Development of a Clean Label Mayonnaise Using Fruit Flour.

Over the past few years, clean label food has been growing, meaning that consumers are searching for shorter and simpler ingredient lists composed of familiar and natural ingredients. The objective of the present work was to develop a vegan clean label mayonnaise, replacing the additives with fruit flour obtained from fruit reduced commercial value. The mayonnaises were prepared by replacing the egg yolk with 1.5% (w/w) lupin and faba proteins, while fruit flour (apple, nectarine, pear, and peach flour) was incorporated to substitute sugar, preservatives, and colorants. Texture profile analysis and rheology-small amplitude oscillatory measurements were performed to evaluate the impact of the fruit flour on mechanical properties. The mayonnaise antioxidant activity was also analyzed in terms of color, pH, microbiology, and stability measurements. The results showed that mayonnaises produced with fruit flour had better structure parameters in terms of viscosity, and texture, but also improved pH and antioxidant activity (p < 0.05) compared to the standard mayonnaise (mayonnaise without fruit flour). The incorporation of this ingredient into mayonnaise increases the antioxidant potential, though it is in lower concentrations compared to the fruit flours that compose them. Nectarine mayonnaise showed the most promising results in terms of texture and antioxidant capacity (11.30 mg equivalent of gallic acid/100 g).

Impact of Grass Pea Sweet Miso Incorporation in Vegan Emulsions: Rheological, Nutritional and Bioactive Properties.

Grass pea (Lathyrus sativus L.) is a pulse with historical importance in Portugal, but that was forgotten over time. Previous to this work, an innovative miso was developed to increase grass pea usage and consumption, using fermentation as a tool to extol this ingredient. Our work's goal was to develop a new vegan emulsion with added value, using grass pea sweet miso as a clean-label ingredient, aligned with the most recent consumer trends. For this, a multidisciplinary approach with microbiological, rheological and chemical methods was followed. Grass pea sweet miso characterization revealed a promising ingredient in comparison with soybean miso, namely for its low fat and sodium chloride content and higher content in antioxidant potential. Furthermore, in vitro antimicrobial activity assays showed potential as a preservation supporting agent. After grass pea sweet miso characterization, five formulations with 5-15% (w/w) of miso were tested, with a vegan emulsion similar to mayonnaise as standard. The most promising formulation, 7.5% (w/w) miso, presented adequate rheological properties, texture profile and fairly good stability, presenting a unimodal droplet size distribution and stable backscattering profile. The addition of 0.1% (w/w) psyllium husk, a fiber with great water-intake capacity, solved the undesirable release of exudate from the emulsion, as observed on the backscattering results. Furthermore, the final product presented a significantly higher content of phenolic compounds and antioxidant activity in comparison with the standard vegan emulsion.

Optimization of Multiple W1/O/W2 Emulsions Processing for Suitable Stability and Encapsulation Efficiency.

Double emulsions are a type of multiple emulsions, which can be defined as a multicompartmentalized system where the droplets are dispersed into the continuous phase containing other emulsions. Although double food-grade emulsions have been manufactured, there is a lack of scientific background related to the influence of different processing conditions. This work analyses the influence of processing variables in (W1/O/W2) double emulsions: passes through the valve homogenizer, pressure applied, lipophilic emulsifier concentration, the ratio between the continuous phase (W2) and the primary emulsion (W1/O), and the incorporation of xanthan gum (XG) as a stabilizer. The results obtained show that these emulsions can be obtained after selecting suitable processing conditions, making them easily scalable in industrial processes. In terms of droplet size distribution, the input of higher energy to the system (20 MPa) during emulsification processing led to emulsions with smaller droplet sizes (D3,2). However, more monodispersed emulsions were achieved when the lowest pressure (5 MPa) was used. As for the number of passes, the optimal (emulsions more monodispersed and smaller droplet sizes) was found around 2-3 passes, regardless of the valve homogenizer pressure. However, emulsions processed at 20 MPa involved lower encapsulation efficiency (EE) than emulsions processed at 5 MPa (87.3 ± 2.3 vs. 96.1 ± 1.8, respectively). The addition of XG led to more structured emulsions, and consequently, their kinetic stability increased. The results obtained indicated that a correct formulation of these W1/O/W2 double emulsions allowed the optimal encapsulation of both hydrophilic and lipophilic bioactive compounds. Thus, the development of food matrices, in the form of multiple emulsions, would allow the encapsulation of bioactive compounds, which would result in the development of novelty food products.

