提高大豆蛋白冻融后乳化性改性工艺优化

为了制备出经冷冻-融化后仍能保持较高乳化性的大豆蛋白,试验以葡聚糖为糖基化供体,采用湿法糖基化技术改性大豆蛋白。根据单因素试验的结果,建立了Box-Behnken模型对加工工艺进行优化,所得的模型拟合度高,切实可行,可用于实际分析和预测。利用响应面分析法探讨了蛋白浓度、蛋白与糖质量比、反应时间3因素对改性产物冻融前后乳化活性和乳化稳定性的影响,优化的工艺条件为:大豆分离蛋白(soybean protein isolate,SPI)质量浓度40 mg/mL,SPI与葡聚糖的质量比为1∶3,反应时间4 h。在此条件下得到的改性产物冻融稳定性显著(P0.05)高于未改性蛋白,冻融前后的乳化活性(emulsifying activity index,EAI)分别是空白对照样的1.687和1.780倍,乳化稳定性(emulsion stability index,ESI)分别是空白对照样的1.367和1.274倍。傅里叶红外光谱证明葡聚糖通过共价键接到大豆蛋白分子中,研究结果为制备冷冻食品加工专用大豆蛋白的产业化生产提供参考。     

葡聚糖分子量对玉米醇溶蛋白接枝物结构和乳化性的影

为了探究葡聚糖接枝作用对玉米醇溶蛋白结构和乳化性的影响,明确蛋白质结构与功能性的关系,本研究以玉米醇溶蛋白(Zein)和不同分子量(6、20、40和70 k Da)葡聚糖(dextran,DX)为原料,采用湿热法制备Zein-DX接枝物,并对接枝物的结构和乳化性进行研究。结果表明,低分子量(6 k Da)DX具有更高的反应活性,赖氨酸和精氨酸是参与Zein与DX接枝反应的主要氨基酸。傅里叶红外光谱(fourier transform infrared,FTIR)证明了DX以共价键与Zein形成了复合物。DX的共价接枝能够导致Zein荧光猝灭的发生,降低Zein的热稳定性,改善Zein的乳化活性(emulsifying activity index,EAI)和乳化稳定性(emulsifying stability index,ESI)。低分子量(6 k Da)DX与Zein形成的接枝物最大发射波长发生显著红移,三级结构变的松散,具有更低的热稳定性,且EAI最高达到(23.28±0.71)m2/g。然而,高分子量(70 k Da)DX与Zein形成的接枝物ESI高达(26.44±0.47)min,高于其他Zein-DX接枝物样品。乳状液粒径和流变性分析表明,随着DX分子量的增加,乳状液粒径降低,黏度增加,这与ESI的研究结果相符。研究结果可为改善玉米蛋白功能性和深入了解玉米蛋白改性机制提供理论依据。     

α和α'亚基缺失对大豆分离蛋白乳化特性的影响

为了探究β-伴大豆球蛋白(7S)中α和α′亚基缺失对大豆分离蛋白乳化特性的影响,该文以东农47(对照)和3种不同蛋白亚基缺失型(α缺失、α′缺失以及α、α′缺失)大豆为原料提取大豆分离蛋白(SoyProteinIsolate,SPI),通过十二烷基磺酸钠聚丙烯酰胺凝胶电泳(Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis,SDS-PAGE)技术分析其亚基组成,然后制备乳状液并测定乳化活性指数(Emulsifying Activity Index,EAI)、ζ-电位、粒径、微观结构、稳定动力学指数(Turbiscan Stability Index,TSI)及界面蛋白吸附量。结果表明:α′亚基缺失型SPI乳状液乳化活性指数最大,为87.59 m2/g;ζ-电位绝对值最大,为47.7 mV;粒径最小,为2.223μm;显微结构显示其分子最小且分布最均匀,稳定动力学指数最小;界面蛋白吸附量最大,为31.40%。4种不同SPI乳状液的稳定性结果由大到小为α′亚基缺失型、东农47、α亚基缺失型、α和α′亚基缺失型。研究结果可为高乳化性大豆蛋白系列产品的开发应用提供理论支撑和技术支持。     

