Determination of soy protein, whey protein, and casein in unheated meats by high-performance liquid chromatography.
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Animals↗
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Disulfide-mediated polymerization of whey proteins in whey protein isolate-stabilized emulsions.
The effects of protein polymerization in whey protein isolate-stabilized emulsions on emulsion properties were investigated. Polymerization, involving intermolecular disulfide bonds between whey proteins adsorbed at the oil-water interface, increased with increasing storage time following emulsion formation. Ageing resulted in increased aggregation of emulsion droplets, emulsion viscosity and susceptibility to creaming but these effects were lower when thiol-disulfide interchange reactions were inhibited by N-ethylmaleimide (NEM). Following heating to 75 degrees C, disulfide-mediated polymerization of whey proteins increased as did droplet aggregation, emulsion viscosity and creaming. While NEM lowered the extent of disulfide-mediated polymerization it did not affect the measured physical properties of the heated emulsions. Non-covalent interactions appeared to be the principal forces leading to aggregation of emulsion droplets but aggregates once formed were stabilized by disulfide bonds.
Animals↗
Astringency of bovine milk whey protein.
Whey protein solutions at pH 3.5 elicited an astringent taste sensation. The astringency of whey protein isolate (WPI), the process whey protein (PWP) that was prepared by heating WPI at pH 7.0, and the process whey protein prepared at pH 3.5 (aPWP) were adjusted to pH 3.5 and evaluated by 2 sensory analyses (the threshold method and the scalar scoring method) and an instrumental analysis (taste sensor method). The taste-stimulating effects of bovine and porcine gelatin were also evaluated. The threshold value of astringency of WPI, PWP, and aPWP was 1.5, 1.0, and 0.7 mg/mL, respectively, whereas the gelatins did not give definite astringency. It was confirmed by the scalar scoring method that the astringency of these proteins increased with the increase in protein concentration, and these proteins elicited strong astringency at 10 mg/mL under acidic conditions. On the other hand, the astringency was not elicited at pH 3.5 by 2 types of gelatin. A taste sensor gave specific values for whey proteins at pH 3.5, which corresponded well to those obtained by the sensory analysis. Elicitation of astringency induced by whey protein under acidic conditions would be caused by aggregation and precipitation of protein molecules in the mouth.
Animals↗
Model studies on reactions of plant phenols with whey proteins.
Whey proteins were modified by reaction with selected phenolic compounds (ferulic-, chlorogenic-, caffeic- and gallic acid) and related substances (quinic acid and p-quinone) as well as with extracts from coffee, tea, potato and pear at pH 9. The derivatives formed were characterized in terms of their physicochemical and digestion properties. The derivatization was accompanied by a reaction at the lysine and tryptophan side chains, whereby their content was decreased in comparison to that in the control whey proteins. Moreover, the solubility of the derivatives decreased over a broad pH range and the derivatization influenced the hydrophobe-hydrophile character of the whey proteins. The isoelectric points were shifted to lower pH values in the order of reactivity as follows: gallic acid > p-quinone > caffeic acid > chlorogenic acid. The other derivatives showed no or few changes compared to the control whey proteins. The formation of high molecular fractions was documented with SDS-PAGE. Especially the derivatives of chlorogenic-, caffeic-, gallic acid and p-quinone showed an increase in molecular weight of beta-lactoglobulin fraction from 18,300 to 20,000 Da. A dimer formation in molecular range 40,000 was also registered. MALDI-TOF-MS was applied to characterize the binding of the individual phenolic compounds or their oxidation products to the whey protein fractions, alpha-lactalbumin and beta-lactoglobulin. In vitro experiments showed that the digestion of the derivatized whey proteins with the enzymes of the gastrointestinal tract (trypsin, chymotrypsin, pepsin and pancreatin) was adversely effected. Similar results with regard to physicochemical characterization and digestion properties of the whey proteins treated with the applied extracts from plant beverages, fruit and vegetable were also documented. Coffee and tee were comparatively the most reactive extracts.
Electrophoresis, Polyacrylamide Gel↗
Effect of pH during heat processing of partially hydrolyzed whey protein.