Safety and Efficacy of a Beverage Containing Lupine Protein Hydrolysates on the Immune, Oxidative and Lipid Status in Healthy Subjects: An Intervention Study (the Lupine-1 Trial).

SCOPE: We have previously demonstrated the anti-inflammatory and antioxidant properties of in vitro administered Lupinus angustifolius protein hydrolysates (LPHs) on human peripheral blood mononuclear cells (PBMCs). This study aims to evaluate the safety and efficacy of a beverage containing LPHs (LPHb) on the immune, oxidative and metabolic status of healthy subjects. METHODS AND RESULTS: In this open-label intervention, 33 participants daily ingest a LPHb containing 1 g LPHs for 28 days. Biochemical parameters are assayed in fasting peripheral blood and urine samples before, during (14 days) and after LPHb ingestion. Participants' health status and the immune and antioxidant responses of PBMCs are also evaluated throughout the trial. The LPHb ingestion is safe and effective in both increasing the anti-/pro-inflammatory response of PBMCs and improving the cellular anti-oxidant capacity. LPHb also reduces the low-density lipoprotein-cholesterol (LDL-C)/high-density lipoprotein-cholesterol (HDL-C) atherogenic index. LPHb effect is particularly beneficial on decreasing not only the LDL-C/HDL-C index but also serum total cholesterol levels in the male cohort that shows the highest baseline levels of well-known cardiovascular risk factors. CONCLUSION: This is the first study to show the pleiotropic actions of a lupine bioactive peptides-based functional food on key steps of atherosclerosis including inflammation, oxidative stress, and cholesterol metabolism.

Lupine protein hydrolysates decrease the inflammatory response and improve the oxidative status in human peripheral lymphocytes.

Although cell-free systems and immortalized cell lines have been used to demonstrate the potential health benefits of lupine proteins and peptides, no study has examined the effects of lupine protein hydrolysates (LPHs) on the immune and oxidative responses of non-immortalized human cells. Therefore, the aims of this study were to evaluate the effects of the in vitro administration of LPHs from Lupinus angustifolius on the immunological and oxidative statuses of human peripheral blood mononuclear cells (PBMCs) from 53 healthy donors. LPHs reduced PBMCs proliferation and the levels of Th1, Th9 and Th17 pro-inflammatory cytokines without being cytotoxic. LPHs also skewed the pro-/anti-inflammatory balance towards a Th2 protective response. Additionally, LPHs increased superoxide dismutase and catalase activities, and the total antioxidant capacity (TAC). This study is the first to show that LPHs reduce T cell inflammatory responses and improve the anti-inflammatory/pro-inflammatory cytokine balance and the TAC by PBMCs. Thus, LPHs may represent an effective option for developing nutritional strategies to prevent pathologies with underlying inflammation and oxidative stress.

Interfacial and foaming interactions between casein glycomacropeptide (CMP) and propylene glycol alginate.

Proteins and polysaccharides are widely used in food formulation. While most of the proteins are surface active, only few polysaccharides can adsorb at the air-water interface; this is the case of propylene glycol alginates (PGA). It is known that casein glycomacropeptide (CMP), a bioactive polypeptide derived from κ-casein by the action of chymosin, presents a great foaming capacity but provides unstable foams. So, the objective of this work was to analyze the impact of mixing CMP and a commercial variety of PGA, Kelcoloid O (KO), on the interfacial and foaming properties at pH 7.0. It was determined the surface pressure isotherm, the dynamics of adsorption and the foaming properties for CMP, KO and the mixed system CMP-KO. CMP dominated the surface pressure of CMP-KO mixed system. The presence of KO synergistically improved the viscoelastic properties of surface film. The foaming capacity of CMP was altered by KO. KO foam presented a higher stability than CMP foam and it controlled the stability against drainage and the initial collapse in the mixed foam.

Kinetics of adsorption of whey proteins and hydroxypropyl-methyl-cellulose mixtures at the air-water interface.

