Jin-Mei Wang

Adsorption and dilatational rheology of heat-treated soy protein at the oil-water interface: relationship to structural properties.

We evaluated the influence of heat treatment on interfacial properties (adsorption at the oil-water interface and dilatational rheology of interfacial layers) of soy protein isolate. The related structural properties of protein affecting these interfacial behaviors, including protein unfolding and aggregation, surface hydrophobicity, and the state of sulfhydryl group, were also investigated. The structural and interfacial properties of soy protein depended strongly on heating temperature (90 and 120 °C). Heat treatment at 90 °C induced an increase in surface hydrophobicity due to partial unfolding of protein, accompanied by the formation of aggregates linked by disulfide bond, and lower surface pressure at long-term adsorption and similar dynamic interfacial rheology were observed as compared to native protein. Contrastingly, heat treatment at 120 °C led to a higher surface activity of the protein and rapid development of intermolecular interactions in the adsorbed layer, as evidenced by a faster increase of surface pressure and dilatational modulus. The interfacial behaviors of this heated protein may be mainly associated with more flexible conformation and high free sulfhydryl group, even if some exposed hydrophobic groups are involved in the formation of aggregates. These results would be useful to better understand the structure dependence of protein interfacial behaviors and to expand utilization of heat-treated protein in the formulation and production of emulsions.

Protein-Based Pickering Emulsion and Oil Gel Prepared by Complexes of Zein Colloidal Particles and Stearate

This paper describes the successful preparation of a protein-based Pickering emulsion, with superior stability against both coalesence and creaming, through a novel strategy of facilitating the formation of protein particles and small molecular weight surfactant complexes; these complexes are able to overcome multiple challenges including limited solubility, poor diffusive mobility, and low interfacial loading. Soluble complexes of water-insoluble corn protein, zein colloidal particles, and surfactant sodium stearate (SS) were fabricated by simple ultrasonication. Gel trapping technology combined with SEM was applied to characterize the adsorbed particles monolayer at the oil-water interface; results revealed an enhanced adsorption and targeted accumulation of zein particles at the interface with the increase of SS concentration. Partial unfolding of zein particles modified by SS above its critical complexation concentration triggered the aggregation and close packing of particles at the oil-water interface and endowed a steric barrier against the coalescence of oil droplets. Moreover, protein-based oil gels without oil leakage were obtained by one-step freeze-drying of the zein-stabilized Pickering emulsions, which could be developed to a viable strategy for structuring liquid oils into semisolid fats without the use of saturated or trans fats.

Pickering Emulsion Gels Prepared by Hydrogen-Bonded Zein/Tannic Acid Complex Colloidal Particles

Food-grade colloidal particles and complexes, which are formed via modulation of the noncovalent interactions between macromolecules and natural small molecules, can be developed as novel functional ingredients in a safe and sustainable way. For this study was prepared a novel zein/tannic acid (TA) complex colloidal particle (ZTP) based on the hydrogen-bonding interaction between zein and TA in aqueous ethanol solution by using a simple antisolvent approach. Pickering emulsion gels with high oil volume fraction (φ(oil) > 50%) were successfully fabricated via one-step homogenization. Circular dichroism (CD) and small-angle X-ray scattering (SAXS) measurements, which were used to characterize the structure of zein/TA complexes in ethanol solution, clearly showed that TA binding generated a conformational change of zein without altering their supramolecular structure at pH 5.0 and intermediate TA concentrations. Consequently, the resultant ZTP had tuned near neutral wettability (θ(ow) ∼ 86°) and enhanced interfacial reactivity, but without significantly decreased surface charge. These allowed the ZTP to stabilize the oil droplets and further triggered cross-linking to form a continuous network among and around the oil droplets and protein particles, leading to the formation of stable Pickering emulsion gels. Layer-by-layer (LbL) interfacial architecture on the oil-water surface of the droplets was observed, which implied a possibility to fabricate hierarchical interface microstructure via modulation of the noncovalent interaction between hydrophobic protein and natural polyphenol.

