Emulsifying properties of soy protein isolate fractions obtained by isoelectric precipitation

Soy protein isolate (SPI) fractions were produced by isoelectric precipitation based on results of isoelectric focusing carried out on the crude soy extract. The fractions were produced from crude protein extract (pH 9.0) sequentially and non‐sequentially at isoelectric points (pIs) of 5.6, 5.1 and 4.5. Emulsions stabilised by soy proteins with pIs between 5.6 and 5.1 had the highest (P < 0.01) emulsion stability index (ESI), while those stabilised with proteins having pIs between 5.1 and 4.5 resulted in the lowest ESI for sequentially precipitated fractions. Non‐sequential fractionation at pI 5.1 produced fractions with higher emulsifying activity index (EAI) than sequential fractionation. SDS‐PAGE profiles indicated that the fractions exhibiting high functionality in terms of ESI and EAI were also richer in 7S globulin protein subunits. © 2001 Society of Chemical Industry     

The effect of addition of flaxseed gum on the emulsion properties of soybean protein isolate (SPI)

The effect of addition of flaxseed gum on the emulsion properties of soybean protein isolate (SPI) were investigated in this study. Flaxseed gum with 0.05-0.5% (w/v) concentration was used together with 1% (w/v) SPI to emulsify 10% (v/v) soybean oil. The emulsion was analyzed for emulsion activity (turbidity), stability, particle size, surface charge, and rheological properties. The turbidity and absolute zeta-potential values decreased initially by the addition of flaxseed gum and subsequently increased with further increase in the gum concentration to reach their peak around 0.35% (w/v) gum. The particle size of the emulsion decreased and reached a minimum value at 0.1% (w/v) gum concentration. Any increase in gum concentration beyond this value resulted into increase in the particle size. This study would help to widen the application of SPI and flaxseed gum mixture, and also contribute to the understanding of protein-gum interaction in emulsion.     

Emulsifying properties of soy protein isolates obtained by microfiltration

Soy protein isolate (SPI) fractions were produced using two different pore size microfiltration membranes. Microfiltration was carried out on SPI produced by isoelectric precipitation of a crude protein extract. Five fractions were obtained: two retentates and two permeates from the two membranes plus an intermediate fraction obtained as the retentate on the small‐pore‐size membrane using the permeate from the larger‐pore‐size membrane. Emulsions stabilised by the retentate fractions exhibited higher values (P < 0.01) of emulsion stability index (ESI) and emulsifying activity index (EAI) than those stabilised with fractions made from the permeates. The intermediate fraction gave intermediate ESI values, while the EAI values were not significantly different from those for SPI and one of the retentates. SDS‐PAGE profiles indicated that the fractions exhibiting high functionality in terms of ESI and EAI were also richer in 7S globulin soy protein subunits. © 2002 Society of Chemical Industry     

Emulsifying properties of chickpea protein isolates: Influence of pH and NaCl

Structure and emulsifying properties of chickpea protein isolates (CPI) as a function of protein concentration, oil volume, pH and ionic strength were studied. The optimum protein concentration 2 g l⁻¹ used to determine the emulsifying properties was obtained. Emulsifying activity index (EAI) increased from 244 to 376 m² g⁻¹ with pH from 3.0 to 11.0 except the protein isoelectric point (pI 5.0), where the EAI was 20 m² g⁻¹ and emulsion droplet size was the largest. At lower ionic strengths (0.0–0.1 M NaCl, pH 7.0), EAI decreased from 253 to 72.4 m² g⁻¹; however, it increased from 72.4 to 231.4 m² g⁻¹ at higher ionic strengths (0.1–1.0 M NaCl). A positive relation between EAI and surface hydrophobicity (S₀) of CPI at various ionic strengths was obtained, while EAI was independent of S₀ under different pH values. α-Helix was the major configuration of CPI at the pI or lower ionic strength.     

