Effect of pH and Ionic Strength on the Physicochemical Properties of Coconut Milk Emulsions

ABSTRACT:  Coconut milk (16% to 17% fat, 1.8% to 2% protein) was extracted from coconut ( Cocos nucifera L.) endosperm and diluted in buffer to produce natural oil-in-water emulsions (10 wt% oil). The effect of pH (3 to 7) and NaCl (0 to 200 mM) on the properties and stability, namely, mean particle size, ζ-potential, viscosity, microstructure, and creaming stability, of the natural coconut milk emulsions was investigated. At pH values close to the isoelectric point (IEP) of the coconut proteins (pH 3.5 to 4) and in the absence of NaCl, coconut milk flocculated, but did not coalesce. Flocculation corresponded to low surface charges and was accompanied by an increase in emulsion viscosity. Adding up to 200 mM NaCl to those flocculated emulsions did not change the apparent degree of flocculation. Coconut milk emulsion at pH 6 was negatively charged and not flocculated. Upon addition of salt, the ζ-potential decreased from –16 to –6 mV (at 200 mM NaCl) but this was not sufficient to induce flocculation in coconut milk emulsions. At low pH (< IEP), the positively charged droplets of coconut milk emulsions only flocculated when the NaCl concentration exceeded 50 mM, as the ζ-potential approached zero.     

Effects of pH and Ethanol on the Kinetics of Destabilisation of Oil-in-Water Emulsions Containing Milk Proteins

Soya oil-in-water emulsions (1: 4, v/v) were prepared using sodium caseinate or β-lactoglobulin (5 or 10 g litre⁻¹) as the surfactant. The kinetics of aggregation induced by pH changes or the addition of ethanol were measured by light scattering in diluted systems either under shear or quiescent conditions. Under shear, emulsions containing caseinate were stable between pH 3 and 3·5 and also at pH⩾5·3, while those formed with β-lactoglobulin were stable below pH 4 as well as at pH⩾5·6. Under quiescent conditions, the emulsions were also destabilised but at a much slower rate. The destabilisation process generally showed an initial lag period which depended on the pH, followed by an explosive growth stage. In aqueous ethanol (50: 50, v/v), under both shear and quiescent conditions, fresh emulsions formed with β-lactoglobulin were only slightly destabilised. Ageing the emulsions for 24 h, however, increased their susceptibility, and destabilisation was achieved at concentrations of ethanol as low as 30: 70, (v/v). Emulsions formed with caseinate on the other hand were destabilised at ethanol concentrations ⩾40: 60 (v/v), with time-courses showing a high initial slope, followed by a final stage at which particle size remained constant. Shear had a relatively small effect on these reactions. The kinetics of pH-induced aggregation in both sets of emulsions could be explained by orthokinetic flocculation while the ethanol-induced association in caseinate emulsions appeared to be a result of Ostwald ripening.     

Formation and Coalescence Stability of Emulsions Stabilized by Different Milk Proteins

The volume fraction of oil emulsified, surface area, droplet diameter, and coalescence rates of emulsions stabilized by different milk proteins were studied at protein concentrations of 0.25, 0.5, 1.0, and 2.0% (w/w); pH 4, 5, and 7; and ionic strengths 0.1 and 0.2. The emulsion activity index (EAI) and coalescence stability generally increased with increasing protein solubility and hydrophobicity. The volume fraction of oil emulsified decreased with increasing ionic strength. Coalescence stability correlated with droplet diameter for emulsions stabilized by α-lactalbumin, β-lactoglobulin, and sodium caseinate (r²=0.96). With the exception of β-lactoglobulin-stabilized emulsions, coalescence stability was largely unaffected by pH.     

