Plasmin levels in fresh milk whey and commercial whey protein products

Growth of psychrotrophic bacteria in nonfat dry milk at refrigeration temperatures was shown previously in our laboratory to cause a shift in plasmin (a native milk protease) from the casein to the whey fraction. The whey fraction from cheesemaking is commonly used to make whey protein concentrates and isolates, which then are used as functional ingredients in various food systems. Plasmin activity in whey protein products may cause breakdown of food proteins to have desirable or undesirable effects on food quality. This raised questions about the level of plasmin in commercial whey protein products and factors that affect this plasmin level. Therefore, the objectives of this study were to determine: 1) plasmin concentrations in sweet and acid whey protein products as influenced by Pseudomonas growth during storage of fresh milk, and 2) plasmin concentrations in commercial whey protein products. Whey type (sweet or acid) had a significantly (P < 0.05) greater effect on whey-associated plasmin activity than did Pseudomonas fluorescens M 3/6 growth. Acid whey protein products had significantly (P < 0.05) higher plasmin concentrations than sweet whey. Plasmin activities associated with acid and sweet whey protein products were both significantly (P < 0.0001) affected by the growth of Pseudomonas fluorescens M 3/6. The interaction effect between bacterial growth and whey type on plasmin activity was not significant (P = 0.2457). Plasmin activity in the reconstituted commercial whey protein concentrates (i.e., sweet and acid) varied considerably (16.3 to 330 micrograms/g of protein), but was significantly lower (2.1 to 4.4 micrograms/g of protein, P < 0.05) in whey isolates. These quantitative data were supported by plasmin activity visualized by casein SDS-PAGE.     

Crosslinking of whey protein by transglutaminase

Guinea pig liver transglutaminase (EC 2.3.2.13) was used to enzymically crosslink the whey protein alpha-lactalbumin, beta-lactoglobulin, blends of these protein fractions, whey proteins in powdered whey, and whey proteins in modified powdered whey. Transglutaminase actively crosslinked whey proteins over a wide pH range (6.5 to 8.0). Crosslinking gradually increased with increased incubation time to 4 h. Crosslinking was negligible with transglutaminase after 4 h of incubation. Reconstituted commercial whey and modified whey powders contained sufficient Ca2+ for crosslinking by .92 units transglutaminase/ml of reconstituted whey powder (2% protein) and modified whey powder solutions (1 to 5% protein). Reconstituted whey and modified whey powder (35% protein) served as protein sources for crosslinking by transglutaminase without further adjustment of pH or Ca2+. Dithiothreitol was required to crosslink the whey protein.     

Functional and technological aspects of whey powder and whey protein products

Commercial whey powder, whey protein concentrates and whey protein isolates (WPIs) were evaluated for certain functional properties and for their application in full‐fat and nonfat yoghurts. The functional properties of whey products varied, and the highest functionality was recorded in samples with high protein levels. Whey powder had the lowest foaming performance and emulsifying capacity, while WPIs possessed the best functional properties of all the other samples. Curd tension (CT), viscosity and syneresis were improved in yoghurts made using fortified cow's milk or reconstituted skim milk with any whey products, while whey powder had no impact on CT.     

Hydrolysed whey protein reduces muscle damage markers in Brazilian elite soccer players compared with whey protein and maltodextrin. A twelve-week in-championship intervention

Health parameters, performance and body composition effects produced by twelve weeks of intervention with hydrolysed whey protein in elite soccer players from a Brazilian team during an actual championship were compared. Twenty-four players were divided into three groups according to supplement: whey protein (WP), hydrolysed whey protein (HWP), or a non-protein placebo (maltodextrin, MALTO). Biochemical, anthropometric and performance tests were applied on week 0 and week 12 of the intervention. Intervention with hydrolysed whey protein resulted in significant decreases in the muscle damage indicators, creatine kinase (−42%) and lactate dehydrogenase (−30%), compared with increases in the MALTO group. Supplementation with whey protein showed no significant changes in these indicators compared with the MALTO group. Muscle mass showed no changes, and physical performance in an aerobic test was decreased in the HWP group compared with the MALTO and WP groups. These data suggest that the consumption of HWP decreases muscle damage.     

