蛋清粉凝胶特性改性研究进展

蛋清粉作为一类干燥的蛋制品,既保有了蛋清蛋白优良的功能特性,同时规避了液蛋制品难贮藏、难运输的固有弊端,因而用途十分广泛。为了进一步满足市场对高凝胶性蛋清粉的需求,国内外研究者对此做了大量的工作。本文从蛋清蛋白的组成着手,阐述了蛋清蛋白凝胶性能的影响机理,着重对蛋清粉凝胶特性的改性研究进展进行了综述,以期为丰富食品蛋白质凝胶化理论研究以及拓展蛋清粉高效应用提供参考。      

Dry-pasteurization of egg albumen powder in a fluidized bed. II. Effect on functional properties: gelation and foaming

Dry‐pasteurization of egg albumen (EA) powder in a fluidized bed was studied in two experiments. Experiment 1 consisted of two different temperatures (90 and 130 °C) and experiment 2 of two air moisture levels (high and low). Powders were processed from 10 min to 3 h. The reference treatment was traditional pasteurization at 90 °C for 21 h. The fluidized bed treatment effects on gel texture, water‐holding capacity (WHC), protein binding, gel colour, foaming capacity, foam stability and surface pressure were evaluated. Gels of EA powders treated at high temperature and high air moisture levels exhibited higher stress, strain and WHC values than gels of untreated EA powder. The gel colour became significantly darker, greener and less yellow by fluidized bed treatment. Foaming and surface activity properties were un‐affected by the treatments, however, foam stability against liquid drainage correlated positively with surface pressure.     

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.     

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.     

Dry-pasteurization of egg albumen powder in a fluidized bed. I. Effect on microbiology, physical and chemical parameters

Present pasteurization methods of dried egg albumen powder require large storage facilities and take a long time. The use of a fluidized bed system for dry pasterurization of egg albumen was studied as an alternative approach. In Experiment 1 two different temperature treatments were investigated (90 °C and 130 °C); whilst in Experiment 2 the effect of high vs. low air moisture was studied at a fixed temperature of 115 °C. Both experiments had process times of between 10 min and 3 h. The Reference method was traditional pasteurization at 90 °C for 21 h. Samples were analysed for microbiological, chemical and physical properties. High temperature or high air moisture treatments ensured greater bacterial elimination, formation of covalently bound protein polymers and increased surface hydrophobicity. The nature of polymer bonds is suggested to be Schiff's bases, which increase correspondingly. The powder colour became darker and more yellow at high temperature for 3 h and particle size increased.     

Rheological properties of foams generated from egg albumin after pH treatment

Rheological properties of foams at pH 4.5 and 8.5 made from egg albumin proteins after pH-induced unfolding and refolding treatments were investigated. The foams behaved as highly elastic materials. Static and dynamic yield stress was investigated using small, steady shear experiments. Yield stress was measured also in oscillation mode and high correlation was found between dynamic yield stress and critical stress amplitude. All pH treatments led to firmer foams than untreated foams at pH 8.5. At pH 8.5 the control foam had a very weak structure (static yield stress at 3.4 Pa and dynamic yield stress at 5.5 Pa for the fresh made foams), while pH-treated foams at pH 8.5 had values (static yield stress up to 39.2 Pa and dynamic yield stress up to 47.1 Pa for the fresh made foams) that were even higher than the values for the control at pH 4.5 (static yield stress at 22.4 Pa and dynamic yield stress at 25.4 Pa for the fresh made foams, which is a good foaming pH for egg albumin). It was shown that an increase in yield stress of foams after drainage is related to foam stability and liquid drainage. This study demonstrated that unfolding egg albumin at low or high pH followed by refolding leads to a substantial increase in foam firmness and gives the foam different properties than foams from untreated egg albumin.     

