Faba Bean Protein Research Articles

Heat induced gelation of pulse protein networks

This study examines the effect of salts (0.5 M NaCl or 0.25 M CaCl2) and protein concentration (7.5–15%) on the gel-forming abilities of lentil (LPC), yellow pea (YPC), and faba bean (FPC) protein concentrates formed at pH 7.0. The surface hydrophobicity of YPC (84.8 arbitrary units, a.u.) was found to be lower than LPC (147.2 a.u.) and FPC (135.0 a.u.). In contrast, the surface charge for LPC, YPC, and FPC was −37.8, −28.4, and −29.3 mV, respectively. The Lg/Vn ratio of YPCs was determined as 0.65 followed by LPC (0.57) and FPC (0.41). The presence of salts reduced the least gelling concentration. LPC and FPC also appeared to have a more ordered structure than YPC as evident by CLSM. The network appeared more ordered as the protein concentration increased or in the presence of NaCl or CaCl2 according to CLSM and synchrotron based micro computed tomography (µCT).

Prediction of emulsification behaviour of pea and faba bean protein concentrates and isolates from structure-functionality analysis.

The effects of different extraction methods on the structure–functionality and emulsification behaviour of pea and faba bean protein isolates, and concentrates were studied at pH 7 and 2, and a regression model was developed to predict emulsion characteristics based on protein properties. The concentrates produced by air classification had lower protein content but higher solubility in water compared to the isolates produced by isoelectric precipitation. The protein secondary structure did not show a consistent difference; however, much higher intrinsic fluorescence was observed for the soluble compared to the insoluble fractions. Interfacial tension of all faba proteins was lower than pea, while there was no significant difference between the concentrates and isolates. The higher protein content of the isolates was found to improve their water holding capacity. Canola oil (40 wt%)-in-water coarse emulsions, prepared with 2 wt% proteins and 0.25 wt% xanthan gum showed smaller particle size at pH 7 than pH 2, while the zeta potential, viscosity and gel strength were higher at pH 7. Emulsions stabilized with concentrates were better or comparable to the isolates in terms of particle size, zeta potential, and microstructure. The regression model predicted that an increase in solubility, intrinsic fluorescence, water and oil holding capacities are more favourable to decrease emulsion particle size, while an increase in solubility, intrinsic fluorescence would lead to higher emulsion destabilization. A decrease in interfacial tension was more favourable to lower destabilization. Emulsion viscosity was more dependent on water holding capacity compared to any other factor. Such models could be extremely beneficial for the food industry to modulate processing for the development of desired pulse protein ingredients.

The effect of heat and transglutaminase treatment on emulsifying and gelling properties of faba bean protein isolate

The effects of heat treatment (90 °C, 5 or 30 min) and enzymatic crosslinking with transglutaminase (TG, 10, 100 or 1000 nkat/g protein) on emulsifying and gelling properties of faba bean protein isolate (FPI) were studied. Heat treatment of FPI caused a clear shift in far-UV CD spectra towards random coil structure and an increase in surface hydrophobicity from 181 to 504 RFU. TG crosslinked heat-treated FPI more efficiently as compared to native FPI. TG-induced crosslinking caused a reduction of surface hydrophobicity from 504 to 435 RFU. Emulsifying activity and stability indexes of FPI stabilized emulsions ranged between 25 and 30 m2/g and 18–35 min, respectively. Rheological properties of the FPI gels induced by heating, followed by acidification or TG treatment (10 or 100 nkat/g protein) were analyzed. FPI showed gel-like characteristics at 10% concentration (G′ = 180 Pa). When the heat-treated FPI dispersion was further acidified or TG-treated (100 nkat/g), G′ values of >6500 and > 3500 Pa were achieved, respectively. Water holding capacity of the FPI gels were >93% and >98% for acid- and TG-induced gels, respectively. The gel microstructures showed mainly heterogeneously-sized protein aggregates, however, no differences were observed between acid- and TG-induced gels.

The Effect of Addition of High‐