适宜物理-酶联合改性提高酸性条件下大豆分离蛋白乳化性

为提高酸性条件下大豆分离蛋白（soy protein isolates,SPI）的乳化性能,该文研究了物理-酶联合改性对SPI（pH值为4）的乳化性能影响,通过对比确定了物理-酶联合改性,即超声波-酶复合改性和挤压膨化-酶复合改性两种改性方法在酸性条件下的乳化性能效果最好;并通过对改性后 SPI（pH 值为4）进行溶解性、游离巯基、二硫键、粒径、扫描电镜（scanning electron microscope,SEM）和激光共焦扫描显微镜（confocal laser scanning microscopy,CLSM）分析,从蛋白结构变化上进一步揭示了乳化性能提高现象的原因。结果表明：超声波联合植酸酶-酸性蛋白酶改性的 SPI （Uphy-aci-SPI）的乳化活性（emulsifying activity index,EAI）为0.53 m2/g,比未改性SPI（0.18 m2/g）显著提高了196%（P<0.05）,乳化稳定性（emulsifying stability index,ESI）为17 min,比未改性SPI（13.5 min）显著提高了25.9%（P<0.05）;挤压膨化联合菠萝蛋白酶改性的SPI（Ebro-SPI）的EAI为0.46 m2/g,比未改性SPI显著增加了155%（P<0.05）,ESI为17 min,比未改性SPI显著增加了25.9%（P<0.05）。在pH值为4的条件下对物理-酶联合改性的SPI的性质分析发现,物理-酶联合改性的SPI与未改性SPI相比,物理-酶联合改性的SPI的溶解性显著增加（P<0.05）;物理-酶联合改性的SPI的乳状液平均粒径减小,CLSM观察乳状液中油与蛋白溶液稳定共融,改善了油滴之间的空间排斥力。物理-酶联合改性的SPI游离巯基的含量显著增加（P<0.05）,二硫键含量显著降低（P<0.05）。SEM观察物理-酶联合改性的SPI为结构松散、破碎均一的微观结构。由此可见,乳化性能的提高是通过深层改变蛋白的结构来实现的。该研究可为探索提高酸性条件下SPI的乳化性能的方法提供理论依据。     

低温等离子快速提高糖基化花生分离蛋白溶解性及乳化性

为进一步提高花生蛋白的溶解特性,扩大花生蛋白在食品工业中的应用。采用低温等离子(Non-Thermal Plasma,NTP)诱导花生分离蛋白-葡聚糖(Peanut Protein Isolate-Dextran,PPI-Dex)湿法糖基化反应,研究NTP在处理0、0.5、1.5、2.0、3.0 min的情况下,反应时间对花生分离蛋白与葡聚糖糖基化反应的影响。在低温等离子处理功率为70 W,反应液温度为60℃的状态下,随着NTP处理时间的延长,PPI-Dex的接枝度增加,在处理时间为1.5min时,PPI-Dex接枝度达最大为21.62%,与超声波接枝PPI-Dex需要40 min,传统湿接枝需要24 h相比,缩短了接枝时间。PPI-Dex接枝后,接枝物溶解度和乳液稳定性显著增强,与未接枝相比,溶解度提高了22.28%。通过测定其分子量、氨基酸含量、红外图谱及表面疏水性变化分析NTP处理对花生分离蛋白结构影响。分析结果表明,NTP处理1.5 min后,花生分离蛋白与葡聚糖发生糖基化反应形成偶联物,偶联物中羟基特征峰3 000～3 500 cm~(-1)及1 000～1 260 cm~(-1)的吸光度与未处理时相比增加,赖氨酸和苯丙氨酸相对含量显著降低(P0.05);同时,α-螺旋含量降低,β-折叠向β-转角转变,蛋白的有序结构被破坏,结构变松散,PPI构型向亲水型转变;接枝物的表面疏水性指数降低。花生分离蛋白与葡聚糖发生糖基化反应,反应位点可能为Lys和Phe。结果表明,低温等离子处理是一种快速促进蛋白与多糖接枝的有效方法。     

