Modified Soy Proteins with Improved Foaming and Water Hydration Properties

Soy proteins were modified by alkali treatment at pH 10.0, followed by papain hydrolysis. Solubility, water hydration capacity (WHC), surface hydrophobicity, foaming and emulsifying properties of unmodified, alkali-treated, and papain-modified soy protein (PMSP) were compared. PMSP exhibited higher solubility (100% at pH > 7.0), WHC (3.13) and hydrophobicity (40.8) than unmodified soy protein which had solubility 68.5%, WHC 0.21, and hydrophobicity 8.1. The PMSP had foaming capacity (22.0 mL) similar to egg white (21.2 mL) at pH 7.0; and enhanced foam stability (36.4) compared to the unmodified control (32.9). In general, alkali-treated soy had lower functional properties. Emulsifying properties of PMSP and alkali treated soy were unchanged by the modification. PMSP could be used as an egg white substitute in foaming applications at neutral pH.     

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.     

Foaming Properties of Whey Protein Isolate and λ‐Carrageenan Mixed Systems

Heating protein with polysaccharide under neutral or near neutral pH can induce the formation of soluble complex with improved functional properties. The objective of our research was to investigate the effects of λ‐carrageenan (λC) concentrations and pH on foaming properties of heated whey protein isolate (WPI) and λC soluble complex (h‐cpx) in comparison to heated WPI with added λC (pWPI‐λC), and unheated WPI with λC (WPI‐λC). In all 3 WPI‐λC systems at pH 7, increasing λC concentration led to improved foamability until a certain concentration before it decreased. Despite their higher viscosity, both heated systems (pWPI‐λC and h‐cpx) showed significantly better foamability and foam stability compared to WPI‐λC. Rheological results of foams with 0.25% λC suggested that higher elasticity and viscous films were produced in h‐cpx and pWPI‐λC systems corresponding to better foam stability. Foam microstructure images indicated that foams produced from h‐cpx had thicker film and consisted of smaller initial bubble area and more uniform bubble size. Results from the effect of pH (6.2, 6.5, and 7.0) further confirmed that stronger interactions between WPI and λC during heating contributed to the improved foaming properties. Foam stability was higher in h‐cpx system at all 3 pH levels, especially under pH 6.2 where there were strongest interactions between the biopolymers.     

Foam properties of algae soluble protein isolate: Effect of pH and ionic strength

In this study the foam properties of algae soluble protein isolate (ASPI), a mixture of mainly proteins and polysaccharides, were investigated as function of isolate concentration (0.1–1.0 mg/mL) and pH (3.0–7.0) at 10 mM and 200 mM NaCl. In addition, adsorption kinetics and dilatational elasticity at the air–water interface were studied. Whey protein isolate (WPI) and egg white albumin (EWA) were used as reference proteins. The consistent dilatational behaviour of ASPI at all pH values and ionic strengths tested indicated a similar interfacial composition at all these conditions. Adsorption kinetics, in contrast, were influenced by varying environmental conditions. At increased ionic strength and close to the theoretical isoelectric point calculated based purely on the amino acid composition of ASPI (pH 7) adsorption increased. Since similar adsorption behaviour was also observed for WPI and EWA, the interfacial properties of ASPI are most likely dominated by its protein fraction. This is further confirmed by the fact that ζ-potential measurements suggested an overall isoelectric point of ASPI below pH 3, while adsorption kinetics varied between pH 5 and pH 7 (the theoretical protein-based isoelectric point of ASPI). The overall foam stability of ASPI stabilized foams was superior to those of WPI and EWA in the pH range 5–7. In conclusion, the molecular and interfacial properties of ASPI, a mixture of proteins and polysaccharides, seem to favour the production of very stable foams in this pH range by the selective adsorption of its protein fraction to the air–water interface.     

