Effect of pH on the functional behaviour of pea protein isolate–gum Arabic complexes

The functional behaviour (solubility, emulsifying and foaming properties) of pea protein isolate (PPI) and gum Arabic (GA) mixtures were investigated as a function of pH (4.30–2.40) within a region dominated by complex coacervation. Emulsion stability was also investigated using a one- and two-step emulsification approach. Complex coacervation was monitored by turbidimetric acid titration at a 2:1 PPI–GA ratio to reveal the formation of soluble (pH 4.23) and insoluble (pH 3.77) complexes, maximum biopolymer interactions (pH 3.60), and dissolution of complexes (pH 2.62). Emulsion stability was greater for mixed systems relative to PPI alone at pHs between 3.10 and 4.00, and in those prepared using the one-step method. Foam expansion was independent of both biopolymer content and pH, whereas foam stability was improved for the mixed system between pH 3.10 and 4.00. The pH-solubility minimum was broadened relative to PPI to more acidic pHs. Findings suggest that admixtures of PPI and GA under complexing conditions could represent a new blended food and/or biomaterial ingredient.     

Functional properties and structural characteristics of phosphorylated pea protein isolate

In order to expand the application of pea proteins in the food industry, pea protein isolate (PPI) was chemically phosphorylated to improve its functional properties. Based on the comprehensive membership value (CMV) degree, the optimal condition for PPI phosphorylation modification was as follows: pH 12, modification temperature at 70 °C and an addition of 7.0% (w/v) sodium tripolyphosphate (STP). Under this condition, the solubility, emulsifying property, emulsifying stability, foaming property and oil absorption capacity of the modified PPI were improved substantially. In addition, the structure of modified PPI was characterised by scanning electron microscope (SEM) and Fourier transform infrared (FTIR) spectroscopy. The results showed that the modified PPI had a smooth and uniform lamellar structure, where the content of α-helix and β-sheet structure increased, but the content of β-corner and random coil structure decreased. The thermodynamic properties were analysed by differential scanning calorimetry (DSC) and the results showed that ∆H of the modified PPI increased significantly. Finally, the optimum phosphorylated PPI was mixed with 0.4% (w/v) xanthan gum to form PPI fat mimics (PPI-FM). PPI-FM was added into mango mousse cake to reduce the amount of light cream, and the result showed up to 20% of light cream could be substituted.     

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.     

Complexation between milk proteins and polysaccharides via electrostatic interaction: principles and applications – a review

This article details recent research conducted on the complexation between milk proteins and polysaccharides and the properties of the complexes, and the application of such relationships to the food industry. Complexation between proteins and polysaccharides through electrostatic interactions gives either soluble complexes in a stable solution or insoluble complexes, leading to phase separation. The formation and the stability of these complexes are influenced by pH, ionic strength, ratio of protein to polysaccharide, charge density of protein and polysaccharide as well as processing conditions (temperature, shearing and time). The functional properties of milk proteins, such as solubility, surface activity, conformational stability, gel‐forming ability, emulsifying properties and foaming properties, are improved through the formation of complexes with polysaccharides. These changes in the functional properties provide opportunities to create new ingredients for the food industry.     

Emulsifying properties of the transglutaminase-treated crosslinked product between peanut protein and fish (Decapterus maruadsi) protein hydrolysates

BACKGROUND: Defatted peanut meal, a protein‐rich by‐product from the oil extraction industry, is underutilised owing to its inferior functional properties. In this study, transglutaminase (TGase) crosslinking and proteolysis were used to improve the emulsifying properties of peanut protein isolate (PPI) extracted from the meal. PPI and PPI hydrolysate (PPIH) were conjugated separately with fish (Decapterus maruadsi) protein hydrolysate (DPH), catalysed by TGase to obtain improvements in the emulsifying properties. RESULTS: Analyses by electrophoresis and high‐performance liquid chromatography indicated that polymers were formed in all TGase‐treated samples. In emulsions of PPIH, PPI‐DPH and PPIH‐DPH the volume/surface average particle diameter (d₃₂), creaming and instability phenomenon were decreased and the zeta‐potential was increased after TGase treatment, showing improved emulsifying activity and emulsion stability. In the case of PPI, TGase treatment had no effect on the emulsifying activity, but the emulsion stability of TGase‐treated PPI was improved. CONCLUSION: The study showed that TGase crosslinking and proteolysis could improve the emulsifying properties of PPI, while proteolysis followed by TGase crosslinking proved more efficient. The emulsifying properties of the heterologous protein systems of PPI‐DPH and PPIH‐DPH were also improved by TGase treatment. Copyright © 2010 Society of Chemical Industry     

