Gel Properties of Whey Protein Concentrates as Influenced by Ionized Calcium

Ionic calcium in four whey protein concentrates (WPC) was decreased using sodium tripolyphosphate (NaTPP) or ethylenediamine tetraacetic acid (EDTA) and effects on gel properties were determined. Total calcium ranged from 0.22–0.41 g/100g WPC and ionic calcium 2.98–47.25 mg/100g protein. Hardness was maximized and expressible moisture (EM) minimized in three WPC gels with 10 mM NaTPP. EDTA had a similar effect on one WPC gel. Addition of 10 mM NaTPP decreased ionic calcium to 5.23–10.31 mg/100g protein. NaTPP or CaCl₂ did not improve hardness or EM of one WPC gel which contained the lowest total and ionized calcium. Chelating agents were effective in improving gel properties of WPC containing higher than optimal calcium.     

Gelation of Calcium-Reduced and Lipid-Reduced Whey Protein Concentrates as Affected by Total and Ionic Mineral Concentrations

Rheological and microstructural properties of five dialyzed whey protein concentrate (WPC) gels were investigated. Maximum WPC gel hardness as determined by shear stress (ST) was observed at 2.7–4.5 mM Ca and 0.6–1.1 mM Ca²⁺ concentrations with a Ca ionization of 20–25%. Gel cohesiveness by shear strain (SN) correlated with total lipid and phospholipid (PLP) concentrations and percent of lipid unsaturation. Microstructural characteristics of the gels, as determined by light microscopy (LM), confirmed their water holding capacity (WHC) and rheological properties.     

水分状态对鱼糜凝胶高温处理热稳定性的影响

探讨不同水分含量及状态对鱼糜凝胶高温处理热稳定性的影响。将鱼糜中添加不同保水剂制成凝胶,经冷风干燥一定时间后进行高温处理,测量冷风干燥不同时间后水分含量、水分活度和水分状态的变化,通过5分法评分标准评定高温处理后鱼糜凝胶的凝胶特性。结果表明:随着冷风干燥时间的延长,空白组及添加保水剂组的鱼糜凝胶的水分含量均呈现相同的下降趋势,水分活度也呈现一定的下降趋势,但下降幅度不尽相同,鱼糜凝胶中的不易流动水和自由水的含量均有一定程度的变化,另外,高温处理后鱼糜凝胶的凝胶特性呈现上升的趋势。说明降低水分含量可有效提高高温处理鱼糜凝胶的凝胶特性,同时可通过添加保水剂改变水分活度和水分状态从而进一步提高鱼糜凝胶的高温处理热稳定性。     

Whey protein concentrate gels with honey and wheat flour

Structural and functional properties of whey protein concentrate (WPC) gels with different honey and wheat flour contents, prepared at pHs 3.75, 4.2 and 7.0, were analysed. Gel structure was observed by scanning electron microscopy. The apparent transition temperatures for protein denaturation and starch gelatinization were determined by differential scanning calorimetry. Gels were characterised through solubility assays in different extraction solutions and polyacrylamide gel electrophoresis of the soluble protein components. The firmness, elasticity, relaxation time, adhesivity and cohesiveness of gels were determined, and the water-holding capacity and superficial colour of gels were also studied. Results suggest that wheat flour could interact with whey proteins, and produces a decrease in the protein solubility of WPC gels, and in the temperature of whey protein denaturation. The effect of wheat flour on the functional properties of WPC gels was different at acidic than at neutral pH: the presence of wheat flour produced an increase in the relaxation time and in the cohesiveness of gels prepared at pH 3.75, whereas at neutral pH a decrease in both properties was observed. Honey and flour content increased the water-holding capacity and browning of WPC gels.     