Biopolymers Produced by Cross-linking Soybean 11S Globulin with Whey Proteins using Transglutaminase

Heterogeneity of biopolymers was determined by cross-linking acetylated-11S acidic subunits (Ac-11S) of soy protein with α-lactalbumin and β-lactoglobulin. The extent of polymerization was determined by electrophoresis and HPLC. Differential scanning calorimetry (DSC) was used to determine thermal properties of starting proteins and biopolymers. HPLC data demonstrated the absence of biopolymers from Ac-11S, acetylated α-lactalbumin and acetylated β-lactoglobulin when each was incubated separately with transglutaminase (TG). However, Ac-11S formed biopolymers with α-lactalbumin and β-lactoglobulin when TG was added. TG catalyzed the formation of heterologous and homologous biopolymers from whey protein isolate (WPI) and soybean 11S globulin (11S). Cross-linking WPI and 11S provided biopolymers with improved heat stability which may be useful to provide functionality to food products.     

Functional Properties of Protein Isolate from Cowpea (Vigna unguiculata L. Walp.)

ABSTRACT: Functional properties of protein isolates prepared from 3 cowpea varieties and 2 soybean varieties in each of 2 y were determined. Both cowpea protein isolate (CPI) and soy protein isolate (SPI) showed a u-shaped curve for solubility with the minimum solubility occurring at pH 4.5. The CPI had lower emulsifying activity than SPI but was similar in stability. Foaming capacity and foaming stability ranged from 58.6 to 60.2 mL and 63.7 to 64.4 min for CPI and from 31.9 to 33.0 mL and 43.4 to 45.0 min for SPI, respectively. Gels were formed at 70 °C for 40 min and 30 min for CPI (12%) and SPI (10%), respectively. The CPI needs modification to enhance functional properties for potential application in food products.     

Surface functional properties of blood plasma protein fractions

The solubility, foaming and emulsifying properties of porcine blood plasma and its main protein fractions (serum, globulins and albumin) were investigated at pH 4.5, 6.0 and 7.5 in order to clarify the contribution of each fraction and encourage the optimisation of plasma-derived products. Soluble protein contents above 85% were obtained in all samples. Plasma, serum and albumin showed good foaming capacities, reasonably similar at different pH conditions, although the highest foam stability corresponded to both albumin and plasma at pH 4.5 and 6.0. All protein fractions showed good emulsifying activities, but the stability of the formed emulsions decreased with acidification, being emulsions of albumin and globulins at pH 7.5 the most stable ones. In addition, the interaction indexes calculated to investigate protein–protein interactions revealed synergistic interactions between albumin and globulins when in co-occurrence in their foaming capacity at pH 6.0 and 7.5, and in the stability of emulsions at pH 4.5 and 6.0, but slightly negative effects in the solubility of the mixture, and a great decrease in the stability of emulsions at pH 7.5. On the other hand, the elimination of fibrinogen improved the stability of emulsions and foams at acidic conditions.     

全蛋液pH值对其功能性质的影响

对全蛋液pH值对其蛋白溶解度、起泡性、乳化性、凝胶强度等功能性质的影响进行了研究。结果表明:在pH 6.5～9.0内,随着全蛋液样品pH值升高,全蛋液的蛋白溶解度、乳化稳定性和凝胶强度逐渐提高,而全蛋液乳化活力逐渐下降;在pH 7.0～7.5内,全蛋液具有较好的起泡力和泡沫稳定性,pH值过高或过低时全蛋液起泡性都会下降;在实际应用中可以根据对全蛋液各种功能性质的不同要求选择适当pH值的全蛋液。     

Simple pH treatment as an effective tool to improve the functional properties of ovomucin

Ovomucin has been considered to contribute a lot to the excellent functional properties of egg white. This work focused on investigating the effects of pH and protein concentration on foaming and emulsifying properties of ovomucin to evaluate the proper use of this egg protein as a functional food ingredient, and to clarify its contribution to the functional properties of egg white under different pH conditions. Protein solubility and surface hydrophobicity were measured through the pH ranged from 2.3 to 11.0. Alkali treatment gave ovomucin improved emulsification properties, which were correlated well with the surface hydrophobicity (r ≥ 0.89, P < 0.01). Although ovomucin showed lower foaming capacity in acid and neutral solution, enhanced foaming stability was observed with weak acid-treated ovomucin (pH 5 to 6) compared to native ovomucin. These results demonstrated that acid and alkali treatment, which leads to partial unfolding of ovomucin can improve functional properties of ovomucin, with the greatest improvement for emulsification properties being from the alkali treatment and for foaming stability being from weak acid treatment. These results are helpful to produce unfolding ovomucin suitable for wide range of applications in food industry, and to provide useful information on the proper use of egg white in different food systems. PRACTICAL APPLICATION: Ovomucin plays a critical functional role in egg white products. However, it is typically insoluble in distilled water or common salt solutions, which has thus limited its commercial applications. Alkaline treatment resulted in gradual increase in solubility, which markedly enhanced the emulsifying properties, on the other hand foaming stability of ovomucin can be promoted by weak acid treatment. The results of this work help to produce unfolding ovomucin suitable for wide range of applications in food industry, and to provide useful information on the proper use of egg white in different food systems.     