空化射流对大豆分离蛋白结构及乳化特性的影响

为了探究空化射流处理对大豆分离蛋白结构及乳化特性的影响。该研究将不同浓度(2%和5%)的大豆分离蛋白溶液在不同时间(2、4、6、8、10min)下进行空化射流处理,以未经处理大豆分离蛋白溶液作为对照,探究空化射流处理对大豆分离蛋白结构和乳化特性的影响。结果表明:适当时间的空化射流处理可以降低大豆分离蛋白的含硫氨基酸含量、溶液平均粒径和7S亚基、A亚基含量,引起蛋白乳液的ζ-电位绝对值和界面蛋白含量的升高和弹性模量出现增大的趋势,进而显著增强蛋白乳化活性和乳化稳定性,2%浓度下相比最低值提高248.94%和95.58%,5%浓度下相比最低值提高70.29%和101.83%,并且其改性处理的最佳时间受蛋白浓度所影响。这表明空化射流物理场可以通过改变大豆分离蛋白的结构和乳液界面特性调节其乳化活性,为大豆分离蛋白改性和空化射流物理场在食品领域的应用提供前期基础。     

挤压温度对大豆分离蛋白与原花青素复合物结构和功能特性的影响

为了探究不同挤压温度（40、60、80、100和120℃）对大豆分离蛋白（Soy Isolate Protein，SPI）与葡萄籽原花青素（Grape Seed Proanthocyanidin Extract，GSPE）复合物功能性质及结构特性的影响。该研究以溶解度、乳化性、乳化稳定性、ζ-电位、粒度为指标，利用荧光光谱、红外光谱分析该复合体系中大豆分离蛋白功能性质及结构的变化。结果表明：相较于挤压SPI，经过挤压处理的SPI-GSPE复合物的溶解度、乳化活性指数、乳化稳定性指数、ζ-电位绝对值及持水性均显著提高（P<0.05），其表面疏水性、持油性显著下降（P<0.05）。随着挤压温度的升高，SPI-GSPE复合物的溶解度、持油性及乳化活性均先增大后减小且在80℃达到最大值，而其表面疏水性先减小后增大且最小值在80℃，ζ-电位绝对值、乳化稳定性及持水性均随温度的升高而降低。粒径分析结果表明，挤压处理后SPI与GSPE形成了更加致密的复合物；荧光光谱及红外光谱结果表明，与GSPE的复合及挤压处理使SPI氨基酸残基所处微环境发生变化，蛋白结构发生变化。以上结果表明挤压温度为80℃时SPI-GSPE复合物功能性质提高幅度最大，为GSPE与SPI复合提高SPI的功能性质提供参考。     

微射流均质预处理提高大豆分离蛋白酶解效率及酶解产物乳化性能

为了探讨微射流均质预处理对大豆分离蛋白酶解效率及酶解产物乳化性能的影响,该文研究比较了微射流均质预处理前后大豆分离蛋白酶解产物的理化性质(水解度、亚基组成、蛋白溶解性、表面疏水性和分子量分布)和乳化性能(通过测定分析样品乳状液的平均粒径和微观结构评估样品的乳化性能)的变化。研究表明:大豆分离蛋白经过微射流均质预处理后采用木瓜蛋白酶水解,其酶解产物(水解度为1.7%)与对照大豆分离蛋白和未经预处理的酶解产物相比,在较低浓度下(30 g/L)制备出粒径细小的稳定乳状液(体积平均粒径≈1.6μm)。微射流均质预处理提高了大豆分离蛋白中α-7S和A-11S亚基的酶解敏感性,使酶解产物在水解度1.3%~1.7%范围内蛋白溶解性显著增加(P0.05),同时保持较高的表面疏水性值,与未经预处理的酶解产物相比形成了更多具有界面活性的可溶性多肽(分子量主要分布在11.3 k Da左右),在乳化过程中可有效防止乳液滴间发生桥联絮凝。因此微射流均质预处理是一种辅助提高大豆蛋白酶解效率和酶解产物乳化性能行之有效的方法。研究结果可为大豆蛋白深加工蛋白乳化剂提供理论和方法参考。     