Stability of model emulsions prepared using whey and muscle proteins

The amount of water (SW) and oil (SO) separated from model emulsions and emulsion stability (ES) of these emulsions prepared from corn oil and of fluid whey, total muscle protein (TMP), whey + TMP and sarcoplasmic protein (SP) were examined. The SW value of whey + TMP emulsions was lower (26,33%) than that of TMP (31,33%), SP (39,0%) practically the same as that of whey only. However, the SO value of whey emulsions was higher (9,40%) than that of muscle protein emulsions (0,0%). It was found that there was no oil separation in whey + TMP emulsions. Whey proteins had the lowest ES (64,6 ± 0,96) among the proteins studied. Nevertheless, whey + TMP emulsions had the highest ES (73,67 ± 0,58).     

Production of an exopolysaccharide-containing whey protein concentrate by fermentation of whey

Using whey as a fermentation medium presents the opportunity to create value-added products. Conditions were developed to partially hydrolyze whey proteins and then ferment partially hydrolyzed whey with Lactobacillus delbrueckii ssp. bulgaricus RR (RR; an EPS-producing bacterium). In preliminary experiments, pasteurized Cheddar cheese whey was treated with Flavourzyme to partially hydrolyze the protein (2 to 13% hydrolyzed). Fermentation (2 L, 38 degrees C, pH 5.0) with RR resulted in EPS levels ranging from 95 to 110 mg of EPS per liter of hydrolyzed whey. There were no significant differences in the amount of EPS produced during fermentations of whey hydrolyzed to varying degrees. Since a high level of hydrolysis was not necessary for increased EPS production, a low level of hydrolysis (2 to 4%) was selected for future work. In scale up experiments, whey was separated and pasteurized, then treated with Flavourzyme to hydrolyze 2 to 4% of the protein. Following protease inactivation, 60 L of partially hydrolyzed whey was fermented at 38 degrees C and pH 5.0. After fermentation, the broth was pasteurized, and bacterial cells were removed using a Sharples continuous centrifuge. The whey was then ultrafiltered and diafiltered to remove lactose and salts, freeze-dried, and milled to a powder. Unfermented hydrolyzed and unhydrolyzed whey controls were processed in the same manner. The EPS-WPC ingredients contained approximately 72% protein and 6% EPS, but they exhibited low protein solubility (65%, pH 7.0; 58%, pH 3.0).     

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.     

Factors regulating astringency of whey protein beverages

A rapidly growing area of whey protein use is in beverages. There are 2 types of whey protein-containing beverages: those at neutral pH and those at low pH. Astringency is very pronounced at low pH. Astringency is thought to be caused by compounds in foods that bind with and precipitate salivary proteins; however, the mechanism of astringency of whey proteins is not understood. The effect of viscosity and pH on the astringency of a model beverage containing whey protein isolate was investigated. Trained sensory panelists (n = 8) evaluated the viscosity and pH effects on astringency and basic tastes of whey protein beverages containing 6% wt/vol protein. Unlike what has been shown for alum and polyphenols, increasing viscosity (1.6 to 7.7 mPa·s) did not decrease the perception of astringency. In contrast, the pH of the whey protein solution had a major effect on astringency. A pH 6.8 whey protein beverage had a maximum astringency intensity of 1.2 (15-point scale), whereas that of a pH 3.4 beverage was 8.8 (15-point scale). Astringency decreased between pH 3.4 and 2.6, coinciding with an increase in sourness. Decreases in astringency corresponded to decreases in protein aggregation as observed by turbidity. We propose that astringency is related to interactions between positively charged whey proteins and negatively charged saliva proteins. As the pH decreased between 3.4 and 2.6, the negative charge on the saliva proteins decreased, causing the interactions with whey proteins to decrease.     

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.     