Thermal gelation of commercial whey protein concentrate: influence of pH 4.6 insoluble protein on thermal gelation

Thermal gels were prepared from solutions of seven commercial whey protein concentrates (WPCs) and were found to vary considerably in strength, as determined by a compressive rheological measurement method. Further studies were carried out on one WPC (WPC5) which had far superior gelling properties to the other six WPCs and revealed that this WPC had a substantial level of protein that was insoluble (sedimentable) at pH 4.6 on centrifugation at 10000 g for 30 min but not insoluble under similar conditions at pH 7.0. When this pH 4.6 insoluble material was removed the gelling properties of WPC5 decreased considerably. Alkaline treatment (pH 9.0 for 3 hours) of a WPC5 supernatant devoid of pH 4.6 insoluble material resulted in a substantial improvement in gelling properties and generation of further pH 4.6 insoluble material. Gel electrophoresis studies and differential scanning calorimetry confirmed that the pH 4.6 insoluble material recovered from WPC5 and the alkaline treated WPC5 supernatant contained denatured protein which was associated via covalent and non-covalent interactions. Transmission electron microscopy of thermal gels prepared from WPC5 solutions containing and devoid of pH 4.6 insoluble material indicated that gel micro structure was dependent on the presence or absence of this denatured aggregated protein material in dispersion prior to heat treatment. Overall, the results suggested that the pH 4.6 insoluble, but pH 7.0 soluble, protein present in a WPC5 dispersion influenced gel microstructure on heating in a manner that had a positive influence on gel rheology.     

Whey protein concentrate/λ-carrageenan systems: Effect of processing parameters on the dynamics of gelation and gel properties

The thermal characteristics, dynamics of gelation and gel properties of commercial whey protein concentrate (WPC), WPC/λ-carrageenan (λ-C) mixtures (M) and WPC/λ-C spray-dried mixtures (DM) have been characterized. In a second stage, the effect of the gelling variables (T, pH, total solid content) on gelation and textural properties of DM was evaluated through a Doehlert uniform shell design.The presence of λ-C either in mixtures (M) or in DM promoted the WPC gelation at lower concentration (8%). M showed higher rates of formation and better gel properties (higher hardness, adhesiveness, springiness and cohesiveness) than DM.Nevertheless, when the effects of pH (6.0–7.0), heating temperature (75–90 °C) and total solid content (12–20 wt%) on gelation dynamics and gel properties of DM were studied, gels with a wide range of rheological and textural properties were obtained. While pH did not affect the gelation dynamics, it had some effect on rheological and textural properties. Total solid content and heating temperature were the most important variables for the dynamics of gelation (gelation rate (1/t_gel), gelation temperature (T_gel), rate constant of gel structure development (k_G), elastic modulus after cooling (G′_c) and textural parameters (hardness, springiness and cohesiveness).     

Relationships Between Physicochemical Properties of Nonfish Protein and Textural Properties of Protein-incorporated Surimi Gel

The physicochemical properties of nonfish proteins were correlated with textural properties of nonfish protein gels and nonfish protein-incorporated surimi gels. Both cold and thermal hydration ability (by centrifugation) of nonfish proteins strongly correlated with compressive force (cohesiveness) of nonfish protein-incorporated surimi gel (r = 0.94 for cold; r = 0.95 for thermal). Hydrophobic amino acid groups in nonfish protein inversely correlated with compressive force (r =?0.88) and penetration force (r =?0.78) of nonfish protein-incorporated surimi gel. Thermal behavior of nonfish protein affected the gel characteristics of nonfish protein and surimi with nonfish protein-incorporated.     

The roles of disulphide and non-covalent bonding in the functional properties of heat-induced whey protein gels

Heat-induced gelation (80 degrees C, 30 min or 85 degrees C, 60 min) of whey protein concentrate (WPC) solutions was studied using transmission electron microscopy (TEM), dynamic rheology and polyacrylamide gel electrophoresis (PAGE). The WPC solutions (150 g/kg, pH 6.9) were prepared by dispersing WPC powder in water (control), 10 g/kg sodium dodecyl sulphate (SDS) solution or 10 mM-dithiothreitol (DTT) solution. The WPC gels containing SDS were more translucent than the control gels, which were slightly more translucent than the gels containing DTT. TEM analyses showed that the SDS-gels had finer aggregate structure (approximately equal to 10 nm) than the control gels (approximately equal to 100 nm), whereas the DTT-gels had a more particulate structure (approximately equal to 200 to 300 nm). Dynamic rheology measurements showed that the control WPC gels had storage modulus (G) values (approximately equal to 13,500 Pa) that were approximately equal to 25 times higher than those of the SDS-gels (approximately equal to 550 Pa) and less than half those of the DTT-gels after cooling. Compression tests showed that the DTT-gels were more rigid and more brittle than the control gels, whereas the SDS-gels were softer and more rubbery than either the control gels or the DTT-gels. PAGE analyses of WPC gel samples revealed that the control WPC solutions heated at 85 degrees C for 10 min contained both disulphide bonds and non-covalent linkages. In both the SDS-solutions and the DTT-solutions, the denatured whey protein molecules were in the form of monomers or small aggregates. It is likely that, on more extended heating, more disulphide linkages were formed in the SDS-gels whereas more hydrophobic aggregates were formed in the DTT-gels. These results demonstrate that the properties of heat-induced WPC gels are strongly influenced by non-covalent bonding. Intermolecular disulphide bonds appeared to give the rubbery nature of heat-induced WPC gels whereas non-covalent bonds their rigidity and brittle texture.     