高压均质-冷冻干燥技术制备大豆分离蛋白微粒及其功能特性

为了进一步改善大豆分离蛋白的分散性及功能性质,该研究以大豆分离蛋白为原料,通过对天然大豆分离蛋白进行高压高剪切处理并联合冷冻干燥技术,制备大豆分离蛋白微粒,考察压力(60～100 MPa)对大豆分离蛋白微粒尺寸、功能性质及结构特性的影响,探究其构效关系。结果表明:随着压力逐渐增加,大豆分离蛋白平均粒径大幅度减小,粒径分布曲线向左侧移动,与天然大豆分离蛋白相比,在100 MPa时大豆分离蛋白粒径减小了1 631%,粒径曲线分布较宽。在60～100MPa压力范围内随着压力的增加。与天然大豆分离蛋白相比,大豆分离蛋白微粒的分散性指数(Protein Dispersibility Index, PDI)和功能性质均显著提高(P0.05),其中在100 MPa时大豆蛋白质的溶解性提高了172.98%,乳化活性和乳化稳定性分别增加了约28.71%和77.82%,持油性增加了约123.76%,起泡性随时间的变化其泡沫高度也均有所提高。由扫描电镜图可以观察到,未经过高压均质的大豆分离蛋白粒子呈聚集状态,球状的表面向内凹陷,经过高压均质联合冷冻干燥处理后的大豆分离蛋白微粒呈现网络结构。在高压和高剪切力的作用下,大豆分离蛋白微粒的疏水基团大量暴露,表面疏水性随之增加,静电斥力增加,α-螺旋和β-转角向β-折叠和无规则卷曲结构的转化是蛋白质的溶解性等功能性质提高的主要原因。溶解性等功能性质的提高有利于大豆分离蛋白更好的应用于食品加工行业,进一步为蛋白的理化性质及结构优化提供新思路。     

高压微射流压力对大豆蛋白-大豆多糖体系功能性质的影响

为提升大豆分离蛋白（soy protein isolate,SPI）的功能性质,该文引入大豆可溶性多糖（soybean soluble polysaccharides,SSPS）,构建大豆分离蛋白-大豆可溶性多糖体系（SPI-SSPS）,研究动态高压微射流（dynamic high-pressure microfluidization,DHPM）处理对SPI-SSPS功能特性的影响。分别采用0,60,100,140和180 MPa的 DHPM压力处理SPI-SSPS,探究不同压力对SPI-SSPS起泡特性、乳化特性、溶解性、粒度分布和表面疏水性的影响。结果表明,DHPM处理能提高SPI的溶解性和起泡特性,且SSPS的存在能显著提高DHPM对SPI功能性质的改善效果（P<0.05）。100和60 MPa的DHPM处理能使SPI-SSPS呈现较高的起泡能力和起泡稳定性,分别为未处理样品的1.2和2.4倍。140 MPa的DHPM处理使SPI-SSPS溶解性较强,为未处理样品的1.8倍。然而,DHPM处理会显著降低SPI-SSPS的乳化特性、粒径和表面疏水性（P<0.05）。随着处理压力的增加,SPI-SSPS的粒度和表面疏水性逐渐降低,在180MPa的DHPM处理下SPI-SSPS具有较小的粒径和较低的荧光强度。综上所述,DHPM结合SSPS改性技术可用于改善SPI的功能性质（如溶解性、起泡性）,促进SPI在食品工业的应用。该文的研究结果可为SPI的功能性质改性提供参考。     

Production and characterization of O/W emulsions containing cationic droplets stabilized by lecithin-chitosan membranes

