Calcium-Induced Destabilization of Oil-in-Water Emulsions Stabilized by Caseinate or by β-Lactoglobulin

The stability to aggregation of 20% soya oil-in-water emulsions stabilized by 0.3 to 2% sodium caseinate or β-lactoglobulin in the presence of calcium chloride solutions was studied using light scattering and electron microscopy. Stability increased with the amount of protein in the emulsion, and decreased with the concentration of added calcium. Growth of particle size with concentration of Ca²⁺ was more in emulsions containing lower concentrations of protein. Sodium chloride at 50 and 100 mM stabilized both systems to the presence of calcium ions. Microstructure and light scattering showed caseinate emulsions formed clusters even at low concentrations of Ca²⁺ while β-lactoglobulin emulsions formed extensive strands.     

Competitive Adsorption Between Sodium Caseinate and Oil-Soluble and Water-Soluble Surfactants in Oil-in-Water Emulsions

Competitive adsorption between sodium caseinate and either a water-soluble surfactant, Tween 60 (polyoxyethylene sorbitan monostearate—PSM) or an oil-soluble surfactant, Span 60 (sorbitan monostearate—SM) was studied in oil-in-water emulsions. Surfactants were present during homogenization. Surface concentration of protein in freshly prepared emulsions decreased as concentration of PSM or SM increased. However, only partial displacement of protein was observed with either surfactant. The reduction in protein surface concentration was greater in the presence of PSM. Interfacial protein composition was independent of surfactant type. In the absence of surfactant, preferential adsorption of β-casein occured in emulsions containing ≤1.0 wt % protein. On addition of surfactant preference for β-casein at the interface was reduced.     

Oil-in-Water Emulsions Stabilized by Sodium Caseinate or Whey Protein Isolate as influenced by Glycerol Monostearate

Competitive adsorption between glycerol monostearate (GMS) and whey protein isolate (WPI) or sodium caseinate was studied in oil-in-water emulsions (20 wt % soya oil, deionized water, pH 7). Addition of GMS resulted in partial displacement of WPI or sodium caseinate from the emulsion interface. SDS-PAGE showed that GMS altered the adsorbed layer composition in sodium caseinate stabilized emulsions containing < 1.0 wt % protein. Predominance of β-casein at the interface in the absence of surfactant was reduced in the presence of GMS. The distribution of α-lactalbumin and β-lactoglobulin between the aqueous bulk phase and the fat surface in emulsions stabilized with WPI was independent of the concentration of added protein or surfactant.     

单硬脂酸甘油酯对酪蛋白再制稀奶油乳化稳定性的影响

分析单硬脂酸甘油酯（glycerin monostearate,GMS）对胶束酪蛋白（micellar casein,MCN）再制稀奶油（recombined dairy creams,RDCs）、酪蛋白酸钙（calcium caseinate,CaC）-RDCs及酪蛋白酸钠（sodium caseinate,NaC）-RDCs乳化稳定性的影响。结果表明：GMS可通过与酪蛋白共同吸附在油水界面上使RDCs的脂肪球分散程度改变,因而乳化稳定性也相应改变。对于MCN-RDCs,GMS可显著增加RDCs的相分离时间,其中2.5% MCN-RDCs的乳化稳定性最大,相分离时间从474 s显著增加至4 622 s。CaC-RDCs中,蛋白添加量为0.5%～2.0%时,GMS的添加使CaC-RDCs的相分离时间由167～483 s增加至177～517 s;而2.5% CaC-RDCs的相分离时间有所下降。NaC-RDCs中,GMS的添加使0.5% NaC-RDCs的相分离时间由1 245 s增加至1 460 s;NaC-RDCs添加量大于1.0%时,相分离时间有不同程度下降。可见,GMS可增加MCN-RDCs的乳化稳定性;而其对CaC-RDCs和NaC-RDCs乳化稳定性的影响与蛋白含量有关,当CaC和NaC添加量分别为0.5%～2.0%、0.5%时,GMS才可增加RDCs体系的乳化稳定性。     