Effect of concentrated flaxseed protein on the stability and rheological properties of soybean oil-in-water emulsions

Flaxseed protein concentrate containing-mucilage (FPCCM) was used to stabilize soybean oil-in-water emulsions. The effects of FPCCM concentration (0.5, 1.0, 1.5% w/v) and oil-phase volume fraction (5, 10, 20% v/v) on emulsion stability and rheological properties of the soybean oil-in-water emulsions were investigated. Z-average diameter, zeta-potential, creaming index and rheological properties of emulsions were determined. The result showed that FPCCM concentration significantly affected zeta-potential, creaming rate and emulsion viscosity. The increasing of FPCCM concentration led to a more negative charged droplet and a lower creaming rate. Oil-phase volume fraction significantly affected Z-average diameter, rheological properties, creaming index and creaming rate. With the increase of oil-phase volume fraction, both Z-average diameter and emulsion viscosity increased, while creaming index and creaming rate decreased. The rheological curve suggested that the emulsions were shear-thinning non-Newtonian fluids.     

Functional properties of fish protein hydrolysates from Pacific whiting(Merluccius productus) muscle produced by a commercial protease

Pacific whiting (Merluccius productus) muscle was used to produce hydrolysates with 10%, 15% and 20% degree of hydrolysis (DH) using the commercial protease Alcalase^® and were characterized at pH 4.0, 7.0 and 10 according their solubility, emulsifying and foaming properties. Protein recovered in soluble fractions increased proportionally with the hydrolytic process, yielded 48.6 ± 1.9, 58.6 ± 4.1 and 67.8 ± 1.4 of total protein after 10%, 15% and 20% DH, respectively. Freeze-dried hydrolysates presented almost 100% solubility (p > 0.05) at the different pHs evaluated. Emulsifying properties (EC, EAI and ESI) were not affected by DH as most samples showed similar (p > 0.05) results. Higher EC (p ? 0.05) than sodium caseinate, used as control, were obtained at pH 4 for most hydrolysates. Hydrolysates showed very low foaming capacity not affected by pH; but foam stability was equal or even better (p > 0.05) than bovine serum albumin (BSA), except at pH 4.0. Results suggest that hydrolysates from Pacific whiting muscle can be produced with similar or better functional properties than the food ingredients used as standards.     

Study of Some Functional Properties of Casein: Effect of pH and Tryptic Hydrolysis

The trypsin was used to hydrolyze commercial casein at varied times and pH range. The functional properties studied were the emulsifying capacity (EC), the emulsifying activity index (EAI), and the emulsion stability (ES). The dispersed phase used was corn oil. The tryptic hydrolysis was beneficial to the solubility and EC of casein in practically all pH values and reaction times. In case of EAI, this same effect was less intense and was observed only in acid region (pH 3.0 to 5.0), while for ES the trypsin action was mainly deleterious in almost all pH range and reaction times.     

Emulsifying properties of sweet potato protein: Effect of protein concentration and oil volume fraction

The effect of protein concentrations (0.1, 0.25, 0.5, 1.0, 1.5 and 2.0% w/v) and oil volume fractions (5, 15, 25, 35 and 45% v/v) on properties of stabilized emulsions of sweet potato proteins (SPPs) were investigated by use of the emulsifying activity index (EAI), emulsifying stability index (ESI), droplet size, rheological properties, interfacial properties and optical microscopy measurements at neutral pH. The protein concentration or oil volume fraction significantly affected droplet size, interfacial protein concentration, emulsion apparent viscosity, EAI and ESI. Increasing of protein concentration greatly decreased droplet size, EAI and apparent viscosity of SPP emulsions; however, there was a pronounced increase in ESI and interfacial protein concentration (P < 0.05). In contrast, increasing of oil volume fraction greatly increased droplet size, EAI and emulsion apparent viscosity of SPP emulsions, but decreased ESI and interfacial protein concentration significantly (P < 0.05). The rheological curve suggested that SPP emulsions were shear-thinning non-Newtonian fluids. Optical microscopy clearly demonstrated that droplet aggregates were formed at a lower protein concentration of <0.5% (w/v) due to low interfacial protein concentration, while at higher oil volume fractions of >25% (v/v) there was obvious coalescence. In addition, the main components of adsorbed SPP at the oil–water interface were Sporamin A, Sporamin B and some high-molecular-weight aggregates formed by disulfide linkage.     