Enhanced Physical and Oxidative Stabilities of Soy Protein-Based Emulsions by Incorporation of a Water-Soluble Stevioside–Resveratrol Complex

To strengthen the effectiveness of resveratrol (RES) as a natural antioxidant in food systems, this work attempted to enhance the water solubility of RES by utilizing the solubilizing properties of stevioside (STE) and investigated the effect of STE-solubilized RES (STE-RES) incorporation on the stability of soy protein isolate (SPI)-based emulsions. The physical properties and oxidative stability of SPI emulsions with STE/STE-RES were evaluated. The water solubility of RES increased with the increase of STE concentration up to its critical micelle concentration, suggesting the solubilization of hydrophobic RES in STE self-assembled micelles. STE micelles competitively adsorbed at the oil-water interface with SPI, forming a mixed SPI and STE interfacial layer, thus resulting in a decrease in particle size and evident enhancement in the physical stability of SPI-based emulsions. After the incorporation of STE-RES, SPI emulsions showed an enhanced oxidative stability with reduced lipid hydroperoxides and volatile hexanal. This improvement was believed to be mainly attributed to the targeted migration of RES to the interface during the adsorption of the STE-RES complex, as evidenced by high interfacial accumulation of RES.

Synergistic foaming and surface properties of a weakly interacting mixture of soy glycinin and biosurfactant stevioside.

The adsorption of the mixtures of soy glycinin (11S) with a biosurfactant stevioside (STE) at the air-water interface was studied to understand its relation with foaming properties. A combination of several techniques such as dynamic surface tension, dilatational rheology, fluorescence spectroscopy, and isothermal titration calorimetry (ITC) was used. In the presence of intermediate STE concentrations (0.25-0.5%), the weak binding of STE with 11S in bulk occurred by hydrophobic interactions, which could induce conformational changes of 11S, as evidenced by fluorescence and ITC. Accordingly, the strong synergy in reducing surface tension and the plateau in surface elasticity for mixed 11S-STE layers formed from the weakly interacting mixtures were clearly observed. This effect could be explained by the complexation with STE, which might facilitate the partial dissociation and further unfolding of 11S upon adsorption, thus enhancing the protein-protein and protein-STE interfacial interactions. These surface properties were positively reflected in foams produced by the weakly interacting system, which exhibited good foaming capacity and considerable stability probably due to better response to external stresses. However, at high STE concentrations (1-2%), as a consequence of the interface dominated by STE due to the preferential adsorption of STE molecules, the surface elasticity of layers dramatically decreased, and the resultant foams became less stable.

Structural rearrangement of ethanol-denatured soy proteins by high hydrostatic pressure treatment.

The effects of high hydrostatic pressure (HHP) treatment (100-500 MPa) on solubility and structural properties of ethanol (EtOH)-denatured soy β-conglycinin and glycinin were investigated using differential scanning calorimetry, Fourier transform infrared and ultraviolet spectroscopy. HHP treatment above 200 MPa, especially at neutral and alkaline pH as well as low ionic strength, significantly improved the solubility of denatured soy proteins. Structural rearrangements of denatured β-conglycinin subjected to high pressure were confirmed, as evidenced by the increase in enthalpy value (ΔH) and the formation of the ordered supramolecular structure with stronger intramolecular hydrogen bond. HHP treatment (200-400 MPa) caused an increase in surface hydrophobicity (F(max)) of β-conglycinin, partially attributable to the exposure of the Tyr and Phe residues, whereas higher pressure (500 MPa) induced the decrease in F(max) due to hydrophobic rearrangements. The Trp residues in β-conglycinin gradually transferred into a hydrophobic environment, which might further support the finding of structural rearrangements. In contrast, increasing pressure induced the progressive unfolding of denatured glycinin, accompanied by the movement of the Tyr and Phe residues to the molecular surface of protein. These results suggested that EtOH-denatured β-conglycinin and glycinin were involved in different pathways of structural changes during HHP treatment.

Soy lipophilic protein nanoparticles as a novel delivery vehicle for conjugated linoleic acid

Soy lipophilic protein nanoparticles (LPP), which present a novel delivery vehicle for conjugated linoleic acid (CLA), were fabricated by ultrasonication of the soy lipophilic protein (LP), which exhibits unique characteristics including a high loading capacity, oxidation protection and a sustained releasing profile in vitro for CLA. The CLA-loaded LPP exhibited a mean diameter of 170 ± 0.63 nm and a loading capacity of 26.3 ± 0.40% (w/w). A coating of sodium caseinate (SC) on the surface improved the colloidal stability of the CLA-loaded LPP. This encapsulation conferred protection against the oxidation of CLA, by which the head space-oxygen consumption and hydrogen peroxide value were obviously decreased in comparison with the SC-encapsulated CLA and CLA alone. The delivery system enables a sustained releasing profile of CLA in a simulated gastrointestinal tract (GIT). These findings illustrate that the LPP could act as an effective delivery device for CLA, which could provide oxidation stability and a sustained release property.

