Influence of pH and protei thermal treatment on the rheology of pea protein-stabilized oil-in-water emulsions

The influence of emulsion pH and previous thermal treatment of the protein on the rheological behavior of pea protein-stabilized emulsions has been studied. Oil-in-water emulsions with 65% weight oil and 6% weight pea protein isolate were prepared. Emulsion pH was varied between 3.5 and 7.0. In addition to this, the protein aqueous phase was submitted to different previous thermal treatments by modifying temperature from 25 to 90°C and heating time from 20 to 60 min. To study the influence of the above-mentioned variables, droplet size distribution and steady-state flow curves were determined, and linear viscoelastic measurements were carried out. An increase in the pH of the emulsion initially leads to an increase in emulsion viscosity and viscoelastic functions, as well as to a decrease in the mean droplet size, up to an emulsion pH close to the protein isoelectric point, where a singular rheological behavior is found. An increase in temperature or heating time on the protein aqueous phase yields higher values of steady-state viscosity and linear viscoelasticity functions, up to a complete denaturation of the protein.     

Effect of droplet size on lipid oxidation rates of oil-in-water emulsions stabilized by protein

In emulsions lipid oxidation is mainly influenced by the properties of the interface. The aim of this work was to investigate the effects of droplet size and interfacial area on lipid oxidation in protein-stabilized emulsions. Emulsions, made of stripped sunflower oil (30% vol/vol) and stabilized by BSA were characterized by surface area values equal to 0.7, 5.1, and 16.3 m²·cm⁻³ oil. The kinetics of O₂ consumption and conjugated diene (CD) formation, performed on emulsions and nonemulsified controls, showed that emulsification prompted oxidation at an early stage. On condition that oxygen concentration was not limiting, the rates of O₂ consumption and CD formation were higher when the interfacial area was larger. Protein adsorbed at the interface probably restrained this pro-oxidant effect. Once most of the O₂ in the system was consumed (6–8 h), CD remained steady at a level depending directly on the ratio between oxidizable substrate and total amount of oxygen. At this stage of aging, the amounts of primary oxidation products were similar whatever the droplet size of the emulsion. Hexanal and pentane could be detected in the headspace of emulsions only at this stage. They were subsequently produced at rates not depending on oil droplet size and interfacial area.     

Influence of concentration and temperature on the flow behavior of oil-in-water emulsions stabilized by sucrose palmitate

To study the influence that concentration and temperature exert on the viscous behavior of emulsions stabilized by a sucrose ester (SE) of high hydrophilic-lipophilic balance (HLB), flow curves and droplet size distributions were determined. Flow curves of presheared emulsions always exhibited a shear-thinning behavior at intermediate shear rates, a tendency to a limiting viscosity at high shear rates, and a metastable region at low rates. This behavior can be fitted to a Carreau model. Both SE and oil concentrations increase emulsion viscosity as a result of a more structured system with a lower droplet size and polydispersity. An increase in temperature usually leads to a decrease in emulsion viscosity. However, at high oil concentration, coalescence and phase separation take place at low temperature. On the other hand, at high temperature, droplet bursting due to shear forces, leading to an increase in viscosity, may result. Despite the strong structural breakdown caused by steady shear, master flow curves may be obtained by using superposition methods.     

Functional properties of soybean and lupin protein concentrates produced by ultrafiltration-diafiltration

Ultrafiltration followed by diafiltration (UF-DF) was evaluated for the production of protein products from partially defatted soybean meal or undefatted lupin (Lupinus albus L.2043N) meal. This study determined the effects of UF-DF on functional properties of the extracted proteins and compared the results with those of protein prepared by acid-precipitation (AP). UF-DF produced only protein concentrates (73% crude protein, dry basis, db), while AP produced protein isolates (about 90% crude protein, db). Soybean protein produced by UF-DF showed markedly higher values for solubilities up to pH 7.0, surface hydrophobicity index, emulsion activity index, and foaming capacity than did the AP soybean protein. UF-DF soy protein was also the most heat-stable among all protein samples tested. With lupin proteins, only the surface hydrophobicity and emulsion activity indices were significantly improved by using UF-DF. UF-DF generally had no adverse effects on, and in most cases even improved, the functional properties of soy protein concentrate produced by this method. UF-DF did not produce a comparable improvement in functional properties of lupin proteins as it did for soybean protein.     