The hydrophilic, foaming and emulsifying properties of casein concentrates produced by various methods

The hydrophilic and surfactant properties of casein concentrates made by different processes such as isoelectric precipitation and neutralization (commercial casein, CC) coagulation by rennet (casein clots, COC) and microfiltration/diafiltration (casein micelles, CM) were studied. Water absorption capacity (WAC), water solubility (WS) and water‐holding capacity (WHC) were highest for CM and lowest for COC. Solubility was higher in water and in pH 5.5, 0.10 m NaCl solution for both CM and COC. Foaming capacity was better for CM than for CC at pH 4.0 and for CC at pH 6.0 and 8.0. Foam stability was low for both CM and CC at pH 4.0 but it was high for CM at pH 6.0 and 8.0 and for CC in the absence of salt. Emulsifying capacity was higher for CC at pH 4.0 and 7.0. Stability of emulsion was high for CC at pH 4.0 and for CM at pH 7.0.     

Physicochemical properties of whey protein isolate stabilized oil-in-water emulsions when mixed with flaxseed gum at neutral pH

Concentrations ranging from 0% to 0.33% (w/v) of gum (Emerson and McDuff) were added to the emulsions at pH 7. Particle size distribution, viscosity, ζ-potential, microstructure, and phase separation kinetics of the emulsions were observed. Both polysaccharides and protein coated droplets are negatively charged at this pH, as shown by ζ-potential measurements. At all the concentrations tested, the addition of gum did not affect significantly (p < 0.05) the apparent diameter of the emulsion droplets. At low concentrations (gum  0.075% (w/v)), no visual phase separation was observed and the emulsion showed a Newtonian behaviour. However, at concentrations above the critical concentration of gum, depletion flocculation occurred: when 0.1 flaxseed gum was present, there was visual phase separation over time and the emulsion exhibited shear-thinning behaviour. These results demonstrate that flaxseed gum is a non-interacting polysaccharide at neutral pH; it could then be employed to strengthen the nutritional value of some milk-based drinks, but at limited concentrations.     

Rheological properties and stability of model salad dressing emulsions prepared with a dry-heated soybean protein isolate–dextran mixture

The rheological characteristics of model salad dressing emulsions, incorporating a dry-heated soybean protein isolate (SPI)–dextran mixture as emulsifier, were investigated by applying dynamic rheometry tests in an attempt to probe the emulsion structure and to elucidate the mechanism of their stability against creaming. Both the viscoelastic properties and the creaming behaviour of the dressings were greatly influenced by the extent of protein–dextran conjugation and also by xanthan gum addition. The results are discussed in terms of emulsion droplet interactions which, depending on the extent of glyco-conjugation, may be dominated by depletion or ‘bridging’ flocculation effects and, thereby, influence the droplet network structure collapse during ageing.     

乙醇浸提法制备亚麻籽浓缩蛋白工艺研究

以冷榨亚麻籽饼为原料,采用乙醇浸提法制备亚麻籽浓缩蛋白。采用单因素试验研究了浸提工艺参数(浸提温度、浸提时间、乙醇体积分数、液固比以及浸提次数)对产品蛋白质含量的影响。在单因素试验基础上,采用正交试验进行工艺参数优化。结果表明,在所考察的范围内,各因素影响的主次顺序为乙醇体积分数浸提时间浸提温度液固比;最优工艺条件为浸提温度50℃、浸提时间75 min、乙醇体积分数70%、液固比6∶1、浸提次数2次,在此条件下亚麻籽浓缩蛋白的回收率为63. 87%,蛋白质含量为65. 38%。     

Gelation properties of goose liver protein recovered by isoelectric solubilisation/precipitation process

Isoelectric solubilisation/precipitation (ISP) process was applied to goose liver (GL) for protein extraction. The gelation properties of proteins extracted by acid processes (ACP, pH 2.0, 2.5 and 3.0) and alkaline processes (ALP, pH 11.0, 11.5 and 12.0) were estimated, where the unextracted ground GL was set as the control. Nearly 58.39~79.00% of GL proteins were recovered by ISP treatments. High molecular weight (100~250 kDa) proteins were found to be partially hydrolysed by ACP, while few changes in proteins occurred during ALP. As evidenced by rheological and textural measurements, ALP proteins formed gels with high elasticity and superior texture, whereas ACP proteins had inferior gelation properties. Moreover, ALP proteins were able to form a highly interconnected and homogeneous three‐dimensional microstructure. Predominantly, gels produced by 11.0 had optimal texture and the lowest cooking loss (P < 0.05). These results suggested that the ISP process (ALP) is a potential method to improve the economic value of GL.     