Effect of moisture content on selected physicochemical properties of two commercial hen egg white powders

After short-term storage at 23 °C, selected physicochemical properties of two hen egg white powders (with and without hydrolysis) were studied. Overall, the effect of moisture content on physicochemical properties of Hydrolysed Egg White powder (HEW) was more severe than those of Dried Egg White powder (DEW). The denaturation temperature (T_d) and its enthalpy change (ΔH_d) of ovalbumin in DEW followed an exponential model, as well as the T_d of HEW. The Gordon-Taylor equation modelled well the glass transition temperatures (T_g) of HEW and DEW. The Guggenheim-Anderson-de Boer (GAB) model fitted well to the type II moisture sorption isotherm. At the critical moisture content (12.0%, dry basis), compared with DEW, the colour of HEW began to darken dramatically and its hardness started to change significantly. These changes were closely related to the inherent characteristics of the two products. The mechanisms relevant to these physicochemical changes were discussed.     

The stability and physical properties of egg white and whey protein foams explained based on microstructure and interfacial properties

The goal of this investigation was to determine if physical models, based on micro-scale (bubbles) and nano-scale (interface) properties, can be used to explain the macroscopic foaming properties of egg white protein (EWP) and whey protein isolate (WPI). Foam properties were altered by adding different amounts of sucrose (4.27–63.6 g/100 mL) and microstructures were observed using confocal laser scanning microscopy and bubbles were quantitatively measured using image analysis. Addition of sucrose decreased the initial bubble size, corresponding to higher foam stability and lower air phase fraction. EWP foams were composed of smaller bubbles and lower air phase fractions than WPI foams. Increased sucrose concentration caused a decreased liquid drainage rate due to a higher continuous phase viscosity and smaller bubble sizes. WPI foams had faster rates for liquid drainage and bubble coarsening than EWP foams. The differences were attributed to faster bubble disproportionation in WPI foams, caused by lower interfacial elasticity and lower liquid phase fractions. The experimentally fitted parameters for foam yield stress did not follow universal trends and were protein type dependent. EWP foams had higher yield stress than WPI foams due to smaller bubble sizes and higher interfacial elasticity. The yield stress of WPI foams increased slightly with addition of sucrose and cannot be accounted for based solely on model parameters. It appears that changes in stability of EWP and WPI foams can be explained based on physical models while unaccounted for protein-specific effects remain regarding foam yield stress.     

Influence of pH on surface properties of aqueous egg albumen solutions in relation to foaming behaviour

The surface properties of aqueous egg albumen protein solutions (0.1 g litre⁻¹) were studied at pH values of 4.8, 7.0, 9.2 and 10.7 and related to foaming behaviour such as bubble size distribution, overrun and drainage. By measurements far from equilibrium of dynamic steady state surface dilation using the overflowing cylinder technique, egg albumen showed ability to slow down surface expansion and to lower the dynamic surface tension. The pH‐effect was small, but at pH 4.8 the film length, at which a motionless surface was created, was longer than at higher pH indicating a somewhat more rigid surface at low pH. Near equilibrium sinusoidal surface area deformation resulted in relatively high moduli of egg albumen, with a significant effect of pH. The surface modulus E showed at pH 4.8 an increase in the course of time, but at higher pH it was constant. Large deformation of egg albumen surface was not destructive, and for all pH values the surface behaved viscoelastic, with highest loss modulus E″ and tan θ values at pH 4.8. Surface deformation frequency sweeps revealed the relaxation processes to be relatively slow at pH 4.8 and faster at pH 7.0–10.7. Foamability measured as overrun of foam as a result of shaking and stirring was highest at pH 4.8 and lowest at pH 10.7. Foam stability against drainage was best at pH 7.0 after 30 min, but at a long‐term scale foam at pH 4.8 was most resistant to drainage. Foam samples were subjected to microscopy and image analysis. The smallest bubbles were found at pH 4.8 (mean diameter 142 µm) and the largest at pH 7.0 (mean diameter 328 µm). In conclusion, the foaming behaviour of an aqueous egg albumen solution at pH 4.8 can be related to dynamic surface properties as follows: the more rigid behaviour of the surface at this pH favours a small bubble size and slow drainage of liquid from the foam. The high overrun at this pH can be explained by a lower dynamic surface tension, but also here film stability during foam making can be promoted by a more rigid liquid surface. © 1999 Society of Chemical Industry     

