Impact of pH on the interactions between whey and egg white proteins as assessed by the foamability of their mixtures

The impact of protein–protein interactions on foaming properties of mixtures consisting of egg white proteins (EWP) and whey proteins (WP) with total protein content of 60 g/L was examined at pH 5, 7 and 9. The ratio between EWP and WP in the mixtures was varied between 67:33, 50:50 and 33:67 (in %; w/w). The ionic strength was adjusted to that of milk (I = 176 mM). The foamability of the protein products was characterized by the foam capacity, stability and firmness. In addition, the hydrophobicity in the protein solutions was assessed as a measure for the physical behaviour and ability of proteins to adsorb at the air–water interface.The individual egg white proteins and whey proteins each showed the best foaming properties at pH 5 and pH 9, respectively. At pH 9 a synergism was observed in the capacity and stability of the foams from EWP/WP-mixtures. This effect appears to be caused by the electrostatic interactions between egg white and whey proteins which occur in the bulk solution after the pH adjustment prior to the foaming. In contrast, at pH 5 no positive influence of foaming the components in a mixture as well as no indication of intermolecular interactions was found. At pH value near the pI of ovalbumin the protein interactions occur when the proteins have adsorbed at the air–water interface. The protein systems foamed at pH 7 showed intermediate foamability compared to the values obtained at alkaline and acidic pH.     

Foaming Characteristics of Commercial Soy Protein Isolate as Influenced by Heat-Induced Aggregation

The foaming properties of commercial soy protein isolate subjected to different temperatures (20–90°C) were assessed. The results revealed that the solubility and surface hydrophobicity of a 5% (w/v) commercial soy protein isolate suspension increased with increasing temperature, which increased foaming capacity and reduced foaming stability. Commercial soy protein isolate supernatant (i.e., soluble fraction) had higher foaming capacity at low temperatures (20–50°C). A high content of commercial soy protein isolate soluble fraction increased foaming capacity but decreased foaming stability. The SDS-PAGE patterns and molecular weight distribution of commercial soy protein isolate revealed that there were soluble, large molecular weight aggregates (>400 kDa) formed mainly from A and B-11S polypeptides of commercial soy protein isolate via disulfide bonds. Additionally, some aggregates also dissociated into small polypeptides and subunits after heat treatment. Commercial soy protein isolate precipitate (i.e., insoluble fraction) had a high content of proline and cysteine, which probably contributed to the foaming stability of commercial soy protein isolate.     

Functional properties of protein isolates,globulin and albumin extracted from Ginkgo biloba seeds

In this study, the functional properties of Ginkgo seed protein isolate (GPI), Ginkgo seed globulin protein (GGP) and Ginkgo seed albumin protein (GAP) extracted from Ginkgo biloba seeds were investigated. The protein contents of GPI, GGP and GAP were 91.0%, 93.4% and 87.8%, respectively in the samples in which the sugar, polyphenol and crude fibre were removed by the preparation procedure. For functional properties of Ginkgo seed proteins in the natural state, GAP showed the highest oil-absorption capacity (9.3 ml/g), foaming capacity (67.8%), emulsifying capacity (65.4%) and emulsion stability (90.6%); while GPI showed the highest water absorption capacity (1.93 ml/g), and GGP showed the highest foam stability (55.5%). The differences of the chemical components, surface hydrophobicity, disulphide bond (SS) and sulfhydryl group (SH) contents of GPI, GGP and GAP, which were correlated significantly with functional properties of Ginkgo seed proteins, were also investigated. The improved functional properties, such as water absorption capacity, solubility, foaming properties and emulsifying properties of Ginkgo seed proteins were observed in a pH range of 8.0–10.0 or sodium chloride concentration of 0.5–0.75 M.     

Effects of succinylation and deamidation on functional properties of oat protein isolate

The effects of two different modification methods (deamidation and succinylation) on the functional properties (solubility, water- and oil-binding capacity, foaming capacity and stability, emulsion activity and stability) of oat protein isolates were evaluated. Protein isolates extracted from defatted oat flour at alkaline pH were acylated by 0.20 g/g of succinic anhydride. The protein isolate was also modified using a mild acidic treatment (HCl, 0.5 N). Succinylation and deamidation improved solubility and emulsifying activity of the native protein isolate. Foaming capacity of oat protein isolate increased after deamidation, whereas succinylation decreased it. The deamidated and succinylated proteins had lower foam and emulsion stabilities than had their native counterpart. Water- and oil-binding capacity, in both modified oat proteins, was higher than those of the native oat protein isolate.     