Whey protein isolate was modified by proteolysis using a broad-spectrum protease in combination with heat treatment of the hydrolysate. Half of the beta-lactoglobulin content was hydrolyzed when the degree of hydrolysis reached 5.1%. alpha-Lactalbumin and BSA were not attacked by the enzyme. Heating of the hydrolysate resulted in the formation of small and large aggregates, the proportion of which depended on the degree of hydrolysis and the pH during heating. The decrease in total sulfhydryl groups, as the degree of hydrolysis and heating pH increased, was associated with the formation of disulfide bonds. Whey protein hydrolysis at a degree of hydrolysis of 1.7%, followed by heating at pH 8.0, resulted in the highest amount of accessible sulfhydryl groups, reflecting the unfolded structure of the aggregates. Hydrolysate solubility at neutral pH averaged 98% when pH during heating was 4.0 or 8.0. Heating of whey protein at pH 6.0 resulted in a much lower solubility, which was attributed to the high proportion of large aggregates. Solubility of the hydrolysate at pH 4.5 was higher when pH during heating was adjusted to 4.0. Solubility of the hydrolysate heated at pH 6.0 and 8.0 improved with degree of hydrolysis > 1.7%. Results are discussed in relation to interactions of proteins and peptides during heat processing.
Aspergillus oryzae↗
Functionality of extrusion--texturized whey proteins.
Whey, a byproduct of the cheesemaking process, is concentrated by processors to make whey protein concentrates (WPC) and isolates (WPI). Only 50% of whey proteins are used in foods. In order to increase their usage, texturizing WPC, WPI, and whey albumin is proposed to create ingredients with new functionality. Extrusion processing texturizes globular proteins by shearing and stretching them into aligned or entangled fibrous bundles. In this study, WPC, WPI, and whey albumin were extruded in a twin screw extruder at approximately 38% moisture content (15.2 ml/min, feed rate 25 g/min) and, at different extrusion cook temperatures, at the same temperature for the last four zones before the die (35, 50, 75, and 100 degrees C, respectively). Protein solubility, gelation, foaming, and digestibility were determined in extrudates. Degree of extrusion-induced insolubility (denaturation) or texturization, determined by lack of solubility at pH 7 for WPI, increased from 30 to 60, 85, and 95% for the four temperature conditions 35, 50, 75, and 100 degrees C, respectively. Gel strength of extruded isolates increased initially 115% (35 degrees C) and 145% (50 degrees C), but gel strength was lost at 75 and 100 degrees C. Denaturation at these melt temperatures had minimal effect on foaming and digestibility. Varying extrusion cook temperature allowed a new controlled rate of denaturation, indicating that a texturized ingredient with a predetermined functionality based on degree of denaturation can be created.
Animals↗
Pressure-induced unfolding and aggregation of the proteins in whey protein concentrate solutions.
Whey protein concentrate solutions (12% w/v, pH 6.65 +/- 0.05) were pressure treated at 800 MPa for 20-120 min and then examined using size exclusion chromatography (SEC), small deformation rheology, transmission electron microscopy, and various types of one-dimensional (1D) and two-dimensional (2D) polyacrylamide gel electrophoresis (PAGE). The pressure-treated samples showed a time-dependent loss of native whey proteins by SEC and 1D PAGE and a corresponding increase in non-native proteins and protein aggregates of different sizes. These aggregates altered the viscosity and opacity of the samples and were shown to be cross-linked by intermolecular disulfide bonds and by noncovalent interactions using 1D PAGE [alkaline (or native), sodium dodecyl sulfate (SDS), and SDS of reduced samples (SDS(R))] and 2D PAGE (native:SDS and SDS:SDS(R)). The sensitivity of the major whey proteins to pressure was in the order beta-lactoglobulin B (beta-LG B) > beta-LG A > bovine serum albumin (BSA) > alpha-lactalbumin (alpha-LA), and the large internal hydrophobic cavity of beta-LG may have been partially responsible for its sensitivity to high-pressure treatments. It seemed likely that, at 800 MPa, the formation of a beta-LG disulfide-bonded network preceded the formation of disulfide bonds between alpha-LA or BSA and beta-LG to form multiprotein aggregates, possibly because the disulfide bonds of alpha-LA and BSA are less exposed than those of beta-LG either during or after pressure treatment. It may be possible that intermolecular disulfide bond formation occurred at high pressure and that hydrophobic association became important after the high-pressure treatment.