SMALL AMPLITUDE OSCILLATORY TESTING (SAOT). INSTRUMENTATION DEVELOPMENT AND APPLICATION TO COAGULATION OF EGG ALBUMEN,WHEY PROTEIN CONCENTRATE AND BEEF WIENER EMULSION3

An instrument to measure the development of protein gels during thermal coagulation was developed. Very small oscillatory movements, sufficiently small to avoid damaging forming structures, were imposed on the sample trapped within a specially constructed cell, and the torques transferred through the sample sensed with strain gauges. Temperatures were controlled with one heating and one refrigerated (20°C) bath and the sample properties determined through both heating and cooling cycles. Egg white (EW) whey protein concentrate (WPC) and beef wiener emulsion (BWE) were tested. EW and WPC were characterized by delayed onset of gelation followed by high temperature thickening. Cooling further stiffened the gel in both cases. B WE was characterized by an initial decrease in transmitted torque as fat melting was detected. This was followed by a rapid rise in transmitted torque as the protein coagulated, followed by a further increase or stiffening on cooling. Detailed parameters describing the thermal gelation of the three materials are given.     

Whey protein hydrolysate: Functional properties,nutritional quality and utilization in beverage formulation

The objective of the study was to analyze the functional and nutritional properties of enzymatically hydrolyzed whey protein concentrate (WPC) and to formulate a beverage mix. WPC hydrolysates were produced using fungal protease and papain, at time intervals of 20, 40 and 60 min and were analyzed for proximate composition and functional properties. A beverage was formulated with hydrolyzed WPC, skim milk powder, cocoa, liquid glucose, sugar and vegetable fat and analyzed for physicochemical properties, sensory attributes and keeping quality. Results revealed that the protein content of WPC was 75.6% and decreased slightly on enzyme treatment (69.6%). The water absorption capacity of WPC was 10 ml/100 g and increased in enzyme treated samples from 16 to 34 ml/100 g with increase in the time of hydrolysis. Emulsion capacity (45 ml of oil/g of control WPC) showed a decreasing trend with increasing time of hydrolysis. Enzyme treatment slightly increased the foam capacity in three samples but lowered foam stability in all. The gel filtration pattern of enzyme treated samples showed an increase in low molecular weight fractions. The amino acid profile showed higher content of methionine in samples treated with enzymes, compared to the control. The in vitro protein digestibility of untreated WPC was 25% and increased in all treated samples to varying degrees (69–70%). Formulated beverage had 52% protein, 10% fat and 6.6% ash. There were no significant differences in the sensory attributes of formulated and commercial beverage. The formulated beverage could be stored well in a PET container for 30 days.     

热诱导温度与pH值对乳清浓缩蛋白凝胶结构和性质的影响

以乳清浓缩蛋白（whey protein concentrate,WPC）为原料,采用动态流变仪、光学微流变仪、圆二色谱仪、荧光分光光度计及扫描电镜探究WPC凝胶形成过程、分子间相互作用和微观结构,并研究热诱导温度（60、85 ℃）和pH值（2.0、4.5、7.0、9.0）对WPC凝胶性质和结构的影响机理。结果表明：pH值通过改变电荷密度影响WPC的凝胶结构;热诱导温度为85 ℃时,蛋白质分子展开更充分,α-螺旋结构含量较低,内源荧光的最大荧光强度波长处红移明显,形成的WPC凝胶具有更高的弹性模量和黏性模量;凝胶的弹性因子和宏观黏度指数较高,固液平衡值较低;相互作用力分析结果说明较高的热诱导温度能促进疏水相互作用、氢键与二硫键的形成,从而改善WPC凝胶的性质和结构。     