Oil-in-water emulsions containing cationic droplets stabilized by lecithin-chitosan membranes were produced using a two-stage process. A primary emulsion was prepared by homogenizing 5 wt % corn oil with 95 wt % aqueous solution (1 wt % lecithin, 100 mM acetic acid, pH 3.0) using a high-pressure valve homogenizer. This emulsion was diluted with aqueous chitosan solutions to form secondary emulsions with varying compositions: 1 wt % corn oil, 0.2 wt % lecithin, 100 mM acetic acid, and 0-0.04 wt % chitosan (pH 3.0). The particle size distribution, particle charge, and creaming stability of the primary and secondary emulsions were measured. The electrical charge on the droplets increased from -49 to +54 mV as the chitosan concentration was increased from 0 to 0.04 wt %, which indicated that chitosan adsorbed to the droplet surfaces. The mean particle diameter of the emulsions increased dramatically and the emulsions became unstable to creaming when the chitosan concentration exceeded 0.008 wt %, which was attributed to charge neutralization and bridging flocculation effects. Sonication, blending, or homogenization could be used to disrupt flocs formed in secondary emulsions containing droplets with high positive charges, leading to the production of emulsions with relatively small particle diameters (approximately 1 microm). These emulsions had good stability to droplet aggregation at low pH (< or =5) and ionic strengths (<500 mM). The interfacial engineering technology utilized in this study could lead to the creation of food emulsions with improved stability to environmental stresses.     

糖接枝处理改善大豆蛋白纤维聚集体泡沫稳定性

为了探究糖接枝对大豆蛋白纤维聚集行为和泡沫性质的影响,明确蛋白质结构与功能的关系,该研究以大豆蛋白(soy protein isolation,SPI)和乳糖(lactose)为原料,通过干热法制备糖接枝大豆蛋白(SPI-lactose conjugate,SPI-Lac),以及在酸性条件下加热诱导其形成纤维聚集体(p H值2.0),制备了一种糖接枝大豆蛋白纤维聚集体(SPI-lactose conjugate fibillar aggregates),并考察了糖接枝对大豆蛋白的纤维聚集行为及泡沫性质的影响。研究结果表明:大豆蛋白在酸性条件下(p H值2.0)经加热后会发生水解,同时水解产物不断聚集形成大分子的纤维聚集体。糖接枝导致大豆蛋白的水解速度下降,但荧光光强和粒径的结果表明糖接枝能增强纤维聚集能力。SPI-Lac在中性条件下的溶解度(p H值5.0—7.0)显著高于SPI(P0.05),且不同时间处理的SPI-Lac纤维聚集体均能改善SPI在酸性条件下的溶解度(p H值2.0—5.0)。此外,不同时间处理的SPI-Lac纤维聚集体在酸性条件下的起泡能力均高于SPI纤维聚集体。SPI和SPI-Lac纤维聚集体的形成会导致SPI起泡能力的下降,但是短时间酸热处理形成的纤维聚集体泡沫稳定性得到显著改善。因此,糖接枝结合短时间酸热处理制备的糖接枝大豆蛋白纤维聚集体在中性条件下的泡沫稳定性显著提高(P0.05),是合理有效的蛋白质改性方法。     

适宜含水率保持油茶籽贮藏品质

为了确定油茶籽贮藏适宜的含水率,研究了在4℃,不同含水率(7%、10%、13%、16%、20%)油茶籽贮藏期间的品质变化。结果表明,较低的含水率能较好保持油茶籽的贮藏特性及营养品质。其中,含水率为7%的油茶籽贮藏效果较好,但与10%处理效果差异不明显(P>0.05)。在整个贮藏期,含水率为7%时油茶籽可溶性蛋白下降了13.05 mg/g,油酸含量下降了2.38%,酸值、过氧化值等品质指标上升速率较慢,同时能较好保持β-谷甾醇和角鲨烯等生物活性成分;其次是10%的含水率处理。而含水率为20%的油茶籽贮藏期间可溶性蛋白下降较快,贮藏结束时为25.47 mg/g,油茶籽劣变严重,所提取的油样品质变差,营养物质含量较少,因此含水率20%的油茶籽不适宜长期贮藏。综合考虑油茶籽品质因素和处理成本,认为控制含水率在10%以下能较好保持油茶籽的贮藏品质。该研究可为科学合理地贮藏油茶籽提供参考。     