Chromatography, Gel↗
Therapeutic applications of whey protein.
Whey, a protein complex derived from milk, is being touted as a functional food with a number of health benefits. The biological components of whey, including lactoferrin, beta-lactoglobulin, alpha-lactalbumin, glycomacropeptide, and immunoglobulins, demonstrate a range of immune-enhancing properties. In addition, whey has the ability to act as an antioxidant, antihypertensive, antitumor, hypolipidemic, antiviral, antibacterial, and chelating agent. The primary mechanism by which whey is thought to exert its effects is by intracellular conversion of the amino acid cysteine to glutathione, a potent intracellular antioxidant. A number of clinical trials have successfully been performed using whey in the treatment of cancer, HIV, hepatitis B, cardiovascular disease, osteoporosis, and as an antimicrobial agent. Whey protein has also exhibited benefit in the arena of exercise performance and enhancement.
Adult↗
Comparative sequence analysis of the mRNAs coding for mouse and rat whey protein.
Whey acidic protein (WAP) is a major milk protein found in mouse and rat. Cloned WAP cDNAs from both species have been sequenced and the respective protein sequences have been deduced. Mouse and rat WAP (134 and 137 amino acids respectively) are acidic, cysteine rich proteins which contain a N-terminal signal peptide of 19 amino acids. Most of the cysteines are located in two clusters containing six cysteine residues each, arranged in an identical pattern. Comparison of the mouse and rat WAPs show that the signal peptide and the first cysteine domain are conserved to a greater extent than the rest of the protein. This result is reflected in the nucleotide sequence homology, where the regions coding for the signal peptide and cysteine domain I are the only regions where the rate of replacement substitution is lower than the rate of silent substitution. The 3' non-coding regions show a 91% conservation which is half the substitution rate for the coding region. This low rate of sequence divergence in the 3' non-translated region of the mRNA may indicate a functional importance for this region.
Amino Acid Sequence↗
Effects of a whey protein product and spray-dried animal plasma on growth performance of weanling pigs.
Five experiments were conducted to evaluate the effects of a high-protein, whey protein product (WPP; 73% CP, 6.8% lysine, 12.8% fat, and 5% lactose) and spray-dried animal plasma (SDAP) on growth performance of weanling pigs. In all experiments, pigs were fed experimental diets from d 0 to 14 after weaning in a pelleted form and then a common diet in meal form for the remainder of the experiment. Dietary treatments were established by substituting WPP or SDAP for dried skim milk (Exp. 1) or soybean meal (Exp. 2, 3, 4, and 5) in the control diet. In Exp. 1, we maintained a constant level of lactose in all diets by adjusting the amount of added crystalline lactose. The amount of lactose in diets used in Exp. 2 through 5 varied slightly by the addition of WPP. In Exp. 1 and 2, 180 weanling pigs (initially 5.8 kg and 19 +/- 1 d of age or 5.5 kg and 17 +/- 1 d of age, respectively) were used. Treatment diets contained SDAP (2.5 and 5%) or WPP (2.7 and 5.4% in Exp.1, and 2.5 or 5.0% in Exp. 2). In Exp. 1, from d 0 to 7 after weaning, ADG and ADFI increased with increasing SDAP (linear, P < .01). No other treatment effects were observed during the d 0 to 14 period. In Exp. 2, from d 0 to 14 after weaning, ADG and G:F increased (linear, P < .04) with increasing SDAP or WWP. In Exp. 3, 305 weanling pigs (initially 4.1 kg and 12 +/- 1 d of age) were used. The control diet contained 2.5% SDAP. The experimental diets were similar to the control diet but contained an additional 2.5 or 5.0% SDAP or 2.5 or 5.0% WPP. From d 0 to 14 after weaning, ADG, ADFI, and G:F increased (quadratic, P < .05) with increasing SDAP up to 5.0%. Increasing WPP increased ADG (quadratic, P < .07) and ADFI (linear, P < .09). In Exp. 4 and 5, 329 and 756 weanling pigs (initially 4.1 kg and 12 +/- 1 d of age and 5.2 kg and 18 +/- 1 d of age, respectively) were fed diets in which WPP was substituted for 0, 25, 50, 75, and 100% (Exp. 4) or 0, 50, and 100% (Exp. 5) of the SDAP in the control diet. In Exp. 4 and 5, from d 0 to 14 after weaning, pigs fed a 1:1 blend of each protein source had better ADG (quadratic, P < .04) than those only fed SDAP. In conclusion, WPP can be used in combination with or as a total replacement for SDAP in diets for weanling pigs without reducing performance.