响应面优化豌豆分离蛋白-木聚糖轭合物的制备及结构功能研究

采用响应面法优化豌豆分离蛋白(PPI)-木聚糖轭合物的制备条件,并对所得PPI-木聚糖轭合物的结构性质和功能特性进行研究。结果表明,PPI-木聚糖轭合物的最佳制备条件为：溶液pH 8.15、加热温度60℃和反应时间160 min;在此条件下,轭合物的接枝度为60.92%。电泳分析结果表明,木聚糖被接枝到PPI分子上,表现为比原蛋白更大的分子质量;红外光谱分析结果表明糖基化改变了PPI的二级结构;内源荧光光谱结果表明PPI的三级结构受到改变,降低了荧光强度。相较于原蛋白,轭合物的溶解度得到显著改善,在pH 4时的溶解度从3.26%提升到9.08%;在pH 5时的溶解度从2.10%提升到7.63%。糖基化产物轭合物的乳化性能也明显提升,乳化活性指数从20.97 m²/g提高到40.23 m²/g;乳化稳定指数从11.23 min提升到65.51 min。     

植物球蛋白/姜黄素纳米复合物的制备及其对O/W型Pickering乳液氧化稳定性影响

本论文以两类植物球蛋白:豌豆分离蛋白(PPI)和大豆分离蛋白(SPI)为材料制备荷载姜黄素蛋白纳米复合物,并探究荷载前后蛋白所制备乳液的物理和氧化稳定性差异。结果表明:PPI和SPI在pH 3.0和pH 7.0下荷载前后蛋白纳米颗粒粒径没有明显变化。pH 7.0时两蛋白姜黄素荷载量均高于pH 3.0,各pH下SPI荷载量要高于PPI。表面疏水性的显著降低与荧光淬灭现象发生表明形成两种蛋白纳米复合物的主要作用力为疏水相互作用,同时在两pH下,PPI比SPI荧光蓝移趋势更明显且有效淬灭常数也更大,即更易形成复合物。与原蛋白相比,荷载后各蛋白颗粒所制备乳液乳化活性有少许降低,同时pH 3.0时各蛋白颗粒乳化活性要高于pH 7.0。各乳液生成初级氧化产物脂质氢过氧化物浓度的变化趋势与生成次级氧化产物TBARS相类似,均为荷载姜黄素后各乳液氧化水平加速,同时pH 3.0时各类型乳液油滴氧化程度均高于pH 7.0。     

Comparative studies on the physicochemical properties of peanut protein isolate–polysaccharide conjugates prepared by ultrasonic treatment or classical heating

Peanut protein isolate (PPI) was glycated with dextran or gum Arabic through ultrasonic treatment or classical heating. The physicochemical properties of PPI–polysaccharide conjugates prepared by ultrasonic treatment were compared to those prepared by classical heating. Compared with classical heating, ultrasound could accelerate the graft reaction between PPI and polysaccharides. PPI could glycate more dextran than gum Arabic under both ultrasonic treatment and classical heating. Despite the higher degree of graft, ultrasonic treatment was able to prepare PPI–polysaccharide conjugates with higher color lightness as well as lower yellow tones than classical heating. During glycation, high molecular weight component was formed, and conarachin mainly participated in glycation reaction instead of arachin. Solubility and emulsifying properties of the conjugates prepared through ultrasonic treatment were both improved as compared to conjugates obtained by classical heating and PPI. The solubility of PPI–dextran was improved for pH range 3 to 9, while that of PPI–gum Arabic was improved for pH > 7. Meanwhile, the emulsifying properties of PPI–gum Arabic were better than those of PPI–dextran conjugates. Decrease of lysine and arginine contents suggested these two amino acids attended the glycation between PPI and polysaccharides. Structural feature analyses suggested that conjugates obtained by ultrasonic treatment had less α-helix and more β-structures, higher surface hydrophobicity and less compact tertiary structure as compared to conjugates obtained by classical heating and PPI.     