Development of Novel Zein-Sodium Caseinate Nanoparticle (ZP)-Stabilized Emulsion Films for Improved Water Barrier Properties via Emulsion/Solvent Evaporation

This work attempted to develop novel high barrier zein/SC nanoparticle (ZP)-stabilized emulsion films through microfluidic emulsification (ZPE films) or in combination with solvent (ethyl acetate) evaporation techniques (ZPE-EA films). Some physical properties, including tensile and optical properties, water vapor permeability (WVP), and surface hydrophobicity, as well as the microstructure of ZP-stabilized emulsion films were evaluated and compared with SC emulsion (SCE) films. The emulsion/solvent evaporation approach reduced lipid droplets of ZP-stabilized emulsions, and lipid droplets of ZP-stabilized emulsions were similar to or slightly lower than that of SC emulsions. However, ZP- and SC-stabilized emulsion films exhibited a completely different microstructure, nanoscalar lipid droplets were homogeneously distributed in the ZPE film matrix and interpenetrating protein-oil complex networks occurred within ZPE-EA films, whereas SCE films presented a heterogeneous microstructure. The different stabilization mechanisms against creaming or coalescence during film formation accounted for the preceding discrepancy of the microstructures between ZP-and SC-stabilized emulsion films. Interestingly, ZP-stabilized emulsion films exhibited a better water barrier efficiency, and the WVP values were only 40-50% of SCE films. A schematic representation for the formation of ZP-stabilized emulsion films was proposed to relate the physical performance of the films with their microstructure and to elucidate the possible forming mechanism of the films.

Formation of Complex Interface and Stability of Oil-in-Water (O/W) Emulsion Prepared by Soy Lipophilic Protein Nanoparticles

A lipophilic protein nanoparticle (LPP) was fabricated by ultrasonication of the soy lipophilic protein (LP), which contains hydrophobic proteins and phospholipids. This LPP (Rh = 136 ± 0.8 nm, ζ-potential = -20 mV, pH 7.0) had an improved dispersibility and acted as an emulsifier. The oil/water (O/W) emulsion stabilized by this LPP exhibited superior physical stability over long-term storage (8 weeks), during a stress storage test (200 mM NaCl addition and heating at 90 °C), and in the presence of Tween 20 (1.0-4.0 wt %), in contrast to those emulsions stabilized by β-conglycinin and glycinin. Langmuir-Blodgett method and interface pressure determination revealed that LPP formed rigid and rough granular film at air/water interface. The excellent stability of emulsions stabilized by LPP highlights the synergic effect between hydrophobic proteins and phospholipids. These findings suggest that the complexes of hydrophobic protein aggregates and biosurfactant could form a stable interface which could be developed into a novel strategy to fabricate a stable food emulsion.

Zein based oil-in-glycerol emulgels enriched with β-carotene as margarine alternatives.

Structuring edible oils into solid lipids without saturated and trans fats has attracted increasing interest due to the benefits for human health and promises potential as novel delivery systems for lipophilic bioactive ingredients. The study shows that a zein stabilized high (ϕ=0.6) oil-in-glycerol (O/G) emulgels enriched with β-carotene was performed, by a facile one-step homogenization. Rheological measurements and morphologies observations indicated that increasing β-carotene resulted in a progressive strengthening of gel-like network and improving their spreadability in the O/G emulgels stabilized by zein, which was closely related to the hydrophobic interaction of zein and β-carotene. The formation of emulgels significantly enhanced the UV photo-stability of β-carotene, and more than 88% of β-carotene was retained in 64h storage under UV exposure, and consequently retarded oil oxidation while storage. Further, cakes prepared using zein-based O/G emulgels as a margarine alternative showed comparable functionalities (texture and sensory attributes) to the standard cake.