Animal Feed↗
Human milk proteins: separation of whey proteins and their analysis by polyacrylamide gel electrophoresis, fast protein liquid chromatography (FPLC) gel filtration, and anion-exchange chromatography.
Human milk proteins are of nutritional and physiological significance to the newborn infant. To further study these proteins, a rapid procedure to separate and analyze human milk whey proteins was developed using fast protein liquid chromatography (FPLC). First, to separate whey proteins from casein, different variables such as low- or high-speed centrifugation at different temperatures with or without adjustment of pH to 4.6 or 4.3 and with or without addition of calcium to whole milk or skim milk were tested. Each variable was evaluated by gel filtration, anion-exchange chromatography, sodium dodecyl sulphate (SDS)-polyacrylamide gradient gel electrophoresis, immunoelectrophoresis, and immunodiffusion. The optimum method for a discrete separation of whey and casein is the adjustment of whole milk to pH 4.3 with addition of 60 mmol calcium/L, followed by ultracentrifugation. Rapid and sensitive separation and analysis of whey proteins was achieved by FPLC gel filtration and anion-exchange chromatography.
Chromatography, Gel↗
Stimulation of net muscle protein synthesis by whey protein ingestion before and after exercise.
Timing of nutrient ingestion has been demonstrated to influence the anabolic response of muscle following exercise. Previously, we demonstrated that net amino acid uptake was greater when free essential amino acids plus carbohydrates were ingested before resistance exercise rather than following exercise. However, it is unclear if ingestion of whole proteins before exercise would stimulate a superior response compared with following exercise. This study was designed to examine the response of muscle protein balance to ingestion of whey proteins both before and following resistance exercise. Healthy volunteers were randomly assigned to one of two groups. A solution of whey proteins was consumed either immediately before exercise (PRE; n = 8) or immediately following exercise (POST; n = 9). Each subject performed 10 sets of 8 repetitions of leg extension exercise. Phenylalanine concentrations were measured in femoral arteriovenous samples to determine balance across the leg. Arterial amino acid concentrations were elevated by approximately 50%, and net amino acid balance switched from negative to positive following ingestion of proteins at either time. Amino acid uptake was not significantly different between PRE and POST when calculated from the beginning of exercise (67 +/- 22 and 27 +/- 10 for PRE and POST, respectively) or from the ingestion of each drink (60 +/- 17 and 63 +/- 15 for PRE and POST, respectively). Thus the response of net muscle protein balance to timing of intact protein ingestion does not respond as does that of the combination of free amino acids and carbohydrate.
Administration, Oral↗
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↗
Hydrogen peroxide alteration of whey proteins in whey and concentrated whey systems.
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Albumins↗
[Changes in biliary secretory immunoglobulins A in mice fed whey proteins].
A whey protein diet has been shown to enhance splenic immune response to sheep red blood cells (SBRC) in mice. This study was designed to investigate the influence of the type of dietary protein on the biliary secretory IgA. A/J mice were fed defined formula diets containing either 20% whey protein, or 20% casein. Another group was fed Purina mouse chow. After 3 weeks of dietary treatment the body weight of each mouse was recorded and the gall-bladder was removed and its whole content analyzed by ELISA to determine S-IgA secretion. Body weight curves were similar in all dietary groups; higher biliary levels of S-IgA appeared in the whey protein fed mice than in the casein (p less than 0.025) or purine (p less than 0.025) fed mice. Dietary protein type may have a direct influence on the immune response in the gastrointestinal tract, without affecting body weight.