Effect of Heating and Homogenization on the Stability of Coconut Milk Emulsions

: The effects of homogenization and heat treatment on the colloidal stability of coconut milk were studied. Fresh coconut milk (15% to 17% fat, 1.5% to 2% protein) was extracted and stored at 30 °C before homogenization at 40/4 MPa (stage I/stage II). Both homogenized and non‐homogenized samples were heated at 50 °C, 60 °C, 70 °C, 80 °C, and 90 °C for 1 h. Homogenization reduced the size of the primary emulsion droplets from 10.9 to 3.0 μm, but increased the degree of flocculation, presumably via a bridging mechanism. This flocculation was also responsible for increased viscosity of the homogenized samples. Heating increased the degree of flocculation in both non‐homogenized and homogenized samples. A slight amount of coalescence was also observed after heating above 80 °C. All samples creamed after 24 h of storage, but the heated samples formed a larger cream layer, presumably because the flocculated droplets packed together less efficiently. Optical microscopy was used to confirm the combination of flocculation and creaming responsible for changes in coconut milk quality. The information obtained from this study provides a better understanding of the emulsion science important in controlling coconut milk functionality.     

大豆分离蛋白与卵磷脂间相互作用对O/W型乳状液稳定性的影响

研究大豆分离蛋白与卵磷脂的复合比例及相互作用对乳化体系稳定性及功能性质的影响。结果显示:乳状液的乳化活性和粒径分布等性质受大豆分离蛋白与卵磷脂比例分配的影响较大。当大豆分离蛋白与卵磷脂间的质量比为10∶1时,复合体系的乳化活性较高(98.1 m~2/g),同时乳液的体积平均直径D_(4,3)最小(13.34μm),乳液双峰分布程度较低。乳化稳定性和ζ-电位测试结果显示,复合体系中大豆分离蛋白与卵磷脂比例为1∶1或100∶1都不利于体系稳定,此时激光共聚焦显微镜观测乳液出现相分离和不规则非球形液滴。这说明大豆分离蛋白与卵磷脂作为复合乳化剂具有最适配比,在该比例下大豆分离蛋白与卵磷脂间的相互作用对食品级水包油(oil-in-water,O/W)乳状液的稳定性是有利的。     

超声处理大豆分离蛋白与壳聚糖复合物对O/W型乳液稳定性的影响

为探究超声处理大豆分离蛋白-壳聚糖（soybean protein isolate-chitosan,SPI-CS）复合物对形成O/W型乳 液性质的影响,主要研究了复合物表面疏水性、乳化活性、乳化稳定性与油-水界面张力、乳液粒径、乳液稳定性 之间的关系。结果表明：未经超声处理的SPI-CS复合物表面疏水性、乳化活性、乳化稳定性和界面吸附性较低,形 成的O/W型乳液粒径相对较大,约100 μm,乳液Zeta电位较低,乳滴有发生聚集的倾向。乳液贮存7 d后乳层析指数 最高。经超声处理后SPI-CS复合物形成的乳状液性质发生明显变化,随着超声功率的增加,形成的O/W型乳液的稳 定性有所增加：超声功率为400 W时SPI-CS复合物形成的乳液最为稳定,乳层析指数最低;当超声功率超过400 W 时,乳液的光学显微镜观察显示其粒径有所增大,同时乳液的Zeta电位、乳化活性和乳化稳定性明显下降,界面张 力降低缓慢。超声处理暴露了蛋白质分子的内部结构,使部分结构展开、柔性增加,促进了其与壳聚糖之间的静电 相互作用,说明超声处理的大豆分离蛋白与壳聚糖形成的复合物影响了O/W型乳液的稳定性及相关性质。     

不同蛋白稳定乳液的冻融稳定性

本文以1%m/V浓度的大豆分离蛋白和乳清浓缩蛋白为材料,对蛋白热处理形成颗粒后制备油分数为0.4的水包油型Pickering乳液,未加热处理的蛋白和酪蛋白酸钠稳定乳液作为对照。将不同蛋白稳定的乳液在-20℃冷冻24 h随后在30℃恒温箱解冻3 h,如此冷冻-解冻处理循环三次,探讨未加热处理的活性蛋白和热诱导形成的蛋白颗粒稳定乳液的冻融稳定性,包括新鲜制备和每次冻融之后乳液的乳滴粒径分布、聚结和絮凝程度、乳液分层和脂肪上浮情况、以及乳液的光学显微结构。结果表明冷冻乳液融化时不可避免的被部分破坏,而大豆分离蛋白热诱导聚集颗粒稳定的Pickering乳液具有优良的冻融稳定性,这可能为一些水包油乳液型冷冻食品、热敏性生物活性物质和低温储存药品的制备和研发提供一条有效的技术途径。     

