Some functional properties of fractionated soy protein isolates obtained by microfiltration

Five soy proteins isolate (SPI) fractions were produced using two microfiltration membranes with different pore sizes. Fractionation was carried out on SPI produced by isoelectric precipitation of a crude protein extract. The five fractions were two retentates and two permeates from the two membranes, the fifth fraction was obtained as the retentate on the smaller-pore-sized membrane fed with the permeate from the larger-pore-sized membrane. Solubility, foaming and emulsifying properties of the collected fractionates were investigated. It was observed that in the pH range 3–8 the retentates featured superior solubility compared with permeates. There was no significant difference (p>0.01) in solubility between the retentates and SPI at pH6. Foaming characteristics of the fractions followed the same trend as solubility with regard to foam expansion. There was, however, no particular trend observed with regards to foam stability. Emulsions stabilised by the retentates exhibited higher values (p<0.01) of emulsion stability index (ESI) and emulsifying activity index (EAI) than those stabilised with permeates. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) profiles indicated that the fractions exhibiting high functionality in terms of solubility, foaming and emulsifying properties were also richer in 7S globulin soy protein subunits.Isoelectric focussing (IEF) profiles showed that retentates were richer in species with isoelectric points (pI) between 5.2 and 5.6 while permeates featured more prominently at pIs between 4.5 and 4.8.     

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     

Fractionation of Soy Protein Hydrolysates using Ultrafiltration Membranes

The effect of membrane pore size on the molecular weight distribution and selected functional properties of a protein hydrolysate produced from soy isolate and Pronase was examined. Molecular weight distributions were similar for permeates from 5000, 10,000 and 50,000 molecular weight cut-off (MWCO) membranes: two large fractions at 2300 and 1000 daltons. The 100,000 MWCO membrane resulted in three fractions of 25,000, 13,000 and 2300 daltons. Solubility of the hydrolysate increased with decrease in MWCO, while foam stability decreased.     

Emulsifying properties of proteins extracted from Australian canola meal

Canola protein albumin fraction, globulin fraction, and canola protein isolate (CPI) were compared to commercial soy protein isolate (SPI) in terms of their emulsifying properties at various pH values. The globulin fraction had higher emulsifying capacity (EC), higher emulsifying activity index (EAI), and the droplet size of emulsions it stabilized was consistently smaller irrespective of pH compared to albumin fraction or CPI. In comparison to SPI, globulin fractions also had higher EC at all pH values tested, higher EAI at acidic pH, and smaller or comparable average emulsion droplet size at both pH 4 and 7. The stability of canola protein based emulsions were comparable to those of SPI based emulsions at most pH values (except the emulsion stabilized by the CPI at pH 4), with no significant (p > 0.05) changes in droplet size during storage for up to 7 days at room temperature. These emulsions, however, experienced separation into the emulsion and serum phases after 24 h storage at room temperature with the exception of CPI- and SPI-stabilized emulsions at pH 9. This study demonstrates the comparable emulsifying properties (forming or stabilizing) of some canola proteins to commercially available SPI, suggesting the potential use of canola proteins in food applications.     

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.     

Microporous Ultrafiltration of Skim Milk

Membranes with porosities of 100 and 200 nm were used to obtain a 4:1 milk volume reduction. Average micelle diameters determined from electron micrographs were 46 nm (permeate) and 52 nm (permeate) for the 100-nm-pore fractions and 46 and 55 nm for the 200-nm-pore fractions. The calculated average micellar volumes of the retentate fractions were about twice those of the corresponding permeate fractions. Casein-whey ratios were 0.7-0.9 in the permeates and 5.0-7.7 in the retentates. Higher α_s2- and lower β-casein contents were found in the permeate micelles than in the retentates.     

Surface Tension of Whey and Whey Derivatives

The surface tension of various whole wheys, solutions of component whey proteins, UF fractions, and the effect of heating on the surface tensions of these solutions were determined using the Wilhemy plate method. The mean surface tension of three commercial cottage cheese wheys, a commercial cheddar cheese whey, and a laboratory rennet whey was found to be 41.7 ± 1.2 dyne/cm (25°C) and did not vary significantly with the type of whey despite differences in both pH and protein content. The surface tensions of aqueous solutions of individual pure protein fractions of whey (serum albumin, β-lactoglobulin, α-lactalbumin, and gammaglobulins), in concentrations approximating normal whey contents, were significantly different and greater than for the whole wheys.Heating of individual protein solutions at 80°C for 50 min produced insignificant changes in measured surface tension despite producing protein precipitation in some of the solutions. Similar heating of the whole whey solutions resulted in a significant decrease in surface tension and marked precipitation in most cases.The fractionation of the wheys into UF permeates and retentates resulted in a retentate fraction of significantly lower surface tension than for UF permeates. Heating increased the surface tension of retentate fractions while the permeate fractions showed a decrease.     