Functional properties of low-fat soy flour produced by an extrusion-expelling system

Low-fat soy flour (LFSF) obtained by extrusion-expelling processing was investigated for functional properties. Flours with the following various levels of protein dispersibility indexes (PDI) and residual oil (RO) contents were investigated: “high” 67±4/10.4±1, “mid” 42±3/7.4±2, and “low” 14±5/6.5±0. The solubility of all three LFSF was minimal at pH 4.0 and increased at more alkaline and acidic pH levels. Water-holding capacity (WHC) increased with a decrease in PDI and RO content, whereas fat-binding capacity (FBC) decreased. Foaming stability increased as PDI and RO increased, with significant differences between all LFSF samples. Emulsification capacity (EC) was measured at three pH levels (5.5, 6.7, and 8.0). At each pH level, the “low” samples showed the least EC compared to the “mid” and “high” samples, with no significan difference between the “mid” and “high” samples at pH 6.7 and 8.0. Emulsification stability and activity decreased from low LFSF to high LFSF. This study showed that in general low LFSF was less functional than the other flours tested and there was no significant difference in the functionality of mid- and high-LFSF samples.     

Effect of sunflower lecithins on the stability of water-in-oil and oil-in-water emulsions

Lecithins are frequently applied in the food industry as emulsifiers, viscosity regulators, and dispersing agents. The main aim of the present work was to study the emulsifying capability of diverse sunflower lecithins so as to evaluate the functionality of these by-products, which are not extensively used at present. The experimental results obtained for water-in-oil (W/O) emulsions showe that dispersions containing levels of 0.1% lecithins were more stable against coalescence than a control system, whereas those with 1% emulsifying agent exhibited the opposite behavior. On the other hand, faster sedimentation kinetics were observed at a concentration of 0.1% than at 1%. Lecithins with high phospholipid content, especially phosphatidylethanolamine and phosphatidylinositol, were found to be the best emulsifying agents for W/O dispersions. In the case of oil-in-water emulsions, it was possible to observe two processes: creaming of emulsions with the addition of 1% of lecithins, and instant creaming followed by coalescence of the cream phase in those cases corresponding to 0.1% added lecithin.     

Comparison of the effects of three different phosphatidylcholines on casein-stabilized oil-in-water emulsions

Soy oil-in-water emulsions, stabilized by casein, but incorporating one of three different phosphatidylcholines (PC), namely egg-PC, di-palmitoyl phosphatidylcholine (DPPC) and di-oleyl phosphatidylcholine (DOPC), have been studied by photon correlation spectroscopy, light scattering, fast protein liquid chromatography, and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Egg-PC enhanced the stability of emulsions made with low casein concentration, and it competed for space with casein at the oil-water interface during the emulsification process, but no further displacement of protein was found. DPPC had little effect on emulsion stability nor did it show a detectable competition at the interface with casein during or after emulsification. DOPC, however, not only competed with casein at the interface during emulsification, it also removed casein from the interface during storage of the emulsion. The displacement of casein caused instability of the emulsions. Adding DOPC to emulsions also led to displacement of casein from the interface and caused instability of the emulsion, but the process was much slower and occurred to a smaller extent compared to emulsions prepared with DOPC. The different behavior of egg-PC, DPPC, and DOPC on the oil-water interface was in good agreement with their relative solubility in the oil phase as measured by spectrophotometry. All three lipids modified the hydrodynamic thickness of the adsorbed casein layer corresponding to their modification of the surface concentration of casein.     

Influence of soybean protein isolates-phosphatidycholine interaction on the stability on oil-in-water emulsions

Soybean protein isolates and phospholipids present specific surface properties with synergistic or antagonistic effects on emulsion stability. Oil-in-water emulsions (25∶75 w/w) were prepared using native and denatured soybean isolates (NSI and DSI, respectively) with the addition of phosphatidylcholine (PC) (protein/PC ratio 100∶1 to 10∶1). The effect of ionic strength was also studied by adding sodium chloride (0–100 mM) to the aqueous phase. Analysis of NSI/PC and DSI/PC emulsions showed that the creaming rate diminished upon addition of PC, with the creamed phase showing more stability than those of the control systems. In DSI/PC systems, the coalescence process was partially controlled, as evidenced by a decrease in the size of oil droplets. Both systems were altered by the presence of sodium chloride, with an increase in the creaming rate attributable to flocculation and the coalescence of droplets. Under these conditions, DSI/PC emulsions exhibited a stronger protein-phospholipid interaction than those of NSI/PC.     