Rheological and structural characterization of gels from whey protein hydrolysates/locust bean gum mixed systems

The gelling ability of whey proteins can be changed by limited hydrolysis and by the addition of other components such as polysaccharides. In this work the effect of the concentration of locust bean gum (LBG) on the heat-set gelation of aqueous whey protein hydrolysates (10% w/w) from pepsin and trypsin was assessed at pH 7.0. Whey protein concentrate (WPC) mild hydrolysis (up to 2.5% in the case of pepsin and 1.0% in the case of trypsin) ameliorates the gelling ability. The WPC synergism with LBG is affected by the protein hydrolysis. For a WPC concentration of 10% (w/w), no maximum value was found in the G′ dependence on LBG content in the case of the hydrolysates, unlike the intact WPC. However, for higher protein concentrations, the behaviour of gels from whey proteins or whey protein hydrolysates towards the presence of LBG becomes very similar. In this case, a small amount of LBG in the presence of salt leads to a big enhancement in the gel strength. Further increases in the LBG concentration led to a decrease in the gel strength.     

Factors Influencing Whey Protein Gel Rheology: Dialysis and Calcium Chelation

Influence of dialyzable compounds on the Theological properties (shear stress and shear strain at failure) of heat-induced whey protein concentrate (WPC) and whey protein isolate (WPI) gels was examined. Dialyzing WPC and WPI suspensions prior to gelation increased the stress of two of three WPC gels and a WPI gel. Dialysis also significantly increased the strain of the same two WPC gels, normalizing all strain values. Replacement of calcium lost through dialysis did not significantly change gel rheology. However, chelating calcium caused a significant decrease in the stress of all gels: a minimum amount of calcium and/or a calcium complex appears to have a major role in whey protein gelation.     

Water Binding and Ingredient Dispersion Pattern Effects on Surimi Gel Texture

Water binding, thermotransitional properties and the dispersion pattern of ingredients were studied in relation to their texture-modifying effects in surimi gels. The DSC-measured bound water (unfreezable at ?30°C) of surimi gels prepared with potato starch with and without pregelatinization highly correlated with compressive force (r=0.94) and inversely correlated with expressible moisture (R=?0.99) of the gels. For nonfish proteins, however, physically bound water contributed more than the DSC-measured bound water to gel strength. The ability to undergo thermal transition (size expansion and water absorption) and dispersion pattern of ingredients were responsible for the differences in texture-modifying effects.     

乳清浓缩蛋白对竹荚鱼鱼糜凝胶化和凝胶劣化的影响

采用质构分析法、扫描电子显微镜等方法研究乳清浓缩蛋白对竹荚鱼鱼糜凝胶劣化的抑制作用。结果表明：添加乳清浓缩蛋白(WPC)能显著改善竹荚鱼鱼糜在30℃凝胶化时的凝胶特性,并且添加量为5%(质量分数),加热时间为5h时,竹荚鱼鱼糜的凝胶特性最佳;添加WPC能显著抑制竹荚鱼鱼糜在50℃凝胶劣化现象,WPC的添加量为5%时,抑制效果显著,添加量为10%时,抑制效果最佳;WPC的添加量低于0.5%时,对竹荚鱼鱼糜凝胶色泽的影响不明显;添加量超过1%时,竹荚鱼鱼糜凝胶的白度显著降低。微观结构的观察表明,添加WPC使鱼糜凝胶的结构变得更加致密,因而能增强竹荚鱼鱼糜的凝胶强度。     

Characterisation of heat-set milk protein gels

Milk protein solutions [10% protein, 40/60 whey protein/casein ratio containing whey protein concentrate (WPC) and low-heat or high-heat milk protein concentrate (MPC)] containing fat (4% or 14%) and 70–80% water, form gels with interesting textural and functional properties if heated at high temperatures (90 °C, 15 min; 110 °C, 20 min) without stirring. Adjustment of pH before heating (HCl or glucono-δ-lactone) produces soft, spoonable gels at pH 6.25–6.6, but very firm, cuttable gels at pH 5.25–6.0. Gels made with low-heat MPC, WPC and low fat gave some syneresis; high-fat gels were slightly firmer than low-fat gels. Citrate markedly reduced gel firmness; adding calcium had little effect on firmness, but increased syneresis of low-heat MPC/WPC gels. The gels showed resistance to melting, and could be boiled or fried without flowing. Microstructural analysis indicated a network structure of casein micelles and fat globules interlinked by denatured whey proteins.     