Animals↗
Water sorption by proteins: milk and whey proteins.
The content and physical state of water in foods influence their physical, chemical, quality, safety, and functional behavior. Information concerning the sorption behavior of dairy proteins, in the water activity (Aw) range 0 to 0.9, is collated in this paper. The sorption behavior of proteins in general, the kinetics of absorption, factors affecting water binding, the phenomenon of desorption hysteresis, and the chemical and physical nature of water/protein interactions are reviewed in general terms. This is followed by a discussion of thermodynamic aspects of sorption phenomena and the adequacy of the various equations for describing sorption isotherms of proteins. After a discussion of the methods available for measuring sorption by milk proteins, the sorption behavior of various milk protein preparations, i.e., nonfat dry milk, whey proteins, caseins, and milk powders is summarized. Finally, the water activity of cheese and its relationship to solute mobility and solvent water are discussed. Some of the unique features of protein behavior, i.e., conformational changes, swelling, and solubilization are cited as possible sources of disparities between various reports.
Absorption↗
Kinetics of heat-induced whey protein denaturation and aggregation in skim milks with adjusted whey protein concentration.
Microfiltration and ultrafiltration were used to manufacture skim milks with an increased or reduced concentration of whey proteins, while keeping the casein and milk salts concentrations constant. The skim milks were heated on a pilot-scale UHT plant at 80, 90 and 120 degrees C. The heat-induced denaturation and aggregation of beta-lactoglobulin (beta-lg), alpha-lactalbumin (alpha-la) and bovine serum albumin (BSA) were quantified by polyacrylamide gel electrophoresis. Apparent rate constants and reaction orders were calculated for beta-lg, alpha-la and BSA denaturation. Rates of beta-lg, alpha-la and BSA denaturation increased with increasing whey protein concentration. The rate of alpha-la and BSA denaturation was affected to a greater extent than beta-lg by the change in whey protein concentration. After heating at 120 degrees C for 160 s, the concentration of beta-lg and alpha-la associated with the casein micelles increased as the initial concentration of whey proteins increased.
Animals↗
Effects of dietary protein supply on caseins, whey proteins, proteolysis and renneting properties in milk from cows grazing clover or N fertilized grass.
The objective of this work was to examine whether variation in the amino acid supply to cows could be a reason for the reduced casein content and poorer renneting properties of milk that often occur in late summer, or whether these effects are related to proteolysis in the raw milk. In a 2 x 2 x 2 factorial design, we investigated the effects of sward (clover v. rye-grass) and supplementary feed with a high or low level of rumen-soluble N or of rumen undegradable protein on milk protein composition during the grazing season. A total of 32 Danish Holstein cows were included in the experiment. Milk protein and casein contents and the ratios casein N:total N and casein:true protein were at a minimum in late summer, whereas the contents of urea, non-protein N and whey protein were higher during this period. These seasonal effects were unrelated to either the type of supplementary feed or the type of sward; neither were they clearly related to proteolysis, although casein: true protein was related to the proteose peptone content. The results indicated that whey proteins other than alpha-lactalbumin or beta-lactoglobulin accounted for the higher proportion or concentration of whey protein in late summer. Based on a principal component analysis including variables such as citric acid, lactose and non-protein N, we suggest that the cows' energy supply during this period may be a critical factor in determining the milk protein composition, although our results were not conclusive. There was an interaction between the supplement of rumen undegradable protein and type of sward. When clover was grazed, a high supplement increased the concentrations of protein and casein in milk and the kappa-casein: total casein ratio. When rye-grass was grazed, the opposite response was found, and overall milk protein yield was not affected. The very low N content of clover in early summer reduced milk protein and casein protein during this period.
Animal Feed↗