酶解产物浓度和油相体积分数对甘薯蛋白酶解产物乳化特性的影响

本文研究了酶解产物浓度(0.10%、0.25%、0.50%、0.75%和1.00%,m/V)和油相体积分数(5%、15%、25%、35%和45%,V/V)对超高压下酶解制得甘薯蛋白酶解产物乳化液显微结构、乳化颗粒平均粒径(d4,3)、乳化活性指数(EAI)、乳化稳定性指数(ESI)和流变学性质的影响。当酶解产物浓度较低和油相体积分数较高时,乳化液的乳化颗粒均一细小。增加甘薯蛋白酶解产物浓度会使其乳化液的d4,3、EAI和ESI均逐渐降低;相反,增加油相体积分数会使乳化液的d4,3逐渐减小,EAI逐渐增大,而ESI则先降低后增加(p0.05)。在酶解产物浓度低和油相体积分数高时,乳化液的初始表观粘度较大,且在1~100 s-1的剪切速率范围内均表现出了剪切变稀现象。酶解产物浓度和油相体积分数与乳化液的d4,3、EAI、ESI和流变学性质密切相关,是影响甘薯蛋白酶解产物乳化特性的重要因素。     

Food Protein Functionality in a Liquid System: A Comparison of Deamidated Wheat Protein with Dairy and Soy Proteins

ABSTRACT: Solubility, surface properties, overrun, foam stability, apparent viscosity, and emulsification properties were evaluated for 3% protein dispersions of deamidated wheat protein (DWP), sodium caseinate (SC), soy protein isolate (SPI), and whey protein isolate (WPI). DWP dispersion had the highest apparent viscosity, 25% higher emulsion activity index (EAI), and 82% higher emulsion stability index (ESI) when compared to SPI dispersions. Dispersions of DWP had similar foaming properties and surface properties when compared to SC, but had 50% higher EAI and 1000% greater ESI when compared to the 2 dairy proteins. The utilization of DWP could be expanded into liquid food systems currently using dairy proteins.     

A Process to Produce Light Colored Protein Isolate from Defatted Glandless Cottonseed Flour

Light colored protein isolates could be produced from aqueous protein extract (at pH 9.0) of defatted cottonseed flour by filtering through an ultrafiltration membrane with 100,000 MWCO (molecular weight cut off) pore size and then spray-drying the retentate. The yield of this protein fraction was approximately 68% of the extracted solid. About 15% of the extracted solid was recovered with the low molecular fraction (50,000 daltons) when the permeate of 100,000 MWCO was applied to 50,000 MWCO membrane. Most of the color-causing pigments were associated with the low molecular fraction.     

Characterization of Nitrogen Fractions During Ripening of a Soft Cheese Made from Ultrafiltration Retentates

Nitrogen fractions of a soft cheese made from UF retentates were used to characterize the ripening of the cheese. Whole milk was fractionated, using UF and diafiltration to a retentate concentration factor of five times. Control and experimental soft, white cheeses were made from whole milk and UF retentate, respectively. Both cheeses were ripened at 8°C for 21 d and analyzed at 7-d intervals. Nitrogen fractions were separated and discontinuous PAGE was used to characterize total protein and whey protein. A ripening extension index related to rennet activity was determined based on the ratio of soluble N to total N. A ripening depth index related to starter peptidase activity was determined by the ratio nonprotein N/total N. Increases in ripening extension index and ripening depth were higher (48.45 and 18.56%, respectively) in UF cheese than in regular cheese (41.06 and 17.11%, respectively). The N fractions soluble in 20% sodium sulfate were composed mainly of bovine serum albumin, β-lactoglobulin A and B, and α-lactalbumin in fresh and ripened UF cheese. Whey protein N represented about 17 and .5% of total N in UF and regular cheese, respectively. No significant breakdown was detected in the whey protein N fraction in the UF cheese.     