用流变学方法研究铝离子存在时阴离子表面活性剂胶束的生长和结构(英文)

表面活性剂溶液的流变行为是影响表面活性剂应用的重要因素之一。用流变学方法 ,通过测定溶液在不同浓度和温度时的剪切粘度和应力研究了铝离子存在时阴离子表面活性剂十二烷基聚氧乙烯 (3)硫酸钠 (AES)胶束的生长和结构。结果表明 ,升高表面活性剂和盐的浓度或降低温度都可以促进胶束的生长 ,并且形成虫状胶束和网络结构 ;溶液的流变行为不符合Maxwell模型 ,表现为非线性粘弹性和非牛顿流体     

Enhancing storage stability of emulsions by binding detergents with soy protein isolate and its hydrolysates

Sodium dodecyl sulfate (SDS) is a frequently used anionic detergent, and proteins are among the widely used minor ingredients in cosmetic products. Proteins may enhance the detergent functions and protect human skin from irritation caused by detergents. Soy protein hydrolysates (SPH) were prepared by modifying soy protein (SP) with papain. Varying concentrations of SP or SPH were mixed with various concentrations of SDS at different pH values to determine: (i) molecular characteristics, degree of hydrolysis (DH), and surface hydrophobicity (S ₀) of SP and SPH; (ii) the effect of SDS concentrations on the S ₀ of SP; (iii) the storage stabilities of oil-in-water emulsions formed by SDS, SP, SPH, SP-SDS, and SPH-SDS; and (iv) the effect of protein concentration (0.01 to 1.5%), DH (1.2 to 12.5%), and pH (3.0, 5.0, 7.0, and 9.0) on storage stabilities of emulsions formed by SP-SDS or SPH-SDS. An increase in emulsion stability (ES) with increasing protein concentration was observed. The ES values of emulsions formed by SPH-SDS complexes were significantly higher than those formed by SP-SDS at pH 7.0 and 9.0. The ES of emulsions formed by the complexes were low at pH 5.0 and increased with increasing pH. At pH 3.0 the emulsions formed by SP-SDS at 1 to 1.5% protein concentration and by SPH-SDS at 1.5% protein concentration were very stable. The results indicate that at least one-half of SDS content can be replaced by SP or SPH while maintaining emulsion stability.     

Altering the viscosity of cationically modified cellulose polymers by the addition of salt

The concentration dependence of viscosity is examined for four cationically modified cellulose polymers (UCARE? JR400, UCARE? JR30M, UCARE? LR400, and UCARE? LR30M) in both salt‐free and 50 mM NaCl solution. Similarities in the four polymer systems include: Newtonian viscosity in the dilute regime, shear thinning at higher concentrations, four concentration regimes in salt‐free solution, and three concentration regimes in salt solution. The zero shear rate viscosity and the degree of shear thinning increase with increasing polymer concentration in both salt and salt‐free solutions. While the addition of salt to the lower molecular weight polymers JR400 and LR400 resulted in small changes in viscosity across all concentrations, JR30M and LR30M exhibited significant decreases (up to 81%) and increases (up to 57%) in viscosity upon the addition of salt in the semidilute and entangled regimes, respectively. This viscosity increase in the entangled regime (when comparing salt‐free and 50 mM NaCl solutions) is reported for the first time in cationically modified cellulose polymers. © 2014 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2015 , 132, 41616.     

Effect of value-enhanced texturized soy protein on the sensory and cooking properties of beef patties

Texturized soy protein (TSP) originating from varieties of value-enhanced soybeans and commodity soybeans, which were processed by extrusion-expelling, were incorporated into ground-beef patties. The soybean varieties included high-cysteine, low-linolenic, lipoxygenase-null, high-sucrose, low-saturated-fat, and high-oleic. The lower the bulk density was, the better the water-holding capacity of TSP. Neither property was affected by the protein dispersibility index or residual oil of the low-fat soy flours from which the TSP was prepared. All extruded-expelled processed flours from value-enhanced soybeans made acceptable TSP. The high-sucrose soybeans produced TSP with higher expansion and improved water-holding capacity. There were no differences in cooking properties or proximate compositions of patties for all treatments. Inside and outside colors were darker for the TSP-extended patties than for the all-beef control, and there was little difference among soybean varieties. The patties containing TSP had significantly more soy flavor and were harder than the all-beef control patties. Some TSP treatments produced more tender and less cohesive cooked patties than did the all-beef control.     

Is plastic fat rheology governed by the fractal nature of the fat crystal network?

