Interfacial and emulsifying properties of lentil protein isolate

The dynamic interfacial tension (DIFT) at oil–water interface, diffusion coefficients, surface hydrophobicity, zeta potential and emulsifying properties, including emulsion activity index (EAI), emulsion stability index (ESI) and droplet size of lentil protein isolate (LPI), were measured at different pH and LPI concentration, in order to elucidate its emulsifying behaviour. Sodium caseinate (NaCas), whey protein isolate (WPI), bovine serum albumin (BSA) and lysozyme (Lys) were used as benchmark proteins and their emulsifying property was compared with that of LPI. The speed of diffusion-controlled migration of these proteins to the oil/water interface, was in the following order: NaCas > LPI > WPI > BSA > Lys, while their surface hydrophobicity was in the following order: BSA > LPI > NaCas > WPI > Lys. The EAI of emulsions stabilised by the above proteins ranged from 90.3 to 123.3 m²/g and it was 93.3 ± 0.2 m²/g in LPI-stabilised emulsion. However, the stability of LPI-stabilised emulsions was slightly lower compared to that of WPI and NaCas-stabilised emulsions at the same protein concentration at pH 7.0. The ESI of LPI emulsions improved substantially with decrease in droplet size when protein concentration was increased (20–30 mg/ml). Reduction of disulphide bonds enhanced both the EAI and ESI compared to untreated samples. Heat treatment of LPI dispersions resulted in poor emulsion stability due to molecular aggregation. The stability of LPI-stabilised emulsions was found to decrease in the presence of NaCl. This study showed that LPI can be as effective emulsifiers of oil-in-water emulsions as are WPI and NaCas at ?20 mg/ml concentrations both at low and neutral pH. The emulsifying property of LPI can be improved by reducing the intra and inter-disulphide bond by using appropriate reducing agents.     

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。     

Effects of high hydrostatic pressure on the physicochemical and emulsifying properties of sweet potato protein

The influence of high hydrostatic pressure (HHP) treatment on the physicochemical and emulsifying properties of sweet potato protein (SPP) at various concentrations, e.g. 2%, 4% and 6% (w/v, SPP‐2, SPP‐4 and SPP‐6), was investigated. Significant differences in hydrophobicity, enthalpy of denaturation and solubility were observed (P < 0.05). Emulsifying activity indexes (EAI) of SPP‐2 and SPP‐6 increased at 400 MPa, whereas EAI of all SPP significantly decreased at 600 MPa (P < 0.05). Emulsion stability (ESI) was significantly decreased for SPP‐2 and SPP‐6, while increase in ESI was observed for SPP‐4 above 200 MPa (P < 0.05). SPP‐2 emulsions showed sharp decrease in apparent viscosity with pressure increase, while pseudo plastic flow behaviour was not changed for all of emulsions. Sporamins A and B were well‐adsorbed in pressurised emulsion without displacement. These results suggest that HHP treatment could be used to modify the physicochemical and emulsifying properties of SPP.     

不同黏度多糖阿拉伯胶和瓜尔胶对肌原纤维蛋白乳化性质的影响

选取两种分子质量相近、黏度相差较大的天然高分子多糖阿拉伯胶（arabic gum,AG）和瓜尔胶（guar gum,GG）分别与肌原纤维蛋白（myofibrillarprotein,MP）进行复合,研究不同多糖添加量（0.1%～0.5%）对MP-多糖复合物乳液性质的影响规律。结果表明,AG和GG均可以显著改善MP的乳化性质,其中AG对乳化活性的改善效果较好,而GG更有利于乳液的稳定性。随着多糖质量分数增加,乳化活性指数和稳定性指数均呈先升高后降低趋势,AG和GG添加量分别为0.3%和0.2%时,乳化活性指数和稳定性指数达到最大值。界面蛋白含量测定结果显示,AG和GG均会导致界面蛋白含量下降,尤其是GG的作用更明显。随着AG和GG添加量增加,乳液粒径逐渐减小,且尺寸分布更加均一,添加量超过0.3%后,GG组乳液出现少量絮凝现象。同一添加量下,GG组乳液粒径明显小于AG组。流变学分析证实,所有乳液均为假塑性流体,表现出弱凝胶性质。AG添加量较少（≤0.3%）时会降低乳液黏度,并明显提高乳液的储能模量,而GG的添加使乳液表观黏度和储能模量均显著提高,与AG相比,高黏度GG制备的乳液拥有更高的...     