大豆分离蛋白-花青素复合物的制备及其蛋白结构与功能性质分析

大豆分离蛋白经热处理后与花青素进行复合形成复合物,采用荧光光谱表征复合体系构象变化,以溶解性、乳化性、乳化稳定性、粒度分析及Zeta电位为指标分析该复合体系中大豆分离蛋白二级结构的变化与功能性质表达之间的关系。结果表明：在pH?7.4的条件下,热处理大豆分离蛋白与花青素复合后,大豆分离蛋白的Zeta电位绝对值显著增大,乳化性、乳化稳定性显著提高,但溶解性显著下降。通过荧光光谱分析发现花青素对热处理大豆分离蛋白的荧光猝灭机制为静态猝灭,蛋白与花青素间形成了结合位点数近似于1的复合物,三维荧光光谱结果表明花青素的复合使得蛋白质多肽链的骨架伸展,蛋白结构发生变化。     

Complex coacervation in pea protein isolate-chitosan mixtures

Protein-polysaccharide interactions play an essential structure-controlling role in foods and biomaterials. Turbidity and electrophoretic mobility measurements were used to investigate the formation of soluble and insoluble complexes between pea protein isolate (PPI) and the cationic polysaccharide, chitosan (Ch) as a function of pH and biopolymer mixing ratio (1:1-20:1 PPI-Ch). In addition, pH-induced conformational changes of PPI upon complexation with Ch were studied by fluorometry. As the PPI-Ch mixing ratio increased from 1:1 to 12.5:1, critical structure forming events (i.e., those associated with the formation of soluble and insoluble complexes) shifted to higher pHs, and progressively behaved similar to those for PPI alone. At biopolymer ratios > 15:1, mixed systems resembled that of PPI alone. Changes to the tertiary conformation of PPI upon complexation with Ch at a 7.5:1 biopolymer ratio were found to occur at pH 6.2, corresponding to the presence of insoluble complexes.     

Stabilization of acidic soy protein-based dispersions and emulsions by soy soluble polysaccharides

Soy soluble polysaccharides (SSPS) are shown to prevent destabilization of soy protein isolate (SPI) dispersions and SPI-based oil-in-water (O/W) emulsions under acidic conditions. Addition of SSPS above a critical concentration (0.25 wt%) increased the stability of 0.50 wt% SPI dispersions against aggregation and phase separation under conditions where SPI would normally precipitate (near its isoelectric point). Though SSPS neutralized SPI surface charge via electrostatic interaction, there was increased stability against aggregation due to steric repulsion. At acidic pH, addition of 1 wt% NaCl electrostatically screened protein–polysaccharide complexation which led to SPI precipitation and sedimentation. However, the order of salt addition had a significant impact on charge screening, with salt added before pH adjustment reducing SPI–SSPS complexation whereas it had less effect when added afterwards. Salt penetration efficacy diminished with decreasing pH. O/W emulsions (5 wt% oil) prepared with 0.50 wt% SPI destabilized at pH 4–5 due to protein aggregation, but addition of ≥0.25 wt% SSPS improved emulsion stability by inhibiting protein–protein interactions thus limiting increases in oil droplet diameter over time. Overall, both dispersion and emulsion stability greatly depended on pH, ionic strength and SSPS concentration. These results demonstrated that SSPS could effectively stabilize acidic SPI dispersions and that SPI–SSPS interactions may be used as a tool to improve the kinetic stability of SPI-based O/W emulsions.     