The aim of this research is to quantify the competitive adsorption of a whey protein concentrate (WPC) and hydroxypropyl-methyl-cellulose (HPMC so called E4M, E50LV and F4M) at the air-water interface by means of dynamic surface tensiometry and Brewster angle microscopy (BAM). These biopolymers are often used together in many food applications. The concentration of both protein and HPMC, and the WPC/HPMC ratio in the aqueous bulk phase were variables, while pH (7), the ionic strength (0.05 M) and temperature (20 degrees C) were kept constant. The differences observed between mixed systems were in accordance with the relative bulk concentration of these biopolymers (C(HPMC) and C(WPC)) and the molecular structure of HPMC. At short adsorption times, the results show that under conditions where both WPC and HPMC could saturate the air-water interface on their own or when C(HPMC) > or = C(WPC), the polysaccharide dominates the surface. At concentrations where none of the biopolymers was able to saturate the interface, a synergistic behavior was observed for HPMC with lower surface activity (E50LV and F4M), while a competitive adsorption was observed for E4M (the HPMC with the highest surface activity). At long-term adsorption the rate of penetration controls the adsorption of mixed components. The results reflect complex competitive/synergistic phenomena under conditions of thermodynamic compatibility or in the presence of a "depletion mechanism". Finally, the order in which the different components reach the interface will influence the surface composition and the film properties.

Bulk and interfacial behaviour of caseinoglycomacropeptide (GMP).

Caseinoglycomacropeptide (GMP) is a hydrophilic glycopeptide released from milk kappa-casein by chymosin hydrolysis during cheese making. GMP is thought to be a potential ingredient for specific dietary applications with several health benefits. In this study GMP was characterized at the air-water interface and its behaviour was related with the self-assembly of GMP in solution as affected by pH. This GMP self-assembly was investigated by dynamic light scattering and the interfacial properties were determined by tensiometry and surface dilatational measurements at pH 4, 5 and 7. At pH 5 GMP exhibited higher surface pressure at equilibrium than at pH 7. At pH 4 the behaviour was more complex due to self-assembly close to GMP pI. Dynamic measurement showed that the adsorption/penetration rate constant (K(ads)) is facilitated at higher GMP bulk concentrations, while the rate constant of rearrangement (K(r)) decreased at higher GMP concentrations which could be attributed to the existence of a steric restriction due to the higher GMP load at the interface. K(r) was higher at pH 5 because of lower electrostatic interactions close to the pI. The viscoelastic properties showed a complex behaviour due to the existence of protein-protein interactions depending on the GMP concentration, on the pH of the bulk and on the rates of diffusion, adsorption and rearrangement of GMP at the air-water interface.

Implications of interfacial characteristics of food foaming agents in foam formulations.

The manufacture of food dispersions (emulsions and foams) with specific quality attributes depends on the selection of the most appropriate raw materials and processing conditions. These dispersions being thermodynamically unstable require the use of emulsifiers (proteins, lipids, phospholipids, surfactants etc.). Emulsifiers typically coexist in the interfacial layer with specific functions in the processing and properties of the final product. The optimum use of emulsifiers depends on our knowledge of their interfacial physico-chemical characteristics - such as surface activity, amount adsorbed, structure, thickness, topography, ability to desorb (stability), lateral mobility, interactions between adsorbed molecules, ability to change conformation, interfacial rheological properties, etc. -, the kinetics of film formation and other associated physico-chemical properties at fluid interfaces. These monolayers constitute well defined systems for the analysis of food colloids at the micro- and nano-scale level, with several advantages for fundamental studies. In the present review we are concerned with the analysis of physico-chemical properties of emulsifier films at fluid interfaces in relation to foaming. Information about the above properties would be very helpful in the prediction of optimised formulations for food foams. We concluded that at surface pressures lower than that of monolayer saturation the foaming capacity is low, or even zero. A close relationship was observed between foaming capacity and the rate of diffusion of the foaming agent to the air-water interface. However, the foam stability correlates with the properties of the film at long-term adsorption.

Structural and shear characteristics of adsorbed sodium caseinate and monoglyceride mixed monolayers at the air-water interface.

The structural and shear characteristics of mixed monolayers formed by an adsorbed Na-caseinate film and a spread monoglyceride (monopalmitin or monoolein) on the previously adsorbed protein film have been analyzed. Measurements of the surface pressure (pi)-area (A) isotherm and surface shear viscosity (eta(s)) were obtained at 20 degrees C and at pH 7 in a modified Wilhelmy-type film balance. The structural and shear characteristics of the mixed films depend on the surface pressure and on the composition of the mixed film. At surface pressures lower than the equilibrium surface pressure of Na-caseinate (at pipi(e)(CS) have important repercussions on the shear characteristics of the mixed films.