Enhancement of Functional Properties of Rice Bran Proteins by High Pressure Treatment and Their Correlation with Surface Hydrophobicity

Changes in functional properties of rice bran proteins as influenced by high-pressure (HP) treatment (100–500 MPa, 10 min) were studied. Properties evaluated were protein solubility, water absorption capacity, oil absorption capacity, foaming capacity, foam stability, emulsifying activity, emulsion stability, least gelation concentration, and surface hydrophobicity. HP treatment at 100 and 200 MPa significantly improved the solubility and oil absorption capacity, while water absorption and foaming capacities increased further reaching the maximum at 500 MPa. Compared with the untreated control sample, the emulsifying activity and foam stability of treated samples were significantly higher and least gelation concentration was lower, but none of them showed any specific trend with pressure level. Emulsion stability and surface hydrophobicity increased with the pressure level until 400 MPa and decreased slightly at 500 MPa. Pearson correlation coefficients clearly showed that surface hydrophobicity was positively correlated with water absorption capacity, foaming capacity, emulsifying activity index, and emulsion stability index, but negatively correlated with least gelation concentration. The pressure treated rice bran protein possessed good functional properties for use as a food ingredient in the formulations.     

Emulsifying and foaming capacity and emulsion and foam stability of sesame protein concentrates

This study examined the effects of oil concentration and pH on the emulsifying and foaming characteristics of sesame protein concentrate (SESPC). SESPC was obtained through a simplified process, and its properties were compared with those of a commercial soybean concentrate (SOYPC). The simplified process did not affect the functional characteristics of SESPC, which were often similar or superior to those of the SOYPC. The maximum emulsifying capacity of SESPC was 38% at an acidic and alkaline pH, while the maximum emulsifying capacity of SOYPC was 44% at the same pH. Emulsifying capacity increased significantly as oil concentration increased; in SESPC, this capacity increased from 7.8 to 60.0%, while in SOYPC it increased from 7.6 to 68.2%. The emulsion stability of SESPC was greater at an acidic pH (51%) than at an alkaline pH (45%); it was also higher than the emulsion stability of SOYPC. The maximum emulsion stability of SESPC (96%) was obtained at a sample concentration greater than 55 g L^− 1 and oil concentration lees than 550 g L^− 1 oil. Minimum (118.3%) and maximum (240%) levels of SESPC foaming capacity were higher than those obtained for SOYPC (92% as maximum). These findings show that SESPC may have potential use as raw matter in the food industry. At an extreme pH, SESPC continued to have important functional characteristics like emulsion stability, oil absorption and foaming capacity.     

Extraction,purification and characterization of globulin from common buckwheat (Fagopyrum esculentum Moench) seeds

Salt-soluble globulin was extracted from common buckwheat (Fagopyrum esculentum Moench) seeds. The protein content of buckwheat globulin (BWG) was over 90%. Anion-exchange chromatography (with stepwise salt gradient elution) was used to obtain two fractions of BWG, corresponding to the basic and acidic polypeptides, respectively, at a ratio of approximately 1:2. Sodium dodecyl sulfate polyacrylamide gel electrophoresis showed that the acidic and basic polypeptides were linked by disulfide bonds. The basic polypeptide has an estimated molecular weight of 23–25 kDa, an isoelectric point in slightly alkaline region (pH 8–9), and showed a high degree of homology with other legumin-like proteins. Disulfide and sulfhydryl contents in BWG were estimated as 36.4 and 3.20 μM/g of protein, respectively. BWG exhibited beneficial functional properties such as high solubility, emulsifying activity and emulsion stability, while the foaming properties were relatively poor. BWG had lower water holding capacity and comparable fat binding capacity when compared to a commercial soy protein product.     

Effect of pH on phosphorylation of potato protein isolate

Potato protein isolate (PPI) was phosphorylated with sodium trimetaphosphate (STMP) at ambient temperature and various reaction pH (5.2, 6.2, 8.0 and 10.5) to improve the functional properties without impairing the nutritional availability. Changes in chemical composition (total and coagulable protein content, ash and minerals content and amino acid composition), functional properties (protein solubility index, emulsifying activity and foaming capacity, water and oil absorption capacity) and phosphorus were determined. The chemical composition and functional properties of phosphorylated potato protein isolate (PP-PPI) were significantly different (p < 0.05). The PP-PPI at pH 5.2 was characterised by the highest content of all amino acids, whereas, PP-PPI under alkaline conditions (pH 10.5) caused decrease in these compounds. PP-PPI at pH 8.0 had the highest oil absorption capacity, emulsion activity and foam capacity, whereas, PP-PPI at pH 10.5 had the highest WAC.     