黄原胶对O/W乳状液稳定性的影响

报道了含有黄原胶的２０Ｏ／Ｗ乳状液贮藏在２７～３０℃的分层动力学的研究。实验运用超声波技术考察了从０．０００５～０．５ｗｔ％的一系列浓度的黄原胶对体系分层特性的影响。在非常低（＜０．００１ｗｔ％）的黄原胶浓度下，实验体系的稳定性变化不大。０．０１～０．０２ｗｔ％的黄原胶可引起样品底部富水层出现，但体系无明显分层。当黄原胶浓度增加到０．０２ｗｔ％以上，乳状液很快分层，且分层的状态取决于黄原胶添加量。只有当添加量超过０．２５ｗｔ％，黄原胶才能起到提高体系稳定性的作用。对非吸附性的黄原胶的这种影响，可以用“排除絮凝”和弱凝胶结构形成的机理进行解释。     

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.     

Sodium Caseinate and Skim Milk Gels Formed by Incubation with Microbial Transglutaminase

Several suspensions and emulsions containing commercial sodium caseinate or skim milk were gelatinized by Ca²⁺-independent microbial transglutaminase treatment. The characteristics of the gels were largely affected by the enzyme concentrations employed. For caseinate gels generally the higher enzyme concentration gave steep decreases in breaking strength, strain and cohesiveness of the gels. The creep tests on emulsified gels prepared to two different enzyme concentrations showed that the gel made with a higher enzyme concentration was the more viscoelastic. For skim milk gels, the enzyme treatment in higher concentration caused substantial increase of the breaking and hardness while the strain and cohesiveness had little or no changes.     

酒精对酪蛋白酸钠溶液及O/W乳状液的影响

介绍了酒精对酪蛋白酸钠溶液及酪蛋白稳定的O/W乳状液性质的影响 .试验表明酒精在一定程度上可以降低酪蛋白酸钠的溶解度 .界面张力的测定则表明酒精的存在在很大程度上可以降低油—水界面和油—酪蛋白溶液界面的界面张力 .含酒精的乳状液体系的粘度会由于酒精的存在而提高 ,在酒精体积分数达 3 0 %时 ,乳状液体系的粘度会突然大幅度升高 .通过O/W乳状液的分层稳定性测定可发现 ,低浓度的酒精可以提高酪蛋白稳定的乳状液的分层稳定性 ,但酒精质体积分数超过 3 2 %时 ,乳状液的分层稳定性会受到破坏 .含酒精的O/W乳状液体系中油相含量的提高在一定范围内可以提高乳状液的稳定性 ,但高分散相浓度的含酒精的乳状液体系中由于连续相中酒精浓度的提高使乳状液体系稳定性下降 .     

Kinetics for Describing the Creaming of Protein-Stabilized O/W Emulsions by Multiple Light Scattering

In the present work, new kinetics to describe the creaming stability of oil-in-water emulsions determined by backscattering measurements （BS） is proposed. The emulsions assayed exhibited a different backscattering profiles regarding creaming destabilization hyperbolic and sigmoid one. Hyperbolic behavior can be described by a second order kinetics, where k_h could be equaled to a rate constant that describes the creaming process and its values would indicate the stability of emulsions. While for the sigmoid BS pattern, kinetics with two terms, is adequate to describe the creaming process in contrast to kinetics previously reported in the literature. The kh value has the same meaning as before, and ks indicates the delaying effect on the creaming rate.     

Flocculation of Whey Protein Stabilized Emulsions as Influenced by Dextran Sulfate and Electrolyte

The creaming stability and viscosity of oil-in-water emulsions stabilized by whey protein isolate were monitored as functions of dextran sulfate (DS) and electrolyte (NaCl) concentration. At a specific DS concentration (the critical flocculation concentration, CFC), the droplets became flocculated, which promoted creaming. Addition of electrolyte caused an increase in CFC. At NaCl concentrations <0.5 wt%, addition of electrolyte decreased emulsion viscosity, but at concentrations >0.5 wt% it caused an increase in viscosity due to increased flocculation. The results were due to the influence of electrostatic screening on the effective volume of DS molecules and colloidal interactions between droplets.     