红衣组分对花生分离蛋白及其酶解产物理化和抗氧化性质的影响

以花生为原料,研究了花生红衣组分对花生分离蛋白及其酶解产物理化和抗氧化性质的影响。研究结果表明:含红衣的分离蛋白酶解速度低于不含红衣的;相同水解度条件下,含红衣的表面疏水性小于脱红衣的;GPC分布中,含红衣的峰值大于脱红衣的;红衣组分能够提高花生分离蛋白及其酶解产物的溶解性、乳化稳定性、乳化活性;在相同水解度条件下,含红衣的水解产物多酚含量显著高于脱红衣的,多酚含量的差异与花生分离蛋白及其水解产物的抗氧化性具有正相关性。     

Effect of extraction conditions on composition,surface activity and rheological properties of protein isolates from flaxseed (Linum usitativissimum L)

Flaxseed protein isolates were prepared by micellisation (FM) and isoeletric precipitation (FI). The influence of preparation conditions on composition and functional properties was investigated. Contents of 0.6% phytic acid and 2.3% pentosans were found for FI, whereas FM was almost phytic acid‐free and had a low content of pentosans (0.6%). Chromatography and electrophoresis identified the 11S globulin (linin) as the main protein fraction in both isolates. Protein solubility, water‐ and oil‐binding capacities, emulsification and rheological properties of dispersions and gels were measured at pH 8 and 3. For the latter, interactions of protein with phytic acid and pentosans are highly probable. FI possesses a lower solubility (about 40–50%) and an overall higher water‐binding capacity than FM. For FI dispersions a higher storage modulus G′ than loss modulus G″ was measured, clearly pointing to the formation of protein networks. Moreover, FI formed stronger gels than FM (G′ about fivefold). The emulsifying activity, however, was distinctly lower for FI. These results point to enhanced complexation and aggregation of the isoelectric‐precipitated protein isolate. © 2002 Society of Chemical Industry     

花生分离蛋白磷酸化改性研究

采用响应面优化法对花生分离蛋白进行磷酸化改性,以氮溶解指数(NSI)为指标得出花生分离蛋白磷酸化改性的最佳条件为三聚磷酸钠添加量7.77%、花生分离蛋白质量分数6.38%、反应温度44.85℃、反应体系pH8.24、反应时间5.68h。得到的花生改性蛋白NSI 最大值为77.74%。改性后,花生分离蛋白的吸油性、吸水性、持水性、乳化性、乳化稳定性、泡沫稳定性都有不同程度的提高。     

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.     

Emulsifying and Surface Properties of Wheat Gluten under Acidic Conditions

The solubility of wheat gluten was greatly improved at pH 4 or lower where it showed good emulsifying activity. This might be due to its high surface activity in the acidic pH range and the formation of a stable protein film surrounding the oil droplets. Among the major gluten proteins, gliadins showed higher surface activity than glutenins. The content of glutenins in the adsorbed protein film was higher than that of gliadins, and glutenins are likely to have been adsorbed more tightly than gliadins. These results suggest that gluten proteins exhibit complex behavior, such as adsorption/desorption/displacement/rearrangement during the adsorption process in a gluten‐stabilized emulsion.     

Complex coacervation of pea protein isolate and alginate polysaccharides

Complex coacervation between pea protein isolate (PPI) and alginate (AL) was investigated as a function of pH (1.50–7.00) and mixing ratio (1:1–20:1 PPI:AL) by turbidimetric analysis and electrophoretic mobility during an acid titration. Conformational changes to the secondary structures during coacervation were also studied by Raman spectroscopy. Critical structure-forming events associated with the formation of soluble (pH 5.00) and insoluble (pH 2.98) complexes were found for a 1:1 PPI–AL mixture, with optimal biopolymer interactions occurring at pH 2.10 (pH_opt). As mixing ratios increased between 4:1 and 8:1, critical pHs shifted towards higher pH. Maximum coacervate formation at pH_opt occurred at a mixing ratio of 4:1. Electrophoretic mobility measurements showed a shift in net neutrality from pH 4.00 in homogenous PPI solutions, to pH 1.55 for the 1:1 mixture. As biopolymer ratios increased towards 8:1 PPI:AL, net neutrality shifted to higher pHs (～3.80). Raman spectroscopy revealed minimal complexation-induced conformational changes. Findings could aid in the design of pH-sensitive biopolymer carriers for use in functional food and bio-material applications.     