Effect of hydroxypropyl methylcellulose on the textural and whipping properties of whipped cream

In this work, hydroxypropyl methylcellulose (HPMC) was added into whipped cream for improving its textural and whipping properties. By determination of the particle size distribution, a single peak for the emulsion after homogenization and two distinguishable peaks for the emulsion after whipping for 5 min were observed. With the increase of HPMC level, the average particle size (d_3,2) decreased for the emulsion after homogenization and increased for the emulsion after whipping for 5 min. Both whipping time and HPMC level showed positive effects on the partial coalescence of fat globules. The partial coalescence of whipped cream with 0.125% HPMC after whipping for 5 min reached 56.25%, significantly (P < 0.05) higher than that (4.77%) without whipping treatment. Surface protein concentration was measured to evaluate the change of protein content at the droplet interface. The results indicated that the increase of HPMC level could decrease the surface protein concentration slightly. The overrun of whipped cream slightly increased when the HPMC level increased in the range of 0.025–0.125%. Firmness, cohesiveness, consistency and viscosity of whipped cream were analysed in this work. HPMC showed a positive dose-dependent effect on all these textural properties.     

Protein hydrolysates from meriga (Cirrhinus mrigala) egg and evaluation of their functional properties

Protein hydrolysates from underutilised meriga (Cirrhinus mrigala) fish egg were prepared by using commercial Alcalase and papain enzymes. The degree of hydrolysis was 62% for Alcalase and 17.1% for papain, after 90 min digestion at 50–55 and 60–65 °C, respectively. The protein content of Alcalase-produced hydrolysate was higher (85%) than that of papain hydrolysate (70%) (p < 0.05). Hydrolysis by both enzymes increased protein solubility of fish egg protein hydrolysates to above 72.4% over a wide pH range (2–12). Results showed that the hydrolysates had good fat absorption capacity (0.9 and 1.0 g/g sample), foam capacity (70% and 25%) and emulsifying capacity (4.25 and 5.98 ml/g hydrolysate), respectively for Alcalase and papain protein hydrolysates. Gel filtration chromatograms and SDS–PAGE analysis indicated the distribution of smaller peptides. These results suggested that fish egg protein hydrolysates could be useful in the food industry.     

Physicochemical and Functional Properties of Winged Bean Flour and Isolate Compared with Soy Isolate

The proximate composition, amino acid profile and functional properties of isolated winged bean proteins were determined and compared with soy protein isolate. Winged bean protein extracted at pH 10 and pH 12 had protein contents of about 90% and 80%, respectively. Alkali extraction of winged bean proteins at pH 10 and pH 12 did not affect the amino acid distribution of the isolated proteins. Oil and water absorption, emulsion, and foaming properties of winged bean isolated compared favorably with soy isolate. Least gelation concentration for winged bean isolate was 18% compared to 14% for soy isolate. Thus, winged bean protein isolate with its high protein content, high lysine and other essential amino acid content and good functionality has a good potential as an ingredient in food products.     

Characterization of globulin from Phaseolus angularis (red bean)

Phaseolus angularis (red bean) seeds contain about 25% protein (dry basis), almost half of which is globulin. Similar to globulins from other Phaseolus species , 7S vicilin is the major fraction of red bean globulin (RBG), with 11S legumin as a minor component. The amino acid profile of RBG met or exceeded the FAO/WHO standard. Circular dichroism measurements indicate that RBG is a protein rich in α-helical and β-turn structures. RBG exhibited higher protein solubility than Supro 610, a commercial soy protein isolate, especially at acidic pHs, with minimal solubility at around pH 5.0. Compared to Supro 610, RBG had lower water hydration capacity and comparable fat binding capacity, which might be because of its lower surface hydrophobicity. RBG had higher emulsifying activity index and emulsion stability than Supro 610, but with poorer foaming properties.     