Influence of environmental conditions on the stability of oil in water emulsions containing droplets stabilized by lecithin-chitosan membranes

Oil-in-water emulsions containing cationic droplets stabilized by lecithin-chitosan membranes were produced using a two-stage process. A primary emulsion containing anionic lecithin-coated droplets was prepared by homogenizing oil and emulsifier solution using a high-pressure valve homogenizer (5 wt % corn oil, 1 wt % lecithin, 100 mM acetic acid, pH 3.0). A secondary emulsion containing cationic lecithin-chitosan-coated droplets was formed by diluting the primary emulsion with an aqueous chitosan solution (1 wt % corn oil, 0.2 wt % lecithin, 100 mM acetic acid, and 0.036 wt % chitosan). The stabilities of the primary and secondary emulsions with the same oil concentration to thermal processing, freeze-thaw cycling, high calcium chloride concentrations, and lipid oxidation were determined. The results showed that the secondary emulsions had better stability to droplet aggregation during thermal processing (30-90 degrees C for 30 min), freeze-thaw cycling (-10 degrees C for 22 h/30 degrees C for 2 h), and high calcium chloride contents (相似文献   

Influence of EDTA and citrate on physicochemical properties of whey protein-stabilized oil-in-water emulsions containing CaCl2

The influence of chelating agents (disodium ethylenediaminetetraacetate (EDTA) and sodium citrate) on the physicochemical properties of whey protein isolate (WPI)-stabilized oil-in-water emulsions containing calcium chloride was determined. The calcium-binding characteristics of EDTA and citrate at 30 degrees C were characterized in aqueous solutions (20 mM Tris buffer, pH 7.0) by isothermal titration calorimetry (ITC). EDTA and citrate both bound calcium ions in a 1:1 ratio, but EDTA had a much higher binding constant. Oil-in-water emulsions (pH 7.0) were prepared containing 6.94% (w/v) soybean oil, 0.35% (w/v) WPI, 0.02% (w/v) sodium azide, 20 mM Tris buffer, 10 mM CaCl(2), and 0-40 mM chelating agent. The particle size, apparent viscosity, creaming stability, free calcium concentration, and particle surface potential of the emulsions were measured. The chelating agents reduced or prevented droplet aggregation in the emulsions. When they were present above a certain concentration (>3.5 mM EDTA or >5 mM citrate), droplet aggregation was prevented. The reduction of aggregation was indicated by decreases in particle size, shear-thinning behavior, apparent viscosity, and creaming. Emulsions containing chelating agents had lower free calcium concentrations and more negatively charged droplets, indicating that the chelating agents improved emulsion stability by binding calcium ions. EDTA could be used at lower concentrations than citrate because of its higher calcium ion binding constant.     

Lipid oxidation in corn oil-in-water emulsions stabilized by casein,whey protein isolate,and soy protein isolate

Proteins can be used to produce cationic oil-in-water emulsion droplets at pH 3.0 that have high oxidative stability. This research investigated differences in the physical properties and oxidative stability of corn oil-in-water emulsions stabilized by casein, whey protein isolate (WPI), or soy protein isolate (SPI) at pH 3.0. Emulsions were prepared with 5% corn oil and 0.2-1.5% protein. Physically stable, monomodal emulsions were prepared with 1.5% casein, 1.0 or 1.5% SPI, and > or =0.5% WPI. The oxidative stability of the different protein-stabilized emulsions was in the order of casein > WPI > SPI as determined by monitoring both lipid hydroperoxide and headspace hexanal formation. The degree of positive charge on the protein-stabilized emulsion droplets was not the only factor involved in the inhibition of lipid oxidation because the charge of the emulsion droplets (WPI > casein > or = SPI) did not parallel oxidative stability. Other potential reasons for differences in oxidative stability of the protein-stabilized emulsions include differences in interfacial film thickness, protein chelating properties, and differences in free radical scavenging amino acids. This research shows that differences can be seen in the oxidative stability of protein-stabilized emulsions; however, further research is needed to determine the mechanisms for these differences.     