Formulation and Stability Characterization of Rutin-Loaded Oil-in-Water Emulsions

In this work, formulation and characterization of oil-in-water (O/W) emulsions loaded with rutin were successfully overhead. We investigated the effect of homogenization pressure on the mean droplet size, droplet size distribution, physical stability, and rutin retention of these emulsions. O/W emulsions with a mean droplet size (d _3,2) of about 150 nm and a span of nearly the unit were formulated by microfluidization at the homogenization pressure 20–150 MPa. The O/W emulsion droplets loaded with rutin were physically stable in terms of variations of d _3,2 and span during 30 days of storage in the dark condition at 4 and 25 °C. The creaming velocity was characterized using centrifugal method showing a relative good shelf life. HPLC analysis demonstrated that 71–85% of initial rutin was retained in the fresh O/W emulsions and declined to 22–35% (w/w) for 30-day storage at 25 °C. Antioxidant activity assays confirmed that rutin-loaded emulsion participated in the antioxidant activity after encapsulation similarly to pure rutin. These results indicate that O/W emulsion systems can function as potential delivery systems to enhance bioavailability to encapsulate liposoluble antioxidant rutin for potential applications in the food industry.     

Physical Stability of Whey Protein-stabilized Oil-in-water Emulsions at pH 3: Potential ω-3 Fatty Acid Delivery Systems (Part A)

ABSTRACT: The oxidative stability of polyunsaturated lipids can be improved by incorporating them in oil droplets surrounded by positively charged whey protein isolate (WPI) membranes. This study dealt with the factors that influence the physical properties of WPI-stabilized oil-in-water emulsions at pH 3. Emulsions containing 5 to 50 wt% corn oil and 0.5 to 5.0 wt% WPI (protein-to-oil ratio of 1:10) were prepared at pH 3. The apparent viscosity of the emulsions increased appreciably at oil concentrations ≥ 35 wt%; however, the particle size was relatively independent of oil concentration. The influence of NaCl (0 to 250 m M ) on the physical properties of 28 wt% emulsions was examined. Significant increases in mean particle size, apparent viscosity, and creaming instability occurred at ≥150 m M NaCl, which were attributed to flocculation induced by screening of the electrostatic repulsion between droplets. The influence of heat treatment (30°C to 90°C for 30 min) on 28 wt% emulsions was examined in the absence and presence of salt, respectively. At 0 m M NaCl, heating had little effect on the physical properties of the emulsions, presumably because the electrostatic repulsion between the droplets prevented droplet aggregation. At 150 m M NaCl, the mean particle diameter, apparent viscosity, and creaming instability of the emulsions increased considerably when they were heated above a critical temperature, which was 70°C when salt was added before heating and 90°C when salt was added after heating. These results have important implications for the design of WPI-stabilized emulsions that could be used to incorporate functional lipids that are sensitive to oxidation, for example, ω-3 fatty acids.     

Characteristics of Sodium Caseinate- and Soy Protein Isolate-Stabilized Emulsion-Gels Formed by Microbial Transglutaminase

ABSTRACT:  Protein-stabilized emulsion gels were prepared via microbial transglutaminase (mTGase) catalysis, and their physicochemical characteristics were examined. Emulsion oil droplet size and interfacial protein load were measured. The sodium caseinate and soy protein isolate emulsion gels exhibited different microstructures and physical properties. The emulsion gels improved the storage stability of aroma compounds. Rheological measurements of the emulsion gels revealed interesting strength, gelation kinetics, and thermal sensitivity properties. The mTGase-induced emulsion gels comprised a fine network which led to less release of aroma compounds upon storage than did emulsions. These results suggest that emulsion gels may be used to improve the texture of food emulsions and to control release of food aromas.     

