Standardized Procedure for Measuring Foaming Properties of Three Proteins, A Collaborative Study

A collaborative study involving nine laboratories was conducted over four years to evaluate a rapid, simple and reliable whipping method for measuring overrun and foam stability. Effectiveness of the method was assessed by measuring the characteristics of foams formed by three protein solutions (5%): sodium caseinate, milk protein isolate, and egg white protein; identifying and systematically eliminating sources of variability. Major sources of variability were protein dispersing technique, the mixer, and the care exercised by the operator during sampling and weighing. The method detected differences in foam stability between egg white, casein and milk protein isolate (pooled SD = 4.5) using different mixers.     

Effects of sucrose on egg white protein and whey protein isolate foams: Factors determining properties of wet and dry foams (cakes)

The effects of sucrose on the physical properties of foams (foam overrun and drainage ½ life), air/water interfaces (interfacial dilational elastic modulus and interfacial pressure) and angel food cakes (cake volume and cake structure) of egg white protein (EWP) and whey protein isolate (WPI) was investigated for solutions containing 10% (w/v) protein. Increasing sucrose concentration (0–63.6 g/100 mL) gradually increased solution viscosity and decreased foam overrun. Two negative linear relationships were established between foam overrun and solution viscosity on a log–log scale for EWP and WPI respectively; while the foam overrun of EWP decreased in a faster rate than WPI with increasing solution viscosity (altered by sucrose). Addition of sucrose enhanced the interfacial dilational elastic modulus (E′) of EWP but reduced E′ of WPI, possibly due to different interfacial pressures. The foam drainage ½ life was proportionally correlated to the bulk phase viscosity and the interfacial elasticity regardless of protein type, suggesting that the foam destabilization changes can be slowed by a viscous continuous phase and elastic interfaces. Incorporation of sucrose altered the volume of angel food cakes prepared from WPI foams but showed no improvement on the coarse structure. In conclusion, sucrose can modify bulk phase viscosity and interfacial rheology and therefore improve the stability of wet foams. However, the poor stability of whey proteins in the conversion from a wet to a dry foam (angel food cake) cannot be changed with addition of sucrose.     

Whipping Studies with Partially Deloctosed Cheese Whey

Whipping properties of various whey preparations were studied by measuring overrun and stability of foams produced in a Hobart mixer. Presence of heat-labile whey proteins resulted in poor whippability, poor foam stability, and low overruns. Removal of the heat-acid coagulated proteins greatly improved wh’ppability, and foams resembled whipped egg whites with overruns of more than 2,500%. Increasing total solids by evaporation of the acid supernatant or by addition of sucrose or soluble starch decreased the overrun but increased foam stability. Air uptake and overrun were negatively affected by calcium hydroxide. Foams from dialyzed supernatants with addition of sucrose were successfully baked into meringues.     

Effects of Lysozyme, Clupeine, and Sucrose on the Foaming Properties of Whey Protein Isolate and β-Lactoglobulin

Lysozyme and clupeine interacted with β-lactoglobulin to form aggregates. Sucrose reduced the aggregation. The addition of lysozyme (0.5%) to β-lactoglobulin (2.5%) reduced the time required to reach an overrun maximum and increased foam stability and heat stability by 124% and 377%, respectively. Lysozyme (0.5%) also improved overrun (98%), foam stability (114%) and heat stability of the foams (12%) made with whey protein isolate (WPI, 5%). Lysozyme and sucrose further improved the foaming properties of β-lactoglobulin and WPI. The addition of clupeine and sucrose gave similar results. The foaming properties of β-lactoglobulin and WPI with the inclusion of sucrose and lysozyme were superior to those of egg white.     

Instrumental Method for Characterizing Protein Foams

A whipping machine for cream analysis (Cream Tester CTII) was used to foam egg white, milk proteins and soy protein isolate. Foam formation and final rigidity were characterized by the current input to the beating motor. In addition, specific volume, rigidity (compressive strength by Instron) and stability (drainage) of the foams were determined by methods that minimized foam damage during handling. Current input during whipping distinguished fresh vs pasteurized egg white and positively correlated with compressive strength of final egg white foams. Such correlation was not found for milk protein and soy protein isolate foams of lower strength and stability.     