Pea (<Emphasis Type="Italic">Pisum sativum,L.</Emphasis>) Protein Isolate Stabilized Emulsions: A Novel System for Microencapsulation of Lipophilic Ingredients by Spray Drying

Oil-in-water emulsions can be considered as an important delivery system for lipophilic food molecules. In this study, pea protein isolate (PPI) was studied for its emulsifying capacity at various pH values and pH 7 was selected to prepare emulsions for the production of dry microcapsules. Emulsions stabilized by PPI just enough to cover oil droplets were mixed with solutions of starch hydrolysates of various dextrose equivalent (DE) and subsequently spray dried to yield powders with 30 wt% oil. Effects of DE (6, 12, 19, and 28) on feed emulsion properties and on the characteristics of the spray-dried powders were examined. Reconstituted emulsion oil droplet size and stability were affected by DE in all cases. Microencapsulation efficiency of dried emulsions increased significantly with increasing DE. The scanning electron microscope results showed that lower maltodextrins DE microcapsules are shallow and presented rough surfaces or invaginations. However, higher carbohydrates DE microcapsules were circular and uniform showing minimum cracks and dents on the surface confirming these DE to be efficient encapsulating materials. The formation of the drying matrix seems control the destabilization of pea protein-coated oil droplets during spray drying. In systems where the matrix is formed in a uniform manner, the interfacial protein film is less affected by the drying process. Thus the functionalities of pea protein can be protected during drying by using high DE carbohydrates.     

Physicochemical and emulsifying properties of protein extracted from soybean meal assisted by steam flash-explosion

The conventional alkaline aqueous extraction is not effective in promoting maximum protein yield from soybean meal (SBM). In this study, the steam flash-explosion (SFE) treatment was firstly employed to significantly improve the protein yield, while the protein content of soy protein isolate (SPI) decreased, concomitant with increase in carbon content of SPI. The SFE treatment led to the dissociation of insoluble protein aggregates in SBM, with subsequent increase of soluble protein aggregates formed via on-disulfide covalent bonds. The covalent coupling of the carbohydrate to the protein during SFE treatment can contribute to the dissolubility of protein and the formation of protein aggregates. After SFE treatment, surface hydrophobicity of SPI was decreased, however the emulsifying properties were improved. The emulsifying activity index and emulsifying stability index were improved to 41.94 m²/g and 35.27 min under 1.3 MPa, 180 s treatment condition. It indicated that compared to surface hydrophobicity, changes of other aspects of protein structure including the covalent coupling of carbohydrate to protein were the predominant factors that ruled the emulsifying property of protein.Industrial relevanceThe steam flash-explosion treatment (SFE) is an eco-friendly, low-energy and non-traditional technology, which could be performed on a large scale for the industry. The SFE treatment can effectively change the physicochemical properties of protein resulting in significant increase of protein yield and improvement in emulsifying properties of protein. After SFE treatment, the protein from heat-denatured soybean meal can be refunctionalized for application in food industry.     

响应面优化转谷氨酰胺酶改性花生分离蛋白工艺的研究

为了改善花生分离蛋白的凝胶特性,研究了利用转谷氨酰胺酶交联改性花生分离蛋白的工艺。在进行了酶添加量、花生分离蛋白浓度和酶作用时间单因素试验基础上,利用响应面试验设计优化了酶交联改性的最佳条件。并分别测定了酶改性前后花生分离蛋白的功能性,包括:溶解性、吸油性、持水性、乳化性和乳化稳定性、起泡性和起泡稳定性。通过响应面分析得到酶改性的最佳条件:酶添加量、花生分离蛋白质量浓度和酶作用时间分别为17.75 U/g、29.60 g/mL和376 min,在此条件下,凝胶的硬度可达到333.49 g。经转谷氨酰胺酶改性后,花生分离蛋白的吸油性和持水性均有不同程度的提高,分别提高了27.41%和61.24%。