Manipulating interfacial behaviour and emulsifying properties of myofibrillar proteins by L-Arginine at low and high salt concentration

The present work examined the impact of L-Arginine (Arg) on the emulsifying properties, interfacial behaviour and conformational characteristics of myofibrillar proteins (MPs) at high (0.6 m ) and low (0.15 m ) salt concentration to maintain good emulsifying properties of MPs at low salt concentration. The data indicated that Arg increased the emulsifying activity index/emulsion stability index (EAI/ESI) and decreased the CI and droplet size of emulsions regardless of salt concentration. Raman spectra revealed that the α-helix content decreased from 60.30% to 51.26% at high salt concentration, and from 60.20% to 54.82% at low salt concentration in the presence of Arg. In addition, MPs treated with Arg exhibited a higher interfacial pressure and more rapidly diffusion to the oil surface. Meanwhile, Arg increased the interfacial protein loading. The results demonstrated that Arg caused the unfolding of MPs, promoting the adsorption of proteins and decreasing the interfacial tension, ultimately improving the stability of emulsions at low salt concentration.     

Effects of protein concentration and oil-phase volume fraction on the stability and rheology of menhaden oil-in-water emulsions stabilized by whey protein isolate with xanthan gum

The influences of protein concentration (0.2, 1, 2 wt%) and oil-phase volume fraction (5%, 20%, 40% v/v) on emulsion stability and rheological properties were investigated in whey protein isolate (WPI)-stabilized oil-in-water emulsions containing 0.2 wt% xanthan gum (XG). The data of droplet size, surface charge, creaming index, oxidative stability, and emulsion rheology were obtained. The results showed that increasing WPI concentration significantly affected droplet size, surface charge, and oxidative stability, but had little effect on creaming stability and emulsion rheology. At 0.2 wt% WPI, increasing oil-phase volume fraction greatly increased droplet size but no significant effect on surface charge. At 1 or 2 wt% WPI, increasing oil-phase volume fraction had less influence on droplet size but led to surface charge more negative. Increasing oil-phase volume fraction facilitated the inhibition of lipid oxidation. Meanwhile, oil-phase volume fraction played a dominant role in creaming stability and emulsion viscosity. The rheological data indicated the emulsions may undergo a behavior transition from an entropic polymer gel to an enthalpic particle gel when oil-phase volume fraction increased from 20% to 40% v/v.     

Emulsifying properties of pea protein/guar gum conjugates and mayonnaise application

Modified plant protein may be used as a healthy and more functional emulsifier in food products. The objective of this study was to evaluate the emulsifying properties of functionally enhanced pea protein (i.e. pea protein conjugated with guar gum, G-PPI) and its potential application to mayonnaise, compared with unmodified pea protein. Emulsions containing G-PPI were prepared at different pH, salt concentrations, protein concentrations and oil/water ratios. Mayonnaise samples were prepared using the pea proteins or egg yolk powder. Various characteristics of the emulsions, including droplet size, apparent viscosity, viscoelasticity and microstructure, were analysed. The emulsions with G-PPI had significantly increased stability of up to 89.4% and apparent viscosity of up to 48.62 mPa.s. The G-PPI emulsion had a smaller average droplet size of 934.4 nm at pH 7 compared with the PPI emulsion (stability 62.7%, apparent viscosity 22.8 mPa.s and droplet size 1664.8 nm). The pH, NaCl concentration, protein concentration and oil/water ratio greatly affected the emulsifying properties. The G-PPI mayonnaise at higher protein concentrations (6 or 8%) exhibited excellent emulsifying and rheological properties. The modified pea protein through the green modification process with natural polysaccharides could be used as a safe and functional emulsifier in different emulsified foods.     

The amino acid composition,solubility and emulsifying properties of sweet potato protein

A protein was purified from the high-protein type sweet potato variety 55-2 available in China. The amino acid composition, solubility and emulsifying properties of the sweet potato protein (SPP) were studied. The SPP was rich in aspartic acid (18.5%) and glutamic acid (9.30%) while essential acid amino acids made up approximately 40.7% of the SPP. The SPP was highly soluble in distilled water over a wide range of pH. However, solubility of the SPP in 1.0 M NaCl and 1.0 M CaCl₂ solutions was low especially at pH below the pI of the SPP. The SPP in CaCl₂ demonstrated emulsifying activity index (EAI) and emulsion stability index (ESI) many folds higher than those in distilled water and NaCl solution (P < 0.05).     

The effect of chitosan on the properties of emulsions stabilized by whey proteins

The influence of the cationic amino polysaccharide chitosan content (0–0.5%) on particle size distribution, creaming stability, apparent viscosity, and microstructure of oil-in-water emulsions (40% of rapeseed oil) containing whey protein isolate (WPI) (4%) at pH 3 was investigated. The emulsifying properties, apparent viscosity and phase separation behaviour of aqueous WPI/chitosan mixture at pH 3 were also studied. The interface tension data showed that WPI/chitosan mixture had a slightly higher emulsifying activity than had whey protein alone. An increase in chitosan content resulted in a decreased average particle size, higher viscosity and increased creaming stability of emulsions. The microstructure analysis indicated that increasing concentration of chitosan resulted in the formation of a flocculated droplet network. This behaviour of acidic model emulsions containing WPI and chitosan was explained by a flocculation phenomenon.     

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.