Effect of micronisation temperature (130 and 170 °C) on functional properties of cowpea flour

Functional properties of cowpea flour from seeds micronised at two different surface temperatures (130 and 170 °C) were studied. Micronisation (130 and 170 °C) significantly (P ? 0.05) increased the water absorption capacity and least gelation concentration of the flour. The treatment significantly (P ? 0.05) reduced the water solubility and swelling indices, gel strength and foaming capacity of the flour. The changes in cowpea flour functional properties, such as the loss of foaming capacity in flours from micronised (130 and 170 °C) seeds, were associated with significant (P ? 0.05) increase in the surface hydrophobicity and cross-linking of the cowpea protein. SDS–PAGE of the protein-rich fractions revealed changes in the protein subunit profile which included the formation of disulphide bonds and possibly Maillard cross-links. The flour from M-170 °C seeds was significantly (P ? 0.05) darker than was the flour from unmicronised and M-130 °C seeds.     

Physicochemical and functional properties of flour and protein isolates extracted from seinat (Cucumis melo var. tibish) seeds

The physicochemical and functional properties of seinat seed flour (SSF), defatted seinat flour (DSSF), and protein isolates were studied. Protein was extracted from DSSF using an alkali solution with isoelectric precipitation and freeze drying. Freeze dried seinat seed protein isolates (FSSPI), SSF, and DSSF were evaluated for their physicochemical and functional properties. SSF contained high levels of crude fat and fiber (31.13% and 24.75%, respectively). FSSPI contained 91.83% protein versus 28.58% for SSF. The amounts of potassium, the mineral with the highest content, were 9,548.33, 6,439.03, and 1,029 mg/100 g in SSF, DSSF, and FSSPI, respectively. The functional properties were variable among samples. The protein solubility of FSSPI was significantly higher (p<0.05) than for DSSF and SSF. FSSPI has a significantly better (p<0.05) foaming capacity, water/fat absorption capacity, and bulk density than SSF and DSSF. FSSPI also showed an emulsifying capacity comparable to commercial soy protein isolates.     

Effect of some traditional processing operations on the functional properties of African breadfruit seed (Treculia africana) flour

The effect of germination, fermentation, roasting and defatting on the proximate composition, water absorption capacity (WAC), oil absorption capacity (OAC), foaming capacity (FC), foaming stability (FS), emulsion capacity (EC), emulsion stability (ES), packed bulk density (PBD), least gelation concentration (LGC) and protein solubility (PS) of breadfruit seed flour (BSF) was investigated. WAC, OAC, FC, EC, PBD and LGC obtained are 190-380%; 130.3-200.5%; 2.3-60.4%; 12.4-52.9%; 0.4-0.6 g/ml; 6-12% (w/v) and 200-420%; 176.4-320.6; 4.2-70.8%; 20.2-60.4%; 0.5-0.7 g/ml; 0.5-0.8% (w/v) in the full fat and defatted flours respectively. Foams were more stable in the untreated; least in fermented and roasted samples. Defatting improved the FC, FS and EC; roasting and fermentation reduced EC of full fat BSF; Processing and defatting had no effect on the PBD; roasting and germination increased LGC while defatting and fermentation reduced it. Full fat flours had the lowest PS at pH 4 and the highest at pH 8. Fermented full fat BS flour had the highest PS at pH 5 and 8. Defatted germinated, raw dried and roasted BSF had lowest PS at pH 4; PS of fermented BSF is lowest at pH 3 and highest at pH 2.     

桑叶蛋白的功能特性研究

采用超声波辅助提取结合盐酸沉析法提取桑叶蛋白,研究pH值、离子强度、蔗糖质量浓度和温度对桑叶蛋白功能特性的影响。结果表明：远离其等电点时,桑叶蛋白具有良好的持水性、溶解度、乳化性及乳化稳定性、起泡性;桑叶蛋白的持水性、溶解度和起泡性与NaCl浓度(0～1.0mol/L)呈正相关,而过高的离子强度(NaCl浓度高于0.6～0.8mol/L)会使桑叶蛋白的乳化性和乳化稳定性下降;蔗糖的加入会增加桑叶蛋白的持水性,但会降低其溶解度和起泡性,对桑叶蛋白的乳化性和乳化稳定性影响不大;桑叶蛋白的吸油性和起泡性与温度(4～80℃)呈正相关,持水性、溶解度、乳化性及乳化稳定性于60℃时最好。     