Functional properties of raw and heat processed cashew nut (Anacardium occidentale, L.) kernel protein isolates

The functional properties viz. solubility, water and oil absorption, emulsifying and foaming capacities of the protein isolates prepared from raw and heat processed cashew nut kernels were evaluated. Protein solubility vs. pH profile showed the isoelectric point at pH 5 for both isolates. The isolate prepared from raw cashew nuts showed superior solubility at and above isoelectric point pH. The water and oil absorption capacities of the proteins were slightly improved by heat treatment of cashew nut kernels. The emulsifying capacity of the isolates showed solubility dependent behavior and was better for raw cashew nut protein isolate at pH 5 and above. However, heat treated cashew nut protein isolate presented better foaming capacity at pH 7 and 8 but both isolates showed extremely low foam stability as compared to that of egg albumin.     

喷雾干燥与冷冻干燥鸡蛋粉特性研究

以鲜鸡蛋为原料,利用喷雾干燥和冷冻干燥技术制备鸡蛋粉,对比2种蛋粉水分含量、水分活度、溶解度、色差、微观结构等理化性质,同时检测起泡性、乳化性,并选用喷雾干燥蛋黄粉制备凝胶探讨功能特性。结果表明:喷雾干燥蛋粉和冷冻干燥的蛋粉水分含量、水分活度、溶解度和色差差异显著(P<0.05),且喷雾干燥蛋粉和冷冻干燥蛋粉起泡性及乳化性均在氯化钠浓度为0.5 g/100 mL时达到最大值;制备凝胶最佳条件为加水量为150%、氯化钠浓度为3%、温度100℃、热处理15 min。此项研究将对蛋粉的应用奠定理论基础。     

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.     

Screening of Proteolytic Enzymes to Enhance Foaming of Whey Protein Isolates

Whey protein isolate (WPI) was modified to enhance foaming characteristics by controlled hydrolysis using proteolytic enzymes. Alcalase, acid fungal protease, chymotrypsin, pepsin and trypsin were used to hydrolyze 5% rehydrated WPI. Decree of hydrolvsis was estimated by freezing point depression and terminated at 2.5 to 3% by heating or pH adjustment. Controls were treated under similar conditions but without enzymes. Hydrolysates were separated into permeate and retentate by ultrafiltration and concentrated by reverse osmosis before freeze drying. Foam capacity, stability and surface tension of hydrolysates were measured. Permeate from Alcalase exhibited the best foaming characteristics, comparable to egg white.     

Functional properties of 8S globulin fractions from 15 mung bean (Vigna radiata (L.) Wilczek) cultivars

The functional properties including solubility, water absorption capacity, oil absorption capacity, foaming properties and emulsifying properties of 8S globulin fractions from 15 mung bean cultivars were investigated in this study. In addition, the effects of pH on solubility, foaming properties and emulsifying properties were studied. The functional properties of the 8S globulin fractions varied significantly among the different mung bean varieties and exhibited better performance in solubility and emulsion stability compared with soya bean 7S protein. A negative correlation was found between water absorption capacity and oil absorption capacity. Remarkable differences in polypeptides constituents were observed in 8S globulin fractions, and the ratio of 11S/8S globulins has a positive effect on water absorption capacity while a negative effect on oil absorption capacity. As a function of pH, the emulsifying activity indexes of the 8S globulin fractions were found to be distinctly dependent on the solubility, while no significant correlation was found between the emulsifying stability and solubility, nor between the foaming properties and solubility. The foaming capacity showed a strong correlation with foam stability.     