The rheological properties of interesterified and noninteresterified butterfat-canola oil blends do not seem to be strongly related to either solid fat content (SFC) or crystal polymorphic behavior, but rather to the microstructure of the fat crystal network. The microstructure of the fats was quantified by using fractal geometric relationships between the elastic moduli (G′) of the fats and their SFC values using the approach of Shih, W.H., W.Y. Shih, S.I. Kim, J. Liu, and I.A. Aksay [Phys. Rev. A 42:4772–4779 (1990))] for weak-link regimes. Chemical interesterification decreased the fractal dimension of the fat crystal network from 2.46 to 2.15. We propose that fat microstructure, as quantified by a fractal dimensionality, could be modified to attain specific rheological properties.     

Effects of ultrasound and microwave pretreatments on the ultrafiltration desalination of salted duck egg white protein

The effects of application of ultrasound and microwave treatments before the ultrafiltration desalination of salted duck egg white protein were investigated in this work. The desalination rate, color, microstructure, foaming capacity, emulsifying index and gelling property were determined. The results showed that ultrasound and microwave pretreatments increased about 10% and 3% desalination rate, respectively, compared to that without any pretreatment sample, beside the product quality was also improved. The effect of ultrasound pretreatment was better than that of microwave in terms of foaming capacity and emulsifying index of the product.     

C-terminal modifications of a protein by UAG-encoded incorporation of puromycin during in vitro protein synthesis in the absence of release factor 1

Deactivation of release factor 1 by polyclonal antibodies in an in vitro translation system, which was used to express the esterase gene, led to the reversible elimination of naturally occurring termination. This technique allowed the antibiotic puromycin to be used as an acceptor substrate for the peptidyl residue in the peptidyl-transferase reaction. This resulted in more than 80 % yield of protein with C-terminally incorporated puromycin. pCpPuromycin that was either conjugated with the Cy3 fluorophor or biotin by N4 alkylation of cytosine, also acted as an acceptor substrate for the peptidyl-transferase reaction and was incorporated into the protein C terminus. The resulting conjugates possessed Cy3-specific fluorescence and affinity to streptavidin-coated surfaces, respectively. This left the enzymatic activity of the reporter protein unaffected. It was also shown that extension of puromycin on its 5'-hydroxyl end by up to ten deoxyoligonucleotides also allowed conjugation with the C terminus of in vitro translated protein when RF1-dependent termination was suppressed. However, the conjugation yield decreased upon addition of more than six nucleotides.     

Effect of alkali on the refunctionalization of soy protein by hydrothermal cooking

The effects of hydrothermal cooking (HTC) at alkaline conditions on refunctionalization of heat-denatured protein of extruded-expelled (EE) soy meals and on preparation of soy protein isolate (SPI) from EE soy meal were determined. Two HTC setups, flashing-out HTC (without holding period) and HTC with holding for 42 s at 154°C, were evaluated. Alkali (NaOH) addition dramatically enhanced the refunctionalization of EE meal having an initial protein dispersibility index of 35. The more alkali added, the more refunctionalization occurred. Extensive refunctionalization was achieved at 0.6 mmol alkali/g EE meal, and additional improvement was small with more alkali. For both HTC setups, the solids and protein yields of SPI from alkali-HTC-treated EE meals were significantly higher than those from HTC without alkali addition. The yield of protein as SPI increased from 40 to 82% after HTC treatment at 0.6 mmol alkali/g EE meal compared with no alkali addition. The emulsification capacities of SPI after alkali-HTC were similar to those from HTC without alkali. SPI from holding-tube HTC-treated EE meals had higher emulsification capacities than those prepared by flashing-out HTC.     

Microtiter plate-based screening for the optimization of DNA-protein conjugate synthesis by means of expressed protein ligation

We report a rapid microtiter plate screening assay for the optimization of the synthesis of covalent DNA-protein conjugates by means of expressed protein ligation (EPL). The EPL method allows for the site-specific coupling of cysteine-modified DNA oligomers with recombinant intein-fusion proteins, the latter containing a C-terminal thioester that enables a mild and highly specific reaction with N-terminal cysteine compounds. To screen for optimal reaction conditions, we developed a microtiter plate-based assay that utilizes DNA-directed immobilization of the products formed in the ligation reaction of cysteine-modified DNA oligonucleotides with the model protein thioester of the maltose-binding protein (MBP), recombinantly expressed as an intein-fusion protein in E. coli. The screening assay allowed the rapid quantitative monitoring of various reaction parameters, such as the ratio of the reactants, reaction times, pH and ion strength of the buffer, the influence of various thiol additives and the nature of the chemical linker within the cysteine-bearing DNA oligonucleotide. As the consequence of the assay-based optimization, the ligation of MBP with the oligonucleotide was improved to near quantitative yields.