The Emulsifying Properties of Commercial Milk Protein Products in Simple Oil-in-Water Emulsions and in a Model Food System

ABSTRACT: The emulsifying properties of six commercial milk protein products were studied. The products were separated into one of two groups depending on whether they contained aggregated (micellar) casein or disordered protein (casein or whey protein). Disordered proteins had a greater emulsifying ability than aggregated proteins. Dispersion of aggregated protein in dissociating buffer improved the emulsifying ability. Comparison of emulsion properties in simple oil-in-water emulsions with those in a model coffee whitener formulation showed that the lower emulsifying ability of aggregated protein could be partially compensated by other ingredients.     

Effect of pH and Ionic Strength on the Heat Stability of Rapeseed 12S Globulin (Cruciferin) by the ANS Fluorescence Method

The heat stability of rapeseed 12S globulin (cruciferin) was examined using 8-anilinonaphthalene-1-sulphonic acid (ANS) as a fluorescence probe. Heating cruciferin (0·06–0·3 mg ml⁻¹ in 10 mM glycyl–glycyl piperizine buffer, pH 7·0, with 0·1–1·0 M NaCl) for 20 min increased its hydrophobicity as monitored by ANS fluorescence measurements. The mid-point temperature for the heat effect (T_m) increased linearly with increasing solvent pH (T_m (°C)=4·16 pH+41 (μ=0.1)) or sodium chloride concentration (T_m (°C)=14·7 [NaCl]+71 (pH=7·0)). The range of T_m values for cruciferin was 45–96°C. At 20°C cruciferin was unstable at pH<3·0 but relatively stable under alkaline conditions (pH 8–10). Though possessing an oligomeric structure, cruciferin appears to heat denature in accordance with the two-stage deactivation model for simple globular proteins.     

Microstructure and Stability of Non-Protein Stabilized Oil-in-Water Food Emulsions Measured by Optical Methods

ABSTRACT: :
The microstructure and stability of oil-in-water emulsions, stabilized with non-protein emulsifiers (sor-bitan esters), were analyzed as a function of emulsification time, rotor speed, hydrophilic-lipophilic balance (HLB), and ionic strength. Sauter average dia (D[3,2]) were determined from micrographs. Back-scattered light data were analyzed and a method to determine creaming rates of the systems was proposed. Creaming rates showed that the relationship between emulsion stability and HLB was non-linear. Addition of NaCl raised creaming rates, resulting in decreased stability, while micrographs showed the presence of flocs. Results were discussed taking account of interactions present in the system.     

Comparison of the Emulsifying Properties of Fish Gelatin and Commercial Milk Proteins

ABSTRACT: We have compared the flocculation, coalescence, and creaming properties of oil-in-water emulsions prepared with fish gelatin as sole emulsifying agent with those of emulsions prepared with sodium caseinate and whey protein. Two milk protein samples were selected from 9 commercial protein samples screened in a preliminary study. Emulsions of 20 vol% n -tetradecane or triglyceride oil were made at pH 6.8 and at different protein/oil ratios. Changes in droplet-size distribution were determined after storage and centrifugation and after treatment with excess surfactant. We have demonstrated the superior emulsifying properties of sodium caseinate, the susceptibility of whey protein emulsions to increasing flocculation on storage, and the coalescence of gelatin emulsions following centrifugation.     