Thermal and Functional Properties of Bovine Blood Plasma and Egg White Proteins

All blood plasma proteins denatured at lower temperatures than the major protein of egg white (ovalbumin). γ-Globulin was the most heat-stable, and fibrinogen was the most heat-sensitive protein of blood plasma. The plasma had similar foaming capacity as egg white, but foam stability of plasma was less. Among plasma fractions, serum albumin, fibrinogen, and α-globulin had good foaming capacities and stabilities. Globulins were the only protein fraction of egg white with good foaming properties. Blood plasma and its component proteins were better emulsifiers than egg white and its component proteins.     

Proteose Peptones and Physical Factors Affect Foaming Properties of Whey Protein Isolate

Effects of peptides and nonprotein components of whey on whey protein isolate (WPI) were studied using a differential pressure method. Decay of WPI foam followed biphasic first-order kinetics, but was affected by solution conditions. WPI foam stability exhibited two pH optima (5.0 and 8.5). Addition of 0.02–0.15M NaCl progressively decreased foaming capacity and foam stability. Addition of 0.01–0.2% proteose-peptones caused a sharp decrease in foam stability, but did not affect WPI foaming capacity. Foam stability was increased by addition of up to 20% lactose. Removal of proteose-peptones should greatly improve foaming properties of whey proteins.     

猕猴桃糖蛋白及其去糖链蛋白功能特性的研究

本文研究了25~60 ℃范围内温度对猕猴桃糖蛋白(CGP)及其去糖链蛋白(GPP)吸油性、溶解性、起泡性和乳化性的影响,以及CGP、GPP的浓度及其溶液pH3~7.5和0~5 g/100 mL范围的NaCl离子强度对CGP和GPP溶解性、起泡性和乳化性的影响。结果表明:25~60 ℃温度范围内CGP吸油性、溶解度高于GPP,随温度升高,CGP、GPP溶解度下降,两者的起泡性先降低后升高,CGP乳化性先降低后升高,GPP乳化性先升高后降低;不同pH条件下,CGP的溶解度始终高于GPP,pH3~6范围内CGP、GPP溶解度均先下降后升高,pH3~7.5范围内CGP、GPP起泡性和乳化性先下降后升高;随离子强度的升高,CGP、GPP溶解度均下降,且CGP的溶解度始终高于GPP,CGP的起泡性和乳化性下降,GPP起泡性先下降后升高而乳化性则相反;CGP、GPP起泡性和乳化性均随其浓度的增高而增高,1.0 mg/mL时起泡性和乳化性最高,0.2 mg/mL时最低。     

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.     

谷朊粉、麦醇溶蛋白与麦谷蛋白基本性质研究

以溶解度、乳化性及乳化稳定性、起泡性及起泡稳定性为考察指标,系统研究不同pH 值条件下,谷朊粉、麦醇溶蛋白、麦谷蛋白的功能特性及其相互间关系。结果表明：pH 值3～11 范围内,谷朊粉的溶解度、乳化性及乳化稳定性、起泡性在pH7 时最小。在同一pH 值条件下,麦醇溶蛋白溶解度、乳化性及乳化稳定性、起泡性及起泡稳定性大于麦谷蛋白,且在乳化性及乳化稳定性方面,麦醇溶蛋白远大于麦谷蛋白。麦醇溶蛋白是提高谷朊粉功能特性的主要成分。     

Selected functional properties of detoxified rapeseed protein preparations effected by phytic acid

Detoxified rapeseed protein preparations with high protein content (>90 %) produced by extraction, ultra-and diafiltration, have a very good solubility and excellent foaming properties (better than egg white). The emulsifying properties (emulsifying activity and emulsion stability) are moderate. The N-solubility profile of these preparations (albumin and globulin mixing) has been influenced by phytic acid (PA). It is possible to observe a shift of the isoelectric range to lower pH-values and parallel a decrease of solubility if the amount of PA (3, 5, 10 %) is increased. The foaming properties have also been dependent on the PA content. A higher concentration of PA (3, 5, 10 %) causes a decrease in the foaming activity. The results have been discussed concerning the interactions between PA and proteins.