Short communication: Calcium partitioning during microfiltration of milk and its influence on rennet coagulation time

Pasteurized skim milk was subjected to (1) microfiltration (MF) at 50°C and (2) MF at 6°C after storage at 2°C. The products of these treatments were retentate (RMF50) and permeate (PMF50), and retentate (RMF6) and permeate (PMF6), respectively. Additionally, RMF50 was subjected to (3) cold MF after water dilution to produce retentate (RMF6R) and permeate (PMF6R). Calcium migration was monitored by analyzing ionic, soluble, and total calcium content in feed, retentates, and permeates. The influence of calcium partitioning and calcium addition to feed, retentates, and retentates diluted with water was determined. Without CaCl₂ addition, only skim milk, RMF50, and RMF6 coagulated after rennet addition. Higher true protein and casein content of RMF50 and RMF6 resulted in shorter time of renneting. The retentates diluted with water showed no signs of coagulation within 40 min. The addition of PMF6R to RMF50 did not affect rennet coagulation time within the observed 40 min in comparison to RMF50 + water. In general, higher CaCl₂ addition resulted in shorter rennet coagulation time. Special attention should be paid to calcium partitioning during membrane processing of cheesemilk. The level of calcium addition should be adopted to calcium content in such cheesemilk, which is affected by conditions of the filtration process (i.e., concentration factor and temperature).     

大豆球蛋白-花青素Pickering乳液性质

制备大豆分离蛋白(soybean protein isolate,SPI)与花青素(anthocyanin,ACN)共价复合Pickering乳液。研究不同ACN体积分数下,共价复合颗粒的表面疏水性,Pickering乳液的乳化性与乳化稳定性、流变性质和微观结构。结果显示,当ACN体积分数由0%增加到0.15%时,共价复合颗粒的表面疏水性由18174降低到8945;Pickering乳液的乳化性增加了127 m^2/g,乳化稳定性增加了近1倍;同时乳液脂滴状态得到了明显的改善。实验结果证明,乳液呈现类固体特性,表现出典型非牛顿假塑性行为。本研究还发现,随着ACN的添加,SPI-ACN共价复合Pickering乳液呈现出桥接乳液形态,这将为食品行业中开发新型Pickering乳液提供理论参考。     

超声处理辅助大豆分离蛋白改善蛋黄乳化性

蛋黄(Egg yolk,EY)的乳化特性易受加工因素影响,为了改善其乳化性能,采用大豆分离蛋白(Soy protein isolate,SPI)辅以超声处理,探究不同超声功率对大豆分离蛋白改善蛋黄乳液乳化性及蛋黄蛋白性能的影响.结果 表明:在EY中添加SPI,可以显著提高EY的乳化活性(Emulsifying acti...     

高压均质对大豆β-伴球蛋白富集组分乳化特性的影响

研究了高压均质对大豆β-伴球蛋白(7S)富集组分乳化活性、乳化稳定性、粒度分布和乳析稳定性的影响。结果表明:与未均质相比,均质处理使7S富集组分乳化活性降低,但可提高其乳化稳定性;乳化活性随均质压力的升高而降低,均质次数对其影响不明显,随着均质压力的升高和均质次数的增多7S富集组分乳化稳定性逐渐提高;高压均质改性的7S富集组分制备的乳状液粒径更小,并且乳析率下降;均质压力不变时,一次均质的7S富集组分比2次均质的7S富集组分形成的乳状液粒径更大,但乳析率降低。     

Emulsifying properties of canola and flaxseed protein isolates produced by isoelectric precipitation and salt extraction

The emulsifying (emulsion capacity, EC; emulsion activity/stability indices, EAI–ESI and creaming stability, CS) and physicochemical properties (surface charge/hydrophobicity, protein solubility, interfacial tension, and droplet size) of chickpea (ChPI), faba bean (FbPI), lentil (LPI), and pea (PPI) protein isolates produced by isoelectric precipitation and salt extraction were investigated relative to each other and a soy protein isolate (SPI). Both the legume source and method of isolate production showed significant effects on the emulsifying and physicochemical properties of the proteins tested. All legume proteins carried a net negative charge at neutral pH, and had surface hydrophobicity values ranging between 53.0 and 84.8 (H₀-ANS), with PPI showing the highest value. Isoelectric precipitation resulted in isolates with higher surface charge and solubility compared to those produced via salt extraction. The EC values ranged between 476 and 542 g oil/g protein with LPI showing the highest capacity. Isoelectric-precipitated ChPI and LPI had relatively high surface charges (~−22.3 mV) and formed emulsions with smaller droplet sizes (~ 1.6 μm), they also displayed high EAI (~ 46.2 m²/g), ESI (~ 84.9 min) and CS (98.6%) results, which were comparable to the SPI.     