Rheology and Oxidative Stability of Whey Protein Isolate-Stabilized Menhaden Oil-in-Water Emulsions as a Function of Heat Treatment

ABSTRACT:  Menhaden oil-in-water emulsions (20%, v/v) were stabilized by 2 wt% whey protein isolate (WPI) with 0.2 wt% xanthan gum (XG) in the presence of 10 mM CaCl₂ and 200 μM EDTA at pH 7. Droplet size, lipid oxidation, and rheological properties of the emulsions were investigated as a function of heating temperature and time. During heating, droplet size reached a maximum at 70 °C and then decreased at 90 °C, which can be attributed to both heating effect on increased hydrophobic attractions and the influence of CaCl₂ on decreased electrostatic repulsions. Combination of effects of EDTA and heat treatment contributed to oxidative stability of the heated emulsions. The rheological data indicate that the WPI/XG-stabilized emulsions undergo a state transition from being viscous like to an elastic like upon substantial thermal treatment. Heating below 70 °C or for less than 10 min at 70 °C favors droplet aggregation while heating at 90 °C or for 15 min or longer at 70 °C facilitates WPI adsorption and rearrangement. WPI adsorption leads to the formation of protein network around the droplet surface, which promotes oxidative stability of menhaden oil. Heating also aggravates thermodynamic incompatibility between XG and WPI, which contributes to droplet aggregation and the accumulation of more WPI around the droplet surfaces as well.     

大豆分离蛋白乳状液稳定性的几种分析方法比较

用不同质量分数(0.5%、1%、2%、3%)的大豆分离蛋白(SPI)和大豆油制备3%O/W型乳状液,比较不同离心力作用下和添加不同量SPI乳状液稳定性的差异以及添加不同量SPI乳状液黏度的差异,考察贮存期延长过程中的浊度法测定乳状液稳定性以及乳状液粒径和Zeta电位的变化,结合外观和微观观察,寻找一种快速准确测定乳状液稳定性的方法。结果表明:离心法、贮存期浊度法与乳状液外观观察的结论一致,都表明添加3%SPI的乳状液最稳定,并且SPI添加量越高,乳状液黏度越大,稳定性越好。储存期乳状液平均粒径和Zeta电位发生变化,但难以作为乳状液稳定性的判断标准。本实验进一步验证,离心法能够快速、准确地预测乳状液的稳定性,适于产品开发和成品检验的需要。     

包封姜黄素的果胶-核桃蛋白复合物乳液稳定性及体外消化

研究旨在开发核桃蛋白和果胶之间的新型复合物,作为姜黄素的递送系统.将姜黄素成功包封在由果胶-核桃蛋白组成的复合物乳液中.贮存14d后,包封姜黄素的果胶-核桃蛋白复合物乳液粒径(D4.3)略有增加,并未发生相分离.在环境压力下,包封姜黄素的核桃清蛋白复合物乳液对NaC1处理(高达300 mmol/L)和热处理(高达90℃...     

木犀草素-乳清蛋白复合物对乳液物理稳定性和氧化稳定性的影响

以乳清蛋白为乳化剂,采用高压均质制备水包油乳液,分别在天然乳清蛋白组和热变性乳清蛋白组中添加 不同质量浓度（0.00、0.05、0.10、0.20、0.40 mg/mL）的木犀草素,探究天然和热变性乳清蛋白与木犀草素之间的 相互作用以及形成的乳清蛋白-木犀草素复合物与乳液稳定性的关系。通过测定荧光光谱、动态激光散射、界面物 质含量以及脂质氧化产物含量,研究热变性乳清蛋白与木犀草素复合物形成乳液的稳定性、界面吸附特性和抗氧化 性。结果表明：荧光光谱显示蛋白质和木犀草素相互作用发生荧光猝灭,二者之间形成了蛋白质-木犀草素基态复 合物;该复合物能显著抑制乳液脂质的氢过氧化物和丙二醛的形成（P＜0.05）,可增强乳液的氧化稳定性,但是 对乳液的物理稳定性无显著影响（P＞0.05）。热处理不利于蛋白质在界面的吸附,但可以提高木犀草素在乳液界 面的吸附;而木犀草素的质量浓度对界面蛋白质的吸附没有显著影响（P＞0.05）。     