Preparation and characterization of papain-modified sesame (Sesamum indicum L.) protein isolates

Defatted sesame meal ( approximately 40-50% protein content) is very important as a protein source for human consumption due to the presence of sulfur-containing amino acids, mainly methionine. Sesame protein isolate (SPI) is produced from dehulled, defatted sesame meal and used as a starting material to produce protein hydrolysate by papain. Protein solubility at different pH values, emulsifying properties in terms of emulsion activity index (EAI) and emulsion stability index (ESI), foaming properties in terms of foam capacity (FC) and foam stability (FS), and molecular weight distribution of the SPI hydrolysates were investigated. Within 10 min of hydrolysis, the maximum cleavage of peptide bonds occurred as observed from the degree of hydrolysis. Protein hydrolysates have better functional properties than the original SPI. Significant increase in protein solubility, EAI, and ESI were observed. The greatest increase in solubility was observed between pH 5.0 and 7.0. The molecular weight of the hydrolysates was also reduced significantly during hydrolysis. These improved functional properties of different protein hydrolysates would make them useful products, especially in the food, pharmaceutical, and related industries.     

复配亚麻籽油和辅酶Q10乳液的制备及表征

亚麻籽油和辅酶Q10都具有水中溶解度低、稳定性差、生物利用度低等缺点。将亚麻籽油和辅酶Q10(coenzyme Q10,CoQ10)同时负载于乳液中,可解决两者的应用瓶颈。使用阿拉伯胶为乳化剂,采用高压均质法制备复配亚麻籽油和CoQ10乳液。采用动态光散射、透射电子显微镜、体外模拟消化、体外释放、稀释稳定性、冻融稳定性、离子强度稳定性、光稳定性和加速氧化稳定性方法对所制备乳液的理化性质进行表征。结果显示,制备的乳液平均粒径为(284±5.6) nm,多分散指数(polydispersity index,PDI)为0.112±0.025,为均匀分散的球形液滴。制备的乳液在模拟小肠液中消化,和亚麻籽油、CoQ10混悬液相比,乳化后亚麻籽油的消化速率和CoQ10的生物可给率明显提高。乳液中CoQ10的释放表现出缓释效果。制备的乳液具有较好的稀释和冻融稳定性。Na^+和Ca^2+会造成乳液Zeta电位的下降,对乳液稳定性影响较大。乳液载体化后CoQ10的光稳定性得到了提高。CoQ10对亚麻籽油具有较好的保护作用。     

Role of continuous phase protein on the oxidative stability of fish oil-in-water emulsions

Whey protein isolate (WPI), soy protein isolate (SPI), and sodium caseinate (CAS) can inhibit lipid oxidation when they produce a positive charge at the interface of emulsion droplets. However, when proteins are used to stabilize oil-in-water emulsions, only a fraction of them actually absorb to the emulsion droplets, with the rest remaining in the continuous phase. The impact of these continuous phase proteins on the oxidative stability of protein-stabilized emulsions is not well understood. WPI-stabilized menhaden oil-in-water emulsions were prepared by high-pressure homogenization. In some experiments WPI was removed from the continuous phase of the emulsions through repeated centrifugation and resuspension of the emulsion droplets (washed emulsion). Unwashed emulsions were more oxidatively stable than washed emulsions at pH 7.0, suggesting that continuous phase proteins were antioxidative. The oxidative stability of emulsions containing different kinds of protein in the continuous phase decreased in the order SPI > CAS > WPI, as determined by both hydroperoxide and headspace propanal formation. Iron-binding studies showed that the chelating ability of the proteins decreased in the order CAS > SPI > WPI. The free sulfhydryls of both WPI and SPI were involved in their antioxidant activity. This research shows that continuous phase proteins could be an effective means of protecting omega-3 fatty acids from oxidative deterioration.