Effect of oxidation induced by hydroxyl radical‐mediated model on molecular structural and physical character of egg white powder

The objective of this study was to determine structure and functional properties changes of oxidised egg white protein derived from hydrogen peroxide (H₂O₂)/ferric chloride (FeCl₃) /ascorbic acid hydroxyl radical‐generating systems at room temperature, including carbonyls, sulfhydryl and total sulfhydryl groups, dityrosine, free amino, surface hydrophobicity, particle size distribution, intermolecular forces, and foamability and emulsibility. Protein carbonyl and dityrosine content of egg white protein were increased (P < 0.05) with increasing the concentrations of H₂O₂. Oxidation decreased free sulfhydryl, total sulfhydryl groups and surface of hydrophobicity comparing with nonoxidised egg white protein. Oxidation also reduced its free amino content (P < 0.05). The low concentration of H₂O₂ contributing the average particle size of egg white protein was smaller than the control group. However, the high concentrations of H₂O₂ caused that egg white protein aggregated and the average particle size became larger. To sum up, oxidation made EWP denaturation and aggregation.     

Effect of heat treatment on foaming properties of ostrich (Struthio camelus) egg white proteins

The effect of heat-treatment on foaming properties of ostrich albumen was investigated. At pH 7.5, coagulation of ovotransferrin (OT) resulted in minimum foaming capacity (FC) and maximum foam density (FD). While both exposure of sulfhydryl groups of ovalbumin (OV) and OT-OV interactions improved FC at lower pH, neither of them had beneficial effect on FC at pH 9. At pH 9, FC and FD were mildly affected by heat-treatment because of less aggregation of OT, then FC decreased due to covalent aggregates composed of ovomucin and OV, but at higher temperatures, higher level of OV unfolding resulted in enhanced FC.     

The physicochemical parameters during dry heating strongly influence the gelling properties of whey proteins

In this study we determined the composition (proportion of native proteins, soluble and insoluble aggregates) and quantified the gelling properties (gel strength and water holding capacity) of pre-texturized whey proteins by dry heating under controlled physicochemical conditions. For this purpose, a commercial whey protein isolate was dry heated at 80 °C (up to 6 days), 100 °C (up to 24 h) and 120 °C (up to 3 h) under controlled pH (2.5, 4.5 or 6.5) and water activity (0.23, 0.32, or 0.52). Gelling properties were quantified on heat-set gels prepared from reconstituted pre-texturized proteins at 10% and pH 7.0. The formation of dry-heat soluble aggregates enhanced the gelling properties of whey proteins. The maximal gelling properties was achieved earlier by increasing pH and water activity of powders subjected to dry heating. An optimized combination of the dry heating parameters will help to achieve better gelling properties for dry heated whey proteins.     

Food properties of egg white protein modified by rare ketohexoses through Maillard reaction

d ‐psicose (Psi), a rare ketohexose, improves food properties of proteins through the Maillard reaction (MR) much more than d ‐fructose (Fru). This encouraged us to investigate the improvement of food properties of proteins through MR with various rare ketohexoses (d ‐psicose, Psi; d ‐tagatose, Tag; and d ‐sorbose, Sor). The food properties of egg white protein (EWP) after reaction with Psi, Tag, Sor and Fru were studied. Psi‐EWP (43.3 μmol TE g^?1) and Tag‐EWP (43.4 μmol TE g^?1) had the highest antioxidant activity, followed by Sor‐EWP (38.4 μmol TE g^?1) and Fru‐EWP (38.9 μmol TE g^?1). MR enhanced the breaking stress of heat‐induced EWP gels by 224–267%. The breaking stress was higher in Psi‐EWP (81.1 kN m^?2), Tag‐EWP (80.0 kN m^?2) and Sor‐EWP (77.8 kN m^?2) than in Fru‐EWP (71.6 kN m^?2). Furthermore, the foaming capacity was highest in Psi‐EWP and Sor‐EWP. Rare ketohexoses improved food properties of EWP more than Fru. Overall, Psi offered the greatest functional improvement.     