酶法改性磷脂对大豆蛋白共建体系乳化稳定性及氧化稳定性的影响

为探究磷脂酶解物-大豆分离蛋白复合乳化体系稳定性及氧化稳定性的机理,研究了不同酶解时间对乳液乳化性质、贮存稳定性和氧化稳定性等特性的影响,通过核磁共振法对酶解后的磷脂产物组分进行分析,并对乳状液的乳化活性、乳化稳定性、粒径分布、Zeta电位、乳层析指数、氢过氧化物值和硫代巴比妥酸反应物值进行测定。结果发现：随着酶解时间的延长,磷脂经4 h酶解后主要产物为溶血磷脂,其与大豆蛋白共建乳化体系后,乳化稳定性、贮存稳定性及氧化稳定性均优于对照组,酶解6 h左右酰基转移现象加剧,产生的溶血磷脂会继续被酶解生成甘油磷脂酰胆碱,导致稳定性略有下降;添加一定酶解时间的磷脂酶解产物,会促进乳化体系通过相互作用在水油界面上形成较稳定的界面膜,可以提高乳液的稳定性及氧化稳定性。     

崂山奶山羊乳的热稳定性影响因素研究

本文以崂山奶山羊乳为研究对象,对山羊乳的一般理化性质进行分析,并重点探讨了山羊乳的热稳定性。采用热凝固时间法(HCT)测定不同泌乳期、温度、pH值及相关助剂对山羊乳热稳定性的影响。结果表明,山羊乳的pH接近中性、酸度为11~23°T,且与泌乳期呈正相关关系。羊乳的稳定性随泌乳期的延长而增强,随加热温度的升高而急剧减弱。pH对羊乳的热稳定性影响较大,pH越大,HCT值越大,当待测乳样的pH值超过6.5时,乳样不再发生沉淀。在pH=6.0、140℃加热条件下,加入适量浓度为0.01~0.20mol/L的柠檬酸盐、磷酸盐、EDTA均可改善羊乳的稳定性,且添加物浓度越大,改善效果越好。添加钙离子亦可改变羊乳的热稳定性,其稳定性随钙离子浓度的升高而降低。羊乳热稳定性随蔗糖浓度的增大呈现出先升高后降低的趋势,添加浓度为35%的蔗糖时,待测羊乳的HCT值最高,羊乳的热稳定性最好。     

Perception of Taste and Viscosity of Oil-in-Water and Water-in-Oil Emulsions

A trained panel performed sensory assessments of intensity of taste and viscosity of 50% oil-in-water and water-in-oil emulsions prepared with varied concentrations of sucrose, NaCl, or citric acid. No main effects of emulsion type occurred for taste intensity or slope of the tastant concentration – intensity relationships. NaCl and citric acid increased perceived viscosity of both emulsion types, and these effects were most pronounced in oil-in-water emulsions. The results are hypothesized as related to functions of saliva and breakdown of emulsion structure in the mouth.     

黄原胶体系的流变性及糖和盐对体系的影响

报道了对黄原胶水溶液以及以黄原胶水溶液为水相的２０％（Ｏ／Ｗ体积分数）乳状液在３０℃的流变学性质的研究。实验中通过振荡和蠕变测试考察了从０．０５％～０．５％系列质量分数的黄原胶溶液和乳状液的流变学性质以及０．５ｍｏｌ／ＬＮａＣｌ和质量分数１０％的蔗糖对这些体系的影响。发现，随着黄原胶质量分数的增加，体系逐渐表现固态的反应，这表明大分子交联或其它方式的缔合逐渐提高了体系结构化的程度。蔗糖的存在在一定程度上增强了大分子的这种功能作用，而ＮａＣｌ的引入则明显降低了大分子的这种影响，并且ＮａＣｌ的这种影响对黄原胶质量分数较高的体系更加明显。乳状液体系的测定结果与水相的情况一致。