Limited enzymatic hydrolysis can improve the interfacial and foaming characteristics of beta-conglycinin.

In this contribution, we have determined the effect of limited enzymatic hydrolysis on the interfacial (dynamics of adsorption and surface dilatational properties) and foaming (foam formation and stabilization) characteristics of a soy globulin (beta-conglycinin, fraction 7S). The degree of hydrolysis (DH = 0, 2, and 5%), the pH of the aqueous solution (pH = 5 and 7), and the protein concentration in solution (at 0.1, 0.5, and 1 wt %) were the variables studied. The temperature and the ionic strength were maintained constant at 20 degrees C and 0.05 M, respectively. The rate of adsorption and surface dilatational properties (surface dilatational modulus, E, and loss angle) of beta-conglycinin at the air-water interface depend on the pH and DH. The adsorption decreased drastically at pH 5.0, close to the isoelectric point of beta-conglycinin, because of the existence of a lag period and a low rate of diffusion. The interfacial characteristics of beta-conglycinin are much improved by enzymatic treatment, especially in the case of acidic aqueous solutions. Hydrolysates with a low DH have improved functional properties (mainly foaming capacity and foam stability), especially at pH values close to the isoelectric point (pI), because the protein is more difficult to convert into a film at fluid interfaces at pH approximately equal to pI.

Spreading of monoglycerides onto beta-casein adsorbed film. Structural and dilatational characteristics.

The effect of monoglycerides (monopalmitin and monoolein) on the structural, topographical, and dilatational characteristics of betacasein adsorbed film at the air-water interface has been analyzed by means of surface pressure (pi)-area (A) isotherms, Brewster angle microscopy (BAM), and surface dilatational rheology. The static and dynamic characteristics of the mixed films depend on the interfacial composition and the surface pressure. At surface pressures lower than that for the beta-casein collapse (at the equilibrium surface pressure of the protein, pi(e)(beta-casein)) a mixed film of beta-casein and monoglyceride may exist. At higher surface pressures the collapsed beta-casein is partially displaced from the interface by monoglycerides. However, beta-casein displacement by monoglycerides is not quantitative at the monoglyceride concentrations studied in this work. The protein displacement by a monoglyceride is higher for monopalmitin than for monoolein and for spread than for adsorbed films. The viscoelastic characteristics of the mixed films were dominated by the presence of beta-casein in the mixture. Even at the higher surface pressures (at pi > pi(e)(beta-casein)) the small amounts of beta-casein collapsed residues at the interface have a significant effect on the surface dilatational properties of the mixed films. The structural, topographical, and viscoelastic characteristics of the mixed films corroborate the fact that protein displacement for monoglycerides is higher for spread than for adsorbed mixed films.

Shear characteristics, miscibility, and topography of sodium caseinate-monoglyceride mixed films at the air-water interface.

In this contribution, we are concerned with the study of structure, topography, and surface rheological characteristics (under shear conditions) of mixed sodium caseinate and monoglycerides (monopalmitin and monoolein) at the air/water interface. Combined surface chemistry (surface film balance and surface shear rheometry) and microscopy (Brewster angle microscopy, BAM) techniques have been applied in this study to mixtures of insoluble lipids and sodium caseinate spread at the air-water interface. At a macroscopic level, sodium caseinate and monoglycerides form an heterogeneous and practically immiscible monolayer at the air-water interface. The images from BAM show segregated protein and monoglyceride domains that have different topography. At surface pressures higher than that for the sodium caseinate collapse, this protein is displaced from the interface by monoglycerides. These results and those derived from interfacial shear rheology (at a macroscopic level) appear to support the idea that immiscibility and heterogeneity of these emulsifiers at the interface have important repercussions on the shear characteristics of the mixed films, with the alternating flow of segregated monoglyceride domains (of low surface shear viscosity, etas) and protein domains (of high etas) across the canal.

Surface shear rheology of WPI-monoglyceride mixed films spread at the air-water interface.