Effect of salt content on the rheological properties of salad dressing-type emulsions stabilized by emulsifier blends

The effects that salt content and composition of emulsifier blends exert on the rheological properties of salad dressing-type emulsions were studied. Binary blends of egg yolk and different types of amphiphilic molecules (Tween 20, sucrose laurate and pea protein), in several proportions, were used to stabilize emulsions. Salt concentration was ranged from 0 to 2.3% w/w. Steady-state flow tests and small-amplitude oscillatory shear measurements within the linear viscoelastic region were carried out. Rheological tests were complemented with droplet size distribution measurements. Rheological properties and physical stability of the emulsions studied were significantly influenced by salt content and the nature of binary emulsifier blends. In general, the values of rheological parameters studied increased with salt content. However, salt affects in much higher extent the properties of emulsions stabilized by high proportions of egg yolk or pea protein in the emulsifier blend, rather than those mainly stabilized by non-ionic low-molecular-weight surfactants, which are less sensitive to changes in the ionic strength. In this sense, the increase observed in the values of viscosity and linear viscoelastic functions of emulsions is more important when a protein is predominant in the emulsifier blend. This effect was explained on the basis of a more apparent increasing interdroplet interactions and viscosity of the continuous medium, both of them induced by salt addition, which lead to the consecution of an extensively flocculated state and improved creaming stability. On the contrary, different blends of pea protein and egg yolk showed a quite similar evolution of the rheological parameters with salt concentration.     

Emulsifying and foaming properties of transglutaminase-treated wheat gluten hydrolysate as influenced by pH,temperature and salt

Hydrolyzed wheat gluten (GH, 77–85% protein) was prepared by limited hydrolysis with chymotrypsin at 37 °C for 4 h (degree of hydrolysis=6.4%) and 15 h (degree of hydrolysis=10.3%). The effect of microbial transglutaminase (MTGase) treatment (55 °C for 1 h, or 5 °C for 18 h) on the emulsifying and foaming properties of GH was evaluated under selected food processing conditions (pH 4.0 and 6.5, 0 and 0.6 M NaCl, and temperature 20 and 5 °C). At pH 4.0 and 0 M NaCl the MTGase treatment substantially increased foaming capacity (FC) of GH compared with their respective control GH samples, as a result of enhanced peptide adsorption to the air–water interface, but FC was similar for both control and MTGase-treated GH at pH 6.5. In contrast, foam drainage stability (FS) of MTGase-treated GH decreased at pH 4.0, but increased significantly (P<0.05) at pH 6.5 when compared with their respective control GH samples. The FC and FS were affected by 0.6 M NaCl in a pH-dependent manner. The MTGase treatments increased emulsion activity index up to 15-fold at pH 6.5, while emulsion stability index was influenced by emulsion temperature and ionic strength conditions. The MTGase-induced changes in functional properties of GH were attributed to pH-dependent solubility changes, the amphiphilic nature of gluten peptides and increased electrostatic repulsion resulting from deamidation.     

胡麻分离蛋白提取工艺研究

为促进胡麻分离蛋白在食品工业中应用,采用碱溶酸沉原理研究胡麻分离蛋白提取工艺。分别讨论料液比、浸提液pH值、浸提温度和时间等条件对蛋白提取率影响,确定最佳提取条件为:料液比1:13、碱提液pH值9.5、时间60、温度60℃,在此条件下,胡麻分离蛋白提取率为42%,纯度达89.37%。     