Determination of the efficiency of removal of whey protein from sweet whey with ceramic microfiltration membranes

Our research objective was to measure percent removal of whey protein from separated sweet whey using 0.1-µm uniform transmembrane pressure ceramic microfiltration (MF) membranes in a sequential batch 3-stage, 3× process at 50°C. Cheddar cheese whey was centrifugally separated to remove fat at 72°C and pasteurized (72°C for 15 s), cooled to 4°C, and held overnight. Separated whey (375 kg) was heated to 50°C with a plate heat exchanger and microfiltered using a pilot-scale ceramic 0.1-µm uniform transmembrane pressure MF system in bleed-and-feed mode at 50°C in a sequential batch 3-stage (2 diafiltration stages) process to produce a 3× MF retentate and MF permeate. Feed, retentate, and permeate samples were analyzed for total nitrogen, noncasein nitrogen, and nonprotein nitrogen using the Kjeldahl method. Sodium dodecyl sulfate-PAGE analysis was also performed on the whey feeds, retentates, and permeates from each stage. A flux of 54 kg/m² per hour was achieved with 0.1-µm ceramic uniform transmembrane pressure microfiltration membranes at 50°C. About 85% of the total nitrogen in the whey feed passed though the membrane into the permeate. No passage of lactoferrin from the sweet whey feed of the MF into the MF permeate was detected. There was some passage of IgG, bovine serum albumen, glycomacropeptide, and casein proteolysis products into the permeate. β-Lactoglobulin was in higher concentration in the retentate than the permeate, indicating that it was partially blocked from passage through the ceramic MF membrane.     

Vatless manufacturing of low-moisture part-skim mozzarella cheese from highly concentrated skim milk microfiltration retentates

Low-moisture, part-skim (LMPS) Mozzarella cheeses were made from concentration factor (CF) 6, 7, 8, and 9, pH 6.0 skim milk microfiltration (MF) retentates using a vatless cheese-making process. The compositional and proteolytic effects of cheese made from 4 CF retentates were evaluated as well as their functional properties (meltability and stretchability). Pasteurized skim milk was microfiltered using a 0.1-microm ceramic membrane at 50 degrees C to a retentate CF of 6, 7, 8, and 9. An appropriate amount of cream was added to achieve a constant casein:fat ratio in the 4 cheesemilks. The ratio of rennet to casein was also kept constant in the 4 cheesemilks. The compositional characteristics of the cheeses made from MF retentates did not vary with retentate CF and were within the legal range for LMPS Mozzarella cheese. The observed reduction in whey drained was greater than 90% in the cheese making from the 4 CF retentates studied. The development of proteolytic and functional characteristics was slower in the MF cheeses than in the commercial samples that were used for comparison due to the absence of starter culture, the lower level of rennet used, and the inhibition of cheese proteolysis due to the inhibitory effect of residual whey proteins retained in the MF retentates, particularly high molecular weight fractions.     

槲皮素、芦丁与大豆分离蛋白非共价作用机制及其功能性和消化性研究

本文分析了槲皮素-大豆分离蛋白与芦丁-大豆分离蛋白复合物功能性(溶解性、乳化性、凝胶性)和消化性的变化,并利用紫外可见光谱法、荧光光谱法研究互作机理,解析了其荧光淬灭类型、结合位点数以及热力学参数。结果发现,两种黄酮均可提高SPI的功能性质,当槲皮素与芦丁添加量分别为8%时,SPI凝胶硬度可分别提高23.23%及187.18%;随着槲皮素添加量的增加,SPI 的 EAI、 ESI 和溶解性先增加后趋于平缓,添加量为6%和4%时,乳化活性和溶解性分别达到最高,与SPI相比,分别提高 20.84%和 10.06%;随着芦丁添加量的增加,SPI 的 EAI、 ESI 和溶解性先增加后略有下降,在添加量为4%和6%时,乳化活性和溶解性分别达到最高,与SPI相比,分别提高26.17%和19.27%。此外,槲皮素、芦丁分别与SPI相互作用后还可提高蛋白的生物利用度,进一步研究两种黄酮多酚与SPI互作机制表明,两种互作复合物的荧光光谱均发生蓝移现象,槲皮素、芦丁与SPI自发结合,并主要通过氢键和范德华力方式作用,其中槲皮素、芦丁与SPI互作机制分别为动态淬灭及静态淬灭。     

酱油渣中蛋白的乳化特性研究

对比分析了酱油渣中蛋白(SRP)、糖基化大豆分离蛋白(GSP)和大豆分离蛋白(SPI)的ξ-电位、疏水性以及乳化活性和乳化稳定性。发现SRP的总糖和蛋白含量比为1∶1.4,其中含有大量的糖蛋白;SRP疏水性是SPI的2.5倍。SRP等电点接近pH=3.5,在酸性环境下溶解性较好。在酸性、高盐环境下SRP乳化能力高于GSP和SPI,在pH=5时,SRP的乳化活性(EAI)是SPI的8.1倍,在NaCl浓度为0.3mol/L时,SRP的EAI是SPI的1.77倍。