Influence of Droplet Charge on the Chemical Stability of Citral in Oil-in-Water Emulsions

Abstract: The chemical stability of citral, a flavor component widely used in beverage, food, and fragrance products, in oil-in-water emulsions stabilized by surfactants with different charge characteristics was investigated. Emulsions were prepared using cationic (lauryl alginate, LAE), non-ionic (polyoxyethylene (23) lauryl ether, Brij 35), and anionic (sodium dodecyl sulfate, SDS) surfactants at pH 3.5. The citral concentration decreased over time in all the emulsions, but the rate of decrease depended on surfactant type. After 7 d storage, the citral concentrations remaining in the emulsions were around 60% for LAE- or Brij 35-stabilized emulsions and 10% for SDS-stabilized emulsions. An increase in the local proton (H⁺) concentration around negatively charged droplet surfaces may account for the more rapid citral degradation observed in SDS-stabilized emulsions. A strong metal ion chelator (EDTA), which has previously been shown to be effective at increasing the oxidative stability of labile components, had no effect on citral stability in LAE- or Brij 35-stabilized emulsions, but it slightly decreased the initial rate of citral degradation in SDS-stabilized emulsions. These results suggest the surfactant type used to prepare emulsions should be controlled to improve the chemical stability of citral in emulsion systems.     

甲基纤维素对大豆分离蛋白乳浊液稳定性影响的研究

本文研究了甲基纤维素对大豆分离蛋白乳浊液稳定性的影响。研究结果表明，在低浓度时，甲基纤维素增加了体系的稳定性，对NaCl引起的液滴絮凝也有很好的抑制作用。而高浓度的甲基纤维素导致pH6．5和7．0的体系同时发生乳析和蛋白质沉积现象。其作用机理可能是，在低浓度时甲基纤维素吸附到液滴蛋白质层的外围形成次级保护层，增加了体系的稳定性，而高浓度时则可能置换出液滴的蛋白质吸附层。     

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。     

Fat Particle Structure and Stability of Food Emulsions

We used a nondestructive Kossel diffraction technique based on the principle of backlight scattering to characterize the structure formation in concentrated model food emulsions. We also measured the effects of temperature, shear, casein micelles and gum on the fat particle packing structure in such systems. Through this technique, we demonstrated the effects of casein micelles on the pair potential of fat particle interactions and shelf life of such systems. We carried out theoretical calculations using a statistical mechanics approach by numerically solving the Ornstein-Zernike equation with Percus-Yevick closure for a bidisperse system consisting of fat particles and micelles, and showed that the experimental results were consistent with theoretical simulations.     

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.     

瓜尔豆胶对大豆分离蛋白乳浊液稳定性的影响

研究了不同pH值条件下瓜尔豆胶对大豆分离蛋白乳浊液乳析稳定性和絮凝稳定性的影响。研究结果表明 ,在瓜尔豆胶浓度低于 0 0 4%时 ,随着瓜尔豆胶浓度的增加 ,乳浊液的稳定性逐渐增加。当多糖浓度高于 0 0 4%时 ,液滴发生排斥絮凝 ,体系的稳定性急剧下降 ,更高浓度的瓜尔豆胶因与乳浊液液滴间的热力学不相容性而导致体系发生各向同性和各向异性相分离。     

中性多糖对大豆分离蛋白乳浊液稳定性影响的机理探讨

本文研究了瓜尔豆胶和甲基纤维素对大豆分离蛋白乳浊液乳析和絮凝稳定性的影响，并提出了可能的作用机理：在低浓度时瓜尔豆胶，非吸附的多糖分子充斥于蛋白质包被的液滴之间使液滴保持分散状态，随着多糖浓度的增加，体系发生排斥絮凝及各向同性与各向异性相分离。较低浓度的甲基纤维素吸附到液滴的蛋白质吸附层，从而保护液滴不发生絮凝；甲基纤维素浓度较高时，置换出液滴吸附的蛋白质而形成沉淀和大粒径的液滴。