cells receiving no hydrolyzed WPI (P<0.05). A similar increase in GSH was observed with N-acetylcysteine (500 microM), a cysteine-donating compound known to elevate intracellular GSH. In contrast, treatment with hydrolyzed sodium caseinate (500 microg/ml), a cystine-poor protein source, did not significantly elevate intracellular GSH. Hydrolyzed WPI (500 microg/ml) significantly protected RWPE-1 cells from oxidant-induced cell death, compared with controls receiving no WPI (P<0.05). The results of this study indicate that WPI can increase GSH synthesis and protect against oxidant-induced cell death in human prostate cells.

Antioxidants↗

PubMed2006

Comparisons of the foaming and interfacial properties of whey protein isolate and egg white proteins.

Whipped foams (10%, w/v protein, pH 7.0) were prepared from commercially available samples of whey protein isolate (WPI) and egg white protein (EWP), and subsequently compared based on yield stress (tau(0)), overrun and drainage stability. Adsorption rates and interfacial rheological measurements at a model air/water interface were quantified via pendant drop tensiometry to better understand foaming differences among the ingredients. The highest tau(0) and resistance to drainage were observed for standard EWP, followed by EWP with added 0.1% (w/w) sodium lauryl sulfate, and then WPI. Addition of 25% (w/w) sucrose increased tau(0) and drainage resistance of the EWP-based ingredients, whereas it decreased tau(0) of WPI foams and minimally affected their drainage rates. These differing sugar effects were reflected in the interfacial rheological measurements, as sucrose addition increased the dilatational elasticity for both EWP-based ingredients, while decreasing this parameter for WPI. Previously observed relationships between tau(0) and interfacial rheology did not hold across the protein types; however, these measurements did effectively differentiate foaming behaviors within EWP-based ingredients and within WPI. Interfacial data was also collected for purified beta-lactoglobulin (beta-lg) and ovalbumin, the primary proteins of WPI and EWP, respectively. The addition of 25% (w/w) sucrose increased the dilatational elasticity for adsorbed layers of beta-lg, while minimally affecting the interfacial rheology of adsorbed ovalbumin, in contrast to the response of WPI and EWP ingredients. These experiments underscore the importance of utilizing the same materials for interfacial measurements as used for foaming experiments, if one is to properly infer interfacial information/mechanisms and relate this information to bulk foaming measurements. The effects of protein concentration and measurement time on interfacial rheology were also considered as they relate to bulk foam properties. This data should be of practical assistance to those designing aerated food products, as it has not been previously reported that sucrose addition improves the foaming characteristics of EWP-based ingredients while negatively affecting the foaming behavior of WPI, as these types of protein isolates are common to the food industry.

Animals↗