Effect of drying method on the moisture sorption isotherms for Inonotus obliquus mushroom

Moisture sorption isotherms of Inonotus obliquus mushroom were studied over a selected temperature range (20-50 °C). Sigmoid sorption isotherms were observed for these samples. The sorption data were analyzed using various conventional models. The Oswin model was found to be the best model for predicting the equilibrium moisture content of mushroom in the range of water activity 0.08-0.96. The monolayer moisture content decreased as temperature increased and was affected by the drying method used. The net isosteric heat of sorption was determined using the Clausius-Clapeyron equation and the value decreased with increase in moisture content of mushroom.     

Rheological characterizations of texturized whey protein concentrate-based powders produced by reactive supercritical fluid extrusion

A powder blend comprising (by weight) 94% whey protein concentrate (WPC80), 6% pre-gelatinized corn starch, 0.6% CaCl₂, and 0.6% NaCl was texturized using a supercritical fluid extrusion (SCFX) process. The blend was extruded at 90 °C in a pH range of 2.89 to 8.16 with 1% (db) supercritical carbon dioxide (SC-CO₂) and 60% moisture content. The texturized WPC-based (TWPC) samples were dried, grounded into powder, reconstituted in water, and evaluated using a range of rheological studies. Most TWPC samples exhibited shear thinning behavior and their mechanical spectra were typical of weak gel characteristics. The TWPC produced under extremely acidic condition of pH 2.89 with SC-CO₂ yielded the highest η^* (10,049 Pa s) and G′ (9,885 Pa) compared to the unprocessed WPC (η^* = 0.083 Pa s and G’ = 0.036 Pa). The SCFX process rendered WPC into a product with cold-setting gel characteristics that may be suitable for use as a food texturizer over a wide range of temperatures.     

Gelation and Emulsification Properties of Partially Insolubilized Whey Protein Concentrates

Ultrafiltered retentate of whey was heat-processed to prepare whey protein concentrates (WPC) with protein solubilities ranging from 27.5% to 98.1% in 0.1M NaCl, pH 7.0. Proximate and protein compositions of each WPC were determined. Properties of 20% (w/w) protein WPC gels in 0.1M and 0.6 M NaCl, pH 7.0, on heating to 60, 70, 80, and 90°C and emulsification properties of WPC (0.5% (w/w) protein) in 0.1M NaCl at pH 6.0, 7.0 and 8.0 were analyzed. Gel apparent stress and strain at failure decreased and expressible moisture increased as solubility decreased from 98.1% to 41.0% at all heating temperatures. Emulsification Activity Index was highest at pH 7.0, emulsions were most stable at pH 8.0.     

Assessment of the techno-functionality,starch digestion rates and protein quality of rice flour–whey protein instant powders produced in a twin extruder

Whey protein concentrate (WPC) is an important raw material for the production of instant beverages due to its protein properties. A central composite design was devised to analyse the effects of thermoplastic extrusion of 2:1 rice flour:WPC blends in physical, chemical–nutritional and functional properties. Three main factors were selected, screw speed (225–375 r.p.m.), conditioning moisture (17%–23%) and temperature (120–180 °C) to evaluate effects on water absorption (WAI) and solubility (WSI) indexes, viscoamylograph cold and final viscosities, in vitro protein and starch digestibilities and starch hydrolysis indexes (HI). A second-order model showed that linear parameters were significant for all variables studies. Conditioning moisture affected properties more significantly than temperature and screws speed. The best treatment (16% moisture conditioning, 180 °C last barrel zone and screws rotating at 350 r.p.m.) in terms of water solubility had high starch in vitro digestibility and excellent protein quality determined in vitro and in vivo with weanling rats.