苦杏仁蛋白的功能特性

采用稀盐溶液浸提及等电点盐析相结合的方法提取制备苦杏仁蛋白,研究pH值、NaCl浓度、蛋白质量浓度和温度等因素对苦杏仁蛋白功能特性(溶解性、持水性、吸油性、乳化性及乳化稳定性、起泡性及起泡稳定性)的影响。结果表明：在等电点pI附近时,苦杏仁蛋白的溶解性、持水性、乳化性及乳化稳定性、起泡性最差;在较低NaCl浓度范围内(0～0.8mol/L)提高NaCl浓度可促进蛋白溶解性、乳化性及乳化稳定性、起泡性及起泡稳定性的提高,而较高的NaCl浓度对蛋白功能特性提高具有抑制作用;当蛋白质量浓度达到一定水平时(3～4g/100mL),蛋白功能特性(乳化性及乳化稳定性、起泡性及起泡稳定性)提高趋于平缓;在适宜的温度范围内,提高温度可有效提高苦杏仁蛋白各项功能特性,但当温度继续上升,各项功能特性持续降低。     

三聚磷酸钠对猪肉肌原纤维蛋白功能特性的影响

以猪肉肌原纤维蛋白（myofibril protein,MP）为研究对象,探讨不同质量浓度三聚磷酸钠（sodium tripolyphosphate,STP）的添加对MP乳化性、乳化稳定性、起泡性等7 个功能特性指标的影响,并进行相关性分析。结果表明：随着STP质量浓度升高,MP的乳化性、乳化稳定性、起泡性、起泡稳定性、凝胶强度和凝胶保水性均呈上升趋势,表面疏水性呈下降趋势;MP的起泡性和凝胶强度在STP质量浓度为0.3 g/100 mL时最大,乳化性、表面疏水性和凝胶保水性在STP质量浓度为0.4 g/100 mL时效果最佳;MP的起泡性、起泡稳定性和乳化性呈极显著正相关（P＜0.01）,乳化性与乳化稳定性呈显著正相关（P＜0.05）,乳化性、乳化稳定性、起泡性、起泡稳定性与表面疏水性呈极显著负相关（P＜0.01）,与凝胶保水性呈极显著正相关（P＜0.01）,表面疏水性与凝胶保水性呈极显著负相关（P＜0.01）,表面疏水性与凝胶强度呈极显著正相关（P＜0.01）。STP可以增强MP的功能特性,其质量浓度为0.3～0.4 g/100 mL时效果最佳。改善乳化性、起泡性和表面疏水性等界面性质可以增强MP的凝胶特性。     

Improved emulsion stabilizing properties of whey protein isolate by conjugation with pectins

Functional properties of glyco-protein conjugates of the anionic polysaccharide pectin with whey protein isolate, obtained by dry heat treatment at 60 °C for 14 days, have been investigated in O/W emulsions containing 20% (w/w) soybean oil and 0.4% (w/w) protein both at pH 4.0 and 5.5. Emulsion stabilizing properties of mixtures and conjugates were compared at five protein to pectin weight ratios by determining changes in droplet size distribution and extent of serum separation with time. The results indicated that the dry heat-induced covalent binding of low methoxyl pectin to whey protein, as shown by SDS-PAGE, led to a substantial improvement in the emulsifying behaviour at pH 5.5, which is near the isoelectric pH of the main protein β-lactoglobulin. At pH 4.0, however, a deterioration of the emulsifying properties of whey protein was observed using either mixtures of protein and pectin or conjugates.The observed effects could be explained by protein solubility and electrophoretic mobility measurements. The protein solubility at pH 5.5 was hardly changed using mixtures of protein and low methoxyl pectin or conjugates, whereas at pH 4.0 it was decreased considerably. Electrophoretic mobility measurements at pH 5.5 revealed a much more pronounced negative charge on the emulsion droplets in the case of protein–pectin conjugates, which clearly indicated that conjugated pectin did adsorb at the interface even at pH conditions above the protein's iso-electric point. Hence, the improved emulsifying properties of whey protein isolate at pH 5.5 upon conjugation with low methoxyl pectin may be explained by enhanced electrosteric stabilization.Comparing two different commercial pectin samples, it was clearly shown that the dextrose content during dry heat treatment of protein–pectin mixtures should be as low as possible since protein–sugar conjugates not only resulted in increased brown colour development, but also gave raise to a largely decreased protein solubility which very badly affected the emulsifying properties.