不同处理方式对鹰嘴豆分离蛋白乳化性质的影响

研究发现微波、超声波、超高压、不同的pH、不同的油含量和不同的离子浓度等都能够影响鹰嘴豆分离蛋白的乳化性质:当微波处理时间为60s,其乳化活性和乳化稳定性都达到最大值;当超声波处理时间为4min时,其乳化活性和乳化稳定性达到最大值;当压力为400MPa时,其乳化活性和乳化稳定性达到最大值;当pH在5.0时,鹰嘴豆蛋白的乳化活力最小,乳化稳定性最高;当NaCl浓度在0.2mol/L时,乳化活性最小,乳化稳定性最高;当加油量在10～30mL范围内,乳化活性逐渐增加,乳化稳定性逐渐降低。      

丝胶蛋白的乳化性能及其影响因素的研究

以废蚕茧为原料,通过高温煮茧得到丝胶蛋白溶液,测定丝胶蛋白溶液的乳化活性、乳化稳定性等指标,结果表明:丝胶蛋白的乳化性能较好。探讨了影响丝胶蛋白乳化性能的因素。乳化性受蛋白质浓度、pH值、离子强度、温度等因素影响较大,具体表现为乳化性能随着蛋白质浓度的增加逐步增大;随pH值的增加先逐渐减小,然后又逐渐增加,在pH值为4时,乳化活性和乳化稳定性达到最小值;乳化活性和乳化稳定性在20℃和50℃之间是随温度的升高而增加,50℃以上随温度的升高而减小;且其受离子浓度影响也是先增后减,在离子浓度为0.6 mol/L时乳化性能最好。     

Antioxidant activity and water-holding capacity of canola protein hydrolysates

Canola protein hydrolysates were prepared using commercial enzymes, namely Alcalase, an endo-peptidase and Flavourzyme with both endo- and exo-peptidase activities. The hydrolysates so prepared were effective as antioxidants in model systems, mainly by scavenging of free radicals and acting as reducing agents. This effect was concentration-dependent and also influenced by the type of enzyme employed in the process. The hydrolysate prepared using flavourzyme showed the highest antioxidant activity among all samples, whereas the hydrolysates prepared by combination of Alcalase and Flavourzyme did not differ significantly (P > 0.05) in antioxidant effectiveness from that produced by Alcalase alone. The hydrolysates were also found to be effective in enhancing water-holding capacity and cooking yield in a meat model system. Their capability in improving the cooking yield of meat was in the order of Flavourzyme hydrolysates > combination hydrolysates > Alcalase hydrolysates. These results suggest that canola protein hydrolysates can be useful in terms of their functionality and as functional food ingredients and that their composition determines their functional properties and thus their potential application in the food and feed industries.     

pH-dependent emulsifying properties of pea [Pisum sativum (L.)] proteins

Emulsifying properties of two partially purified legumin and vicilin (PL and PV) and protein isolate (PPI) from dry pea seeds at various pH values (3.0, 5.0, 7.0 and 9.0) were investigated. The tested emulsion characteristics included droplet size, flocculation and coalescence indices (FI and CI), creaming index, as well as interfacial protein adsorption. Some physicochemical properties of these proteins, e.g., free sulfhydryl and disulfide bond contents, protein solubility (PS), surface hydrophobicity (H_o) and thermal stability (and denaturation), were also characterized. The results indicated that emulsifying ability and emulsion stability of various pea proteins considerably varied with the preparation process, protein composition and pH. Overall, all the pea proteins exhibited least emulsifying ability at pH 5.0 (around isoelectric point), and concomitantly, the resultant emulsions were most unstable against coalescence and creaming. The emulsifying ability of these proteins at pH 3.0 was generally better than that at neutral or alkali pH values, and among all the three proteins, PL exhibited highest emulsifying ability at this pH. The flocculated state and size of droplets in fresh emulsions did not directly affect stability of these emulsions against flocculation and coalescence (upon 24 h of storage), and even creaming (up to 7 days). Interestingly, the PL and PV exhibited much better creaming stability than PPI, at pH deviating from the pI. The emulsifying properties of these proteins were not only related to their PS and H_o, but also associated with the protein adsorption and nature (e.g., viscoelasticity) of interfacial protein films. These results can greatly extend the knowledge for understanding the emulsifying properties of pea proteins, especially the pH dependence of emulsion characteristics.