On hen egg fractionation: applications of liquid chromatography to the isolation and the purification of hen egg white and egg yolk proteins

Liquid chromatography has been used as a means of egg protein analysis or as a method for the purification of egg proteins. Several Chromatographic methods, including gel permeation, ion-exchange, reversed-phase, hydrophobic interaction, and immobilized-ligand-affinity chromatography, have been carried out for the separation or the purification of egg yolk or egg white proteins. Ion-exchange chromatography appears to be the most frequently used method for protein isolation and it is the easiest to adapt to a process scale. From an analytical point of view reversed-phase chromatography is, at the moment, the recommended method for egg white analysis. Egg white has been fractionated more often by liquid chromatography than has egg yolk. Several Chromatographic methods have been developed on a laboratory scale, but the application of these techniques on an industrial scale remains limited.     

Rheological properties of angel food cake made with pH unfolded and refolded egg albumen

Angel food cake was made using egg albumen subjected to the pH-induced unfolded and refolded treatment. The effect of treatment on the rheological properties of angel food cake was investigated. Egg albumen solutions were prepared and pH was adjusted to 1.5, 4.5, 8.5 or 12.5 and then held 60 min to unfold the proteins. After holding, the solutions were readjusted to pH 4.5 or 8.5, and held for 45 min to partially refold the proteins. Egg white foam with sucrose was whipped and flour and the rest of sucrose were folded into the foam. The foam batter was heated in a TA Instrument AR 2000 controlled stress rheometer equipped in a parallel geometry. Samples were heated from 21 °C to 150 °C at a rate of 8.5 °C per min and then cooled down to 21 °C to bake the angel food cake. At 21 °C, oscillatory stress sweep was performed. There was no relationship between the G′ value of angel cake batter and its G′ value at 150 °C. Changes in rheological properties of batters and angel food cakes using different combinations of ingredients were studied. The pH unfolding and refolding procedure led to more rigid final products compared to the controls with egg albumen samples not subjected to pH treatment. Adding sucrose to the flour increased the starch gelation temperature up to 82 °C. Higher protein concentrations resulted in better foams in the cake batter, but the batter made with an intermediate protein concentration produced the most rigid angel food cake. Adding egg albumin did not change gelation temperature of the starch. It appears that incorporation of flour with the egg white foam, leads to about a ten times decrease in the strength of the foam, and a decrease in the gelatinization process of starch after adding sugar, are crucial in forming of an angel food cake texture.     

Effect of sugar, citric acid and egg white type on the microstructural and mechanical properties of meringues

Meringues are characterized by a predominant air phase and their overall quality is intimately related with microstructure. The formation of meringues microstructure relies on the capacity of egg white (EW) proteins to form voluminous and stable foams and it is ultimately related with the chemical properties of proteins and with the addition of ingredients such as sugars, salts, acids and surfactants.The study aimed at assessing the influence of sugar/EW ratio, citric acid and EW type on the microstructural and mechanical properties of meringues. Meringues prepared with different sugar/EW, citric acid level and different EW type were subjected to microstructural analysis by X-ray microtomography and to mechanical assessment by compression tests.Results demonstrate the ability of X-ray microtomography to reconstruct the 3D microstructure of meringues allowing the measurement of porosity, size, shape and distribution of pores. Citric acid, sugar concentration and EW type play a fundamental role on meringues microstructural parameters and mechanical properties. Low sugar/EW ratios as well as increasing citric acid levels increase the air phase and result in a softer texture of meringues. Moreover, low sugar/EW ratios and increasing citric acid in the meringue result in a reduction of pore size and also influence the shape of pores. Meringues microstructural and mechanical properties are affected by the EW quality: fresh and pasteurized EWs and EWs stored at refrigerated temperatures scored the highest structural and mechanical performances, while powdered and frozen EWs and albumens from old eggs showed the worst results. Not only the balance among ingredients but also the choice of raw materials can strongly affect the final quality of meringues.     