乳清蛋白在运动营养中的应用

乳清蛋白作为一类高质量蛋白,为运动员或健身人群快速补充蛋白质的运动产品的首选成分。本文将从乳清蛋白组成成分、乳清蛋白在运动营养方面的功效、乳清蛋白在运动营养方面的产品开发三个方面来全面介绍了乳清蛋白在运动营养中的应用。     

Production of a high gel strength whey protein concentrate from cheese whey

In order to develop a process for the production of a whey protein concentrate (WPC) with high gel strength and water-holding capacity from cheese whey, we analyzed 10 commercially available WPC with different functional properties. Protein composition and modification were analyzed using electrophoresis, HPLC, and mass spectrometry. The analyses of the WPC revealed that the factors closely associated with gel strength and water-holding capacity were solubility and composition of the protein and the ionic environment. To maintain whey protein solubility, it is necessary to minimize heat exposure of the whey during pretreatment and processing. The presence of the caseinomacropeptide (CMP) in the WPC was found to be detrimental to gel strength and water-holding capacity. All of the commercial WPC that produced high-strength gels exhibited ionic compositions that were consistent with acidic processing to remove divalent cations with subsequent neutralization with sodium hydroxide. We have shown that ultrafiltration/diafiltration of cheese whey, adjusted to pH 2.5, through a membrane with a nominal molecular weight cut-off of 30,000 at 15 degrees C substantially reduced the level of CMP, lactose, and minerals in the whey with retention of the whey proteins. The resulting WPC formed from this process was suitable for the inclusion of sodium polyphosphate to produce superior functional properties in terms of gelation and water-holding capacity.     

Isolation and characterisation of κ-casein/whey protein particles from heated milk protein concentrate and role of κ-casein in whey protein aggregation

Milk protein concentrate (79% protein) reconstituted at 13.5% (w/v) protein was heated (90 °C, 25 min, pH 7.2) with or without added calcium chloride. After fractionation of the casein and whey protein aggregates by fast protein liquid chromatography, the heat stability (90 °C, up to 1 h) of the fractions (0.25%, w/v, protein) was assessed. The heat-induced aggregates were composed of whey protein and casein, in whey protein:casein ratios ranging from 1:0.5 to 1:9. The heat stability was positively correlated with the casein concentration in the samples. The samples containing the highest proportion of caseins were the most heat-stable, and close to 100% (w/w) of the aggregates were recovered post-heat treatment in the supernatant of such samples (centrifugation for 30 min at 10,000 × g). κ-Casein appeared to act as a chaperone controlling the aggregation of whey proteins, and this effect was stronger in the presence of α_S- and β-casein.     

Efficiency of removal of whey protein from sweet whey using polymeric microfiltration membranes

Our objective was to measure whey protein removal percentage from separated sweet whey using spiral-wound (SW) polymeric microfiltration (MF) membranes using a 3-stage, 3× process at 50°C and to compare the performance of polymeric membranes with ceramic membranes. Pasteurized, separated Cheddar cheese whey (1,080 kg) was microfiltered using a polymeric 0.3-μm polyvinylidene (PVDF) fluoride SW membrane and a 3×, 3-stage MF process. Cheese making and whey processing were replicated 3 times. There was no detectable level of lactoferrin and no intact α- or β-casein detected in the MF permeate from the 0.3-μm SW PVDF membranes used in this study. We found BSA and IgG in both the retentate and permeate. The β-lactoglobulin (β-LG) and α-lactalbumin (α-LA) partitioned between retentate and permeate, but β-LG passage through the membrane was retarded more than α-LA because the ratio of β-LG to α-LA was higher in the MF retentate than either in the sweet whey feed or the MF permeate. About 69% of the crude protein present in the pasteurized separated sweet whey was removed using a 3×, 3-stage, 0.3-μm SW PVDF MF process at 50°C compared with 0.1-μm ceramic graded permeability MF that removed about 85% of crude protein from sweet whey. The polymeric SW membranes used in this study achieve approximately 20% lower yield of whey protein isolate (WPI) and a 50% higher yield of whey protein phospholipid concentrate (WPPC) under the same MF processing conditions as ceramic MF membranes used in the comparison study. Total gross revenue from the sale of WPI plus WPPC produced with polymeric versus ceramic membranes is influenced by both the absolute market price for each product and the ratio of market price of these 2 products. The combination of the market price of WPPC versus WPI and the influence of difference in yield of WPPC and WPI produced with polymeric versus ceramic membranes yielded a price ratio of WPPC versus WPI of 0.556 as the cross over point that determined which membrane type achieves higher total gross revenue return from production of these 2 products from separated sweet whey. A complete economic engineering study comparison of the WPI and WPPC manufacturing costs for polymeric versus ceramic MF membranes is needed to determine the effect of membrane material selection on long-term processing costs, which will affect net revenue and profit when the same quantity of sweet whey is processed under various market price conditions.     

Rheological properties and structure of inulin–whey protein gels

The rheological properties, structure and synergistic interactions of whey proteins (1–7%) and inulin (20% and 35%) were studied. Gelation of whey proteins was induced with Na⁺. Inulin was dissolved in preheated whey protein solutions (80 °C, 30 min). Inulin gel formation was strongly affected by whey proteins. The presence of whey proteins at a level allowing for protein gel network formation (7%) significantly increased the G′ and G″ values of the gels. Scanning electron micrographs showed a thick structure for the mixed gel. Whey proteins at low concentrations (1–4%) were not able to form a gel; further, these low concentrations partly or wholly impaired formation of a firm inulin gel. Although interactions between inulin and whey proteins may be concluded from hydrophobicity measurements, the use of an electrophoretic technique did not show any inulin–whey protein complexes.     

Microparticulation of mixtures of whey protein and inulin

This study investigated the effect of the presence of inulin, in the range 0 - 3.81 g/100g, on the physical and microstructural properties of microparticulated whey protein concentrates (MWPC) and powders. Substitution of lactose with inulin increased levels of whey protein denaturation during microparticulation. The increased denaturation levels were correlated with reductions in lactose and calcium content of the microparticulated solutions, which increased aggregate size and solution viscosity post-processing. In conclusion, it appears possible to successfully manufacture a low-calorie microparticulated whey protein based fat replacer using the dietary fibre inulin as the carbohydrate source.     

乳清蛋白粉营养成分分析研究

目的分析不同批次乳清蛋白粉蛋白、脂肪、乳糖、维生素、矿物质及其他功能性营养素的含量及波动情况。方法依照国标方法对乳清蛋白粉营养成分进行检测,并对检测数据进行汇总,分析不同批次间乳清蛋白粉营养素指标的波动范围及相对标准偏差。结果不同批次间乳清蛋白粉营养素波动不大,部分维生素(维生素B12、叶酸、泛酸、维生素C)、矿物质(锌、镁)、功能性营养成分(α-亚麻酸、胆碱、左旋肉碱)相对标准偏差在15%以上,波动较大。结论乳清蛋白粉营养成分含量整体比较稳定。     

乳清蛋白在运动营养中作用

该文通过对乳清蛋白成分介绍,阐明乳清蛋白对于运动营养益处,主要表现为提高免疫力、抗氧化、防止损伤与疲劳等方面,并指出运动饮料将成为乳清综合利用一个重要方向。     

Solubility and heat stability of whey protein concentrates.

Rennet whey protein concentrates have excellent nutritional properties, but their use in fluid food systems is impaired by the poor heat stability of the protein. Heating whey protein concentrated solutions at neutral pH caused up to 70% losses in solubility. In the absence of added calcium, protein coagulation occurred. near the iso-electric zone whereas in the presence of .03 M calcium chloride, similar protein coagulation occurred in the whole pH range (pH 2 to pH 12). Tryptic hydrolysis of the protein increased the heat stability of whey protein concentrates considerably.     

Inhibition of Streptococcus mutans binding to hydroxylapatite using partially digested whey protein concentrate and individual whey proteins

The effect of a bovine whey protein concentrate partially digested with lipase to release free fatty acids (WPD) on growth and viability of Streptococcus mutans, and its adherence to hydroxylapatite (HA) in phosphate-buffered saline were examined. The effects of other whey mixtures and individual whey proteins, β-lactoglobulin (BLG), lactoferrin (LF), caseinoglycomacropeptide (CGMP) and α-lactalbumin were also investigated. Bacterial viability was assessed by incubation with whey protein and measuring colony-forming units. S. mutans binding was quantified using Syto-13 nucleic-acid binding dye and Alamar Blue, which measures cellular metabolic activity. WPD was bactericidal, and inhibited S. mutans growth and adhesion to HA. Other wheys inhibited S. mutans adhesion, particularly acid whey, as well as the parent compound for WPD, Carbelac 80, and a whey protein isolate. BLG, CGMP and LF inhibited S. mutans adhesion. A mixture containing 56% BLG and 20% CGMP was as effective an inhibitor of bacterial adhesion as WPD.