Improvement of Foaming Property of Egg White Protein by Phosphorylation through Dry-Heating in the Presence of Pyrophosphate

ABSTRACT:  Egg white protein (EWP) was phosphorylated by dry-heating in the presence of pyrophosphate at pH 4 and 85 °C for 1 d, and the foaming properties of phosphorylated EWP (PP-EWP) were investigated. The phosphorus content of EWP increased to 0.71% as a result of phosphorylation. To estimate the foaming properties of EWP, the foams were prepared by 2 methods: bubbling of the 0.1% (w/v) protein solution and whipping of the 10% (w/w) protein solution with an electric mixer. The foaming power, which was defined as an initial conductivity of foam from 0.1% (w/v) protein solution, was a little higher in PP-EWP than in native EWP (N-EWP), and the foaming stability of PP-EWP was much higher than that of dry-heated EWP (DH-EWP) and N-EWP. The microscopic observation of foams from the 10% (w/w) solution showed that the foams of PP-EWP were finer and more uniform than those of N- and DH-EWP. Although there were no significant differences in the specific gravity and overrun of the foams between PP- and DH-EWP ( P  < 0.05), the specific gravity and overrun of the foams from PP-EWP were smaller and higher, respectively, than that of the foams from N-EWP. The drainage volume was smaller in the foams from PP-EWP than in those from N- and DH-EWP. These results demonstrated that phosphorylation of EWP by dry-heating in the presence of pyrophosphate improved the foaming properties, and that it was more effective for the foam stability than for the foam formation.     

Measurement of the Yield Stress of Protein Foams by Vane Rheometry

The yield stresses of protein foams made from varying protein types (spray dried egg white and whey protein isolate), protein concentrations, whip times, and mixer models were evaluated using vane rheometry. Two methods of analysis (point and slope methods) were investigated. Yield stress values determined by slope and point methods were similar for egg white protein foams but did not agree in the analysis of whey protein foams. Point method values were very reproducible in all foams tested. Egg white protein solutions formed stiffer foams more rapidly and at lower protein concentrations than foams made from whey protein isolate. Vane rheometry was shown to be a reliable method of determining yield stress in protein foams.     

Factors determining the physical properties of protein foams

Protein foams are an integral component of many foods such as meringue, nougat and angel food cake. With all these applications, the protein foam must first obtain the desired level of air phase volume (foamability), and then maintain stability when subjected to a variety of processes including mixing, cutting and heating. Therefore, factors determining foamability and stability to mechanical and thermal processing are important to proper food applications of protein foams. We have investigated the effects of protein type, protein modification and co-solutes on overrun, stability and yield stress. The level of overrun generated by different proteins was: whey protein isolate hydrolysates >whey protein isolate=β-lactoglobulin=egg white>α-lactalbumin. The level of yield stress generated by different proteins was: egg white>whey protein isolate hydrolysates≥β-lactoglobulin>whey protein isolate>α-lactalbumin. Factors that decreased surface charge (pH∼pI or high ionic strength) caused a more rapid adsorption of protein at the air–water interface, generally increased dilatational viscoelasticity and increased foam yield stress. The elastic component of the dilatational modulus of the air–water interface was correlated with foam yield stress. The properties of foams did not predict performance in making angel food cakes. A model for foam performance in angel food cakes is proposed.     

Characterization of Apple Juice Foams for Foam-mat Drying Prepared with Egg White Protein and Methylcellulose

ABSTRACT: Intrinsic stability and rheological properties of apple juice foams for foam mat drying were studied. Foams were prepared from clarified apple juice by adding various concentrations of 2 foaming agents of different nature: a protein (egg white at 0.5%, 1%, 2%, and 3% w/w) and a polysaccharide (methylcellulose at 0.1%, 0.2%, 0.5%, 1%, and 2% w/w), and whipping at different times (3, 5, and 7 min). In general, egg white foams were less stable but showed a higher degree of solidity (stronger structures), higher foaming capacity, and smaller bubble average diameter than methylcellulose foams. Foam stability increased with increasing concentrations of either methylcellulose or egg white. Increasing whipping times increased the stability of egg white foams only. Stability parameters (maximum drainage and drainage half-time) were correlated in terms of rheological parameters of the continuous phase (consistency index and apparent viscosity at 30/s, respectively). The correlations ( R ²= 0.766 and 0.951, respectively) were considered acceptable because they were independent of whipping time and foaming agent nature and concentration. Results on foam rheology obtained by dynamic and vane tests were in agreement, but the latter method was more sensitive. Optimal concentrations to obtain the most solid foams (0.2% methylcellulose and 2% to 3% egg white, respectively) were the same concentrations required for maximum foaming capacity. Based on this observation and previous models, an empirical expression was proposed to predict the degree of solidity (in terms of inverse phase angle and yield stress) only as a function of foam structural properties (air volume fraction and average bubble size). The model proved to be satisfactory to fit experimental results ( R ²= 0.848 and 0.975, respectively), independently of whipping time, foaming agent nature and concentration.     