Impact of food processing on the structural and allergenic properties of egg white

BackgroundEgg is one of the most nutritious foods that is easily available and it has become a favorite source of major nutrients like lipids and proteins around the world. However, eggs can trigger severe allergic reactions, especially in infants and children. The reactions are mostly IgE-mediated with a range of symptoms related to nose and throat and further can lead to life-threatening anaphylaxis. A total of ten allergens have been recognized to date and researchers are actively working on understanding their structure-function relationship which could help reduce the allergy incidences. Major egg allergens are abundant in egg white which include ovalbumin (OA), ovomucoid (OVM), ovotransferrin (OVT) and lysozyme (Lys). In addition to allergens, avidin present in egg white is also extensively studied due to its anti-nutritional properties. Avidin is known to form a complex with biotin which makes it unavailable for absorption.Scope and approachThis review focuses on the effects of thermal and non-thermal processing methods on the structure and functional properties of various egg proteins including a wide range of allergens and anti-nutrients.Key findings and conclusionsNovel processing techniques including various non-thermal techniques show promising results in reducing the allergic reactions of egg. Anti-nutrients like avidin can be partly inactivated under combined high-pressure processing and heat treatment.     

Foaming,gelling and rheological properties of egg albumen as affected by the housing system and the age of laying hens

The aim of this work was to study the foaming, gelling and rheological properties of albumen as simultaneously affected by the housing system (i.e. conventional cage, organic and barn) and the age of layers (27, 30, 35, 43, 53 and 68 weeks). Significant effects of the two considered factors and of their interactions were found for almost all the studied properties. In particular, with the increasing of the hen age, a loss in albumen consistency and a weakening of the albumen gel structure were observed. As regards the housing system, differences observed, even if statistically significant, were little and unlikely to have a real effect on technological performances of the eggs when used as food ingredients. Significant correlations amongst technological properties of albumen and its pH and protein content were also found.     

Solubility and density of egg white proteins: Effect of pH and saline concentration

Influence of different pH values (3.0, 4.6, 6.0, 8.0 and 9.0) and salt concentrations (0.05, 0.1, 0.2, 0.35 and 0.5 mol/l) for three types of salt (NaCl, Na₂SO₄ and (NH₄)₂SO₄) on the solubility of egg white protein and density of egg white, at room temperature (25 °C) was studied. The results showed that the solubility of egg white protein was influenced by pH as well as concentration and type of salt present in the medium. Protein solubility increased with increase in pH, with higher solubility showed at pH 9.0 and lower solubility at pH 4.6. This behavior was verified for all the salts analysed. At acid pH (pH 3.0), it was observed the tendency of solubility elevation on the increase of the saline concentration, due to the salting-in effect. The density increased with increase in the salt concentration.     

Synergy between ovalbumin and lysozyme leads to non-additive interfacial and foaming properties of mixtures

This study was undertaken to characterize the interfacial and foaming properties of different mixtures at the air–water interface under the same concentration range, and to put into light putative particular behaviors of mixtures. Different complementary techniques have been coupled such as null ellipsometry, surface tension and shear elastic constant measurements as well as polarization-modulation infrared reflection–absorption spectroscopy (PM-IRRAS). Moreover, the foaming properties were also investigated by a bubbling method.