Surface shear viscosity of food emulsifiers may contribute appreciably to the long-term stability of food dispersions (emulsions and foams). In this work we have analyzed the structural, topographical, and shear characteristics of a whey protein isolate (WPI) and monoglyceride (monopalmitin and monoolein) mixed films spread on the air-water interface at pH 7 and at 20 degrees C. The surface shear viscosity (etas) depend on the surface pressure and on the composition of the mixed film. The surface shear viscosity varies greatly with the surface pressure. In general, the greater the surface pressure, the greater are the values of etas. The values of etas for the mixed WPI-monoolein monolayer were more than one order of magnitude lower than those for a WPI-monopalmitin mixed film, especially at the higher surface pressures. At higher surface pressures, collapsed WPI residues may be displaced from the interface by monoglyceride molecules with important repercussions on the shear characteristics of the mixed films. A shear-induced change in the topography and a segregation between domains of the film forming components were also observed. The displacement of the WPI by the monoglycerides is facilitates under shear conditions, especially for WPI-monoolein mixed films.

Dynamic properties of soy globulin adsorbed films at the air-water interface.

In this paper we present surface dilatational properties of soy globulins (beta-conglycinin, glycinin, and reduced glycinin with 10 mM of dithiothreitol (DTT)) adsorbed onto the air-water interface, as a function of adsorption time. The experiments were performed at constant temperature (20 degrees C), pH (8.0), and ionic strength (0.05 M). The surface rheological parameters were measured as a function of protein concentration (ranging from 1 to 1x10(-3)% wt/wt). We found that the surface dilatational modulus, E, increases, and the phase angle, phi, decreases with time, theta, which may be associated with protein adsorption. These phenomena have been related to protein adsorption, unfolding, and/or protein-protein interactions (at long-term adsorption) as a function of protein concentration in solution. From a rheological point of view, the surface viscoelastic characteristics of soy globulin films adsorbed at the air-water interface are practically elastic. The main conclusion is that the dilatational properties of the adsorbed films depend on the molecular structure of the protein.

Structure, miscibility, and rheological characteristics of beta-casein-monoglyceride mixed films at the air-water interface.

In this work we have used different and complementary interfacial techniques (surface film balance, Brewster angle microscopy, and interfacial dilatational rheology) to analyze the static (structure, morphology, reflectivity, miscibility, and interactions) and dynamic characteristics (surface dilatational properties) of beta-casein and monoglyceride (monopalmitin and monoolein) mixed films spread on the air-water interface. The static and dynamic characteristics of the mixed films depend on the interfacial composition and the surface pressure. At higher surface pressures, collapsed beta-casein residues may be displaced from the interface by monoglyceride molecules with important repercussions on the interfacial characteristics of the mixed films. From the frequency dependence of the surface dilatational properties, we have elucidated the relationships between interfacial dilatational rheology and changes in molecular structure, interactions, miscibility, and relaxation phenomena in protein-monoglyceride mixed films.

The Effect of pH on Monoglyceride-Caseinate Mixed Monolayers at the Air-Water Interface.

The surface pressure (pi) area (A) isotherms and Brewster angle microscopy (BAM) of monoglyceride-caseinate mixed films spread on buffered water at pH 5 and 7 and at 20 degrees C were determined as a function of the mass fraction (X) of monoglyceride (monopalmitin or monoolein) in the mixture. The structural characteristics, miscibility, and morphology of monoglyceride-caseinate mixed films are very dependent on surface pressure and monolayer composition. The monolayer structure was more expanded as the pH and the monoglyceride concentration in the mixture were increased. From the concentration and surface pressure dependence on excess area, free energy, and collapse pressure, it was deduced that, at a macroscopic level, monoglyceride (either monopalmitin or monoolein) and caseinate form a practically immiscible monolayer at the air-water interface. The BAM images and the evolution with the surface pressure of the relative reflectivity of BAM images give complementary information on the interactions and structural characteristics of monoglyceride-caseinate mixed monolayers, which at a microscopic level corroborated in part the conclusions derived from the pi-A isotherm at a macroscopic level. Over the overall range of existence of the mixed film the monolayer presents some heterogeneity due to the fact that domains of monoglyceride (especially of monopalmitin) and spots of collapsed caseinate residues are present during the monolayer compression-expansion cycle, giving relative intensity peaks with high relative film thickness. At higher pi, after the caseinate collapse, characteristic squeezing-out phenomenon was observed. At the monoglyceride monolayer collapse the mixed film is practically dominated by the presence of monoglyceride. The prevalence of monoglyceride in the interface increases with the amount of monoglyceride in the mixture and at higher pi. However, some degree of interactions exists between monoglyceride and caseinate in the mixed film and these interactions are more pronounced as the monolayer is compressed at the highest surface pressures. Copyright 2001 Academic Press.