Comparative effect of thermal treatment on the physicochemical properties of whey and egg white protein foams

The optimization of the functionalities of commercial protein ingredients still constitutes a key objective of the food industry. Our aim was therefore to compare the effect of thermal treatments applied in typical industrial conditions on the foaming properties of whey protein isolate (WPI) and egg white proteins (EWP): EWP was pasteurized in dry state from 1 to 5 days and from 60 °C to 80 °C, while WPI was heat-treated between 80 °C and 100 °C under dynamic conditions using a tubular heat exchanger. Typical protein concentrations of the food industry were also used, 2% (w/v) WPI and 10% (w/v) EWP at pH 7, which provided solutions of similar viscosity. Consequently, WPI exhibited a higher foamability than EWP. For WPI, heat treatment induced a slight decrease of overrun when temperature was above 90 °C, i.e. when aggregation reduced too considerably the amount of monomers that played the key role on foam formation; conversely, it increased foamability for EWP due to the lower aggregation degree resulting from dry heating compared to heat-treated WPI solutions. As expected, thermal treatments improved significantly the stability of WPI and EWP foams, but stability always passed through a maximum as a function of the intensity of heat treatment. In both cases, optimum conditions for foam stability that did not impair foamability corresponded to about 20% soluble protein aggregates. A key discrepancy was finally that the dry heat treatment of EWP provided softer foams, despite more rigid than the WPI-based foams, whereas dynamically heat-treated WPI gave firmer foams than native proteins.     

Foams Prepared from Whey Protein Isolate and Egg White Protein: 1. Physical, Microstructural, and Interfacial Properties

ABSTRACT:  Foams were prepared from whey protein isolate (WPI), egg white protein (EWP), and combinations of the 2 (WPI/EWP), with physical properties of foams (overrun, drainage 1/2 life, and yield stress), air/water interfaces (interfacial tension and interfacial dilatational elasticity), and foam microstructure (bubble size and dynamic change of bubble count per area) investigated. Foams made from EWP had higher yield stress and stability (drainage 1/2 life) than those made from WPI. Foams made from mixtures of EWP and WPI had intermediate values. Foam stability could be explained based on solution viscosity, interfacial characteristics, and initial bubble size. Likewise, foam yield stress was associated with interfacial dilatational elastic moduli, mean bubble diameter, and air phase fraction. Foams made from WPI or WPI/EWP combinations formed master curves for stability and yield stress when normalized according to the above-mentioned properties. However, EWP foams were excluded from the common trends observed for WPI and WPI/EWP combination foams. Changes in interfacial tension showed that even the lowest level of WPI substitution (25% WPI) was enough to cause the temporal pattern of interfacial tension to mimic the pattern of WPI instead of EWP, suggesting that whey proteins dominated the interface. The higher foam yield stress and drainage stability of EWP foams appears to be due to forming smaller, more stable bubbles, that are packed together into structures that are more resistant to deformation than those of WPI foams.     

三步沉淀法纯化鸡卵类黏蛋白

鸡卵类黏蛋白（hen’s egg ovomucoid,HOVM）是鸡蛋清中最重要的过敏原蛋白,探讨三步沉淀（一步三氯乙酸沉淀以及两步硫酸铵盐析沉淀）从鸡蛋清中提取并纯化HOVM的工艺条件,并利用十二烷基硫酸钠-聚丙烯酰胺凝胶电泳以及高效液相色谱（high performance liquid chromatography,HPLC）技术检测纯化效果。结果表明：用等体积去离子水稀释的鸡卵清液加入质量分数10%三氯乙酸去除大部分杂蛋白后,所得上清液加入硫酸铵至终饱和度50%,盐析沉淀进一步去除非HOVM的杂蛋白,上清液中最后再追加硫酸铵至终饱和度80%,离心所得沉淀再经过透析冻干即为高纯度的HOVM;HPLC（检测波长220 nm）检测所获HOVM的纯度为99.202%,此工艺条件下得到HOVM的提取率约为27.05%。     

Effect of ultraviolet processing on selected properties of egg white

The effect of ultraviolet processing (10.6 and 63.7 kJ m(-2)) on selected properties of egg white (absorbance, particle size, protein fractions, free sulfhydryl content, immunoreactivity, viscosity, gelling and foaming properties) was investigated. Ultraviolet exposure induced the development of browning, the formation of large protein aggregates by disulfide exchange, and protein backbone cleavage. However, egg white proteins were differently sensitive to UV radiation. No changes in immunoreactivity, gelling temperature and gel firmness were observed. Independently on the UV dose, light treated egg white produced foams with higher stability. This effect was attributed to protein aggregates jamming in the fluid interstices between bubbles and/or to the higher viscosity of the aqueous phase. The latter was also associated to higher foam volume.     

Interfacial and Foaming Properties of Two Types of Total Proteose-Peptone Fractions

Total proteose-peptone (TPP) fractions were extracted from skimmed milk (UHT) and whey protein concentrate (WPC) on a laboratory scale. Protein solutions (0.1 %, 0.5 %, and 1 % w/w) were characterized as function of pH: 4.0, 4.6–4.7 (native pH), and 7.0. Their foaming capacities and stabilities were studied. Beforehand, the surface properties that govern them were investigated, notably the kinetics of adsorption and mechanical properties of monolayer films at the air–water interface involved in the formation and the stability of foams respectively. The TPP extracted from skimmed milk showed the lowest values as well as a significant reduction in surface tension and presented a good mechanically resistant film. The TPP extracted from WPC presented a better foaming capacity and stability which was unexpected. However, foaming properties and surface properties of TPP fractions depended on the pH. The considerable influence of extraction source and method on proteose-peptone’s properties were highlighted.     

Coagulation of Egg White of Soft-Shell Turtle (Pelodiscus Sinensis) at High Pressure or High Temperature

The coagulations of soft-shell turtle egg white at high pressure or at high temperature were investigated and compared to chicken egg white. Unlike chicken egg white, no coagulation of soft-shell turtle egg white was observed after high-pressure processing (HPP; 200–600 MPa) or heating treatment (75°C). Basic amino acids, histidine, lysine, and arginine were present at higher percentages in soft-shell turtle egg white proteins than in chicken egg white proteins. Sodium dodecyl sulfate/polyacrylamide gel electrophoresis showed that the intensities of soft-shell turtle egg white components were balanced, there were more components with high molecular mass in soft-shell turtle egg white, and that aggregates formed in both soft-shell turtle egg white and chicken egg white. This work revealed some differences in soft-shell turtle egg white compositions. The low protein content in egg white was responsible for the non-coagulation of soft-shell turtle egg white in response to high pressure or temperature.     

Optimization of dry heat treatment of egg white in relation to foam and interfacial properties

The properties of foams processed with reconstituted egg white were investigated as a function of the denaturation undergone by the proteins during the pasteurization stage in dry state. Various time-temperature tables were applied on the original egg white powder, ranging from 1 to 7 days, and from 60 to 80 °C. Differential Scanning Calorimetry was used to determine the denaturation degree of each EWP induced by the dry heat treatment. The rheological properties of the interface, using the drop tensiometer method, were shown to be significantly affected by the denaturation and to be a relevant parameter for foamability, stability and foam texture. The bulk properties of the foams were interrelated with interfacial properties by using principal component analysis (PCA) and cluster analysis (HCA). The resulting classification of the heat treatments reveals that mild treatment offers a good compromise between the heating cost and the functional properties of the foams.     

Effect of protein–polysaccharide mixtures on the continuous manufacturing of foamed food products

The aim of this work is to understand the effects of protein and polysaccharide interactions on the physicochemical properties of highly viscous Newtonian model foods and their impact on continuous foaming operation in laminar flow conditions. Model foods consisted of modified glucose syrups. Foaming was carried out at constant gas-to-liquid flow rate ratio as a function of rotation speed. Overrun, mean bubble diameter d₃₂ and stability over time were used to characterize foams. Results showed that blow-by occurred during foaming of models including either 0.1% guar or xanthan without proteins, while 0.1% pectin allowed a total incorporation of the gas phase with large bubbles. For proteins, models with 2% whey protein isolate (WPI) were able to form foams with the desired overrun and small bubbles, while foaming was less effective with 2% Na-caseinates. With WPI, guar addition did not improve significantly foam properties. Overrun was reduced in WPI–xanthan mixtures, probably because the matrix exhibited viscoelastic trends even though xanthan decreased d₃₂. WPI–pectin mixtures provided abundant and stable foams with the smallest d₃₂ and the best stability because WPI reinforced the time-dependent behaviour of pectin recipes. However, blow-by was observed with 0.1% pectin when WPI was replaced by Na-caseinates, which demonstrates the key role of specific protein–polysaccharide interactions on overrun. Conversely, bubble diameters in foams were governed by process parameters and could be adequately described using a laminar Weber number based on foam viscosity measured during foaming for all model foods that provided stable foams.     

不同打发状态蛋清泡沫及其凝胶特性的比较

蛋清具有良好的起泡性和凝胶性,其在充气食品中具有难以取代的地位。为研究不同状态蛋清泡沫凝胶的理化性质,该文在室温条件下以恒定搅拌速率（980 r/min）制备了不同打发状态（打发时间为0、50、70和90 s）的蛋清泡沫,并测定了蛋清泡沫的理化特性。随后将不同打发时间的蛋清泡沫加热固化,制备了蛋清泡沫凝胶,通过显微观察、色度、质构和流变分析考察了蛋清泡沫凝胶的特性。实验结果表明,在恒定的搅拌速率下蛋清泡沫的气泡状态会随打发时间的变化而变化。适当延长打发时间,有利于形成比重较低的（0.16～0.17）、具有高起泡性和泡沫稳定性的固态泡沫。打发70 s的蛋清泡沫（蛋清泡沫呈小弯钩状,比重为0.165）稳定性最佳,且经加热固化后,该蛋清泡沫凝胶的亮度（L*=90.28）显著升高,硬度（27.69 g）和弹性（0.78 mm）显著降低（P<0.05）,凝胶性质优良。结果揭示了蛋清泡沫的流变学性质能显著影响蛋清泡沫及其凝胶的性能,为蛋清泡沫在充气食品中的应用提供了理论参考。     

Foaming Properties of Lipid-Reduced and Calcium-Reduced Whey Protein Concentrates

The ability of whey protein concentrates (WPC) to form highly expanded and stable foams is critical for food applications such as whipped toppings and meringue-type products. The foaming properties were studied on six experimental and three commercial WPC, manufactured by membrane fractionation processes to contain reduced lipids and calcium. Lipid-reduced WPC had excellent foaming properties. Experimental delipidized WPC MF 0.45 and commercial delipidized WPC E had higher (P < 0.05) foam expansion than egg white protein (EWP). However. WPC B made bv low-pH UF and isoelectric orecinitation did not form a foam. Lipids and ash were the main factors affecting foaming properties.     

Protein–protein interactions: Their importance in the foaming of heterogeneous protein systems

Analysis of egg albumen foams by electrophoresis showed that the basic protein lysozyme (pI 10.7) was strongly retained. Addition of low concentrations (0.01–0.10% w/v) of the basic proteins clupeine (pI 12) and lysozyme to solutions (0.50% w/v) of several acidic proteins (pI 4.7–6.0) greatly improved their foaming properties at pH values between the isoelectric points. Sucrose strongly enhanced the action of the basic proteins, while not significantly affecting the foaming of the acidic proteins alone. Basic proteins did not enhance the foaming of ovalbumin and egg albumen in the absence of sucrose. Clupeine enhanced foaming more effectively than lysozyme under all conditions studied. Lysozyme was least effective near the isoelectric point of the acidic protein, where electrostatic interactions were weakest. Sodium chloride (0.1M ) had a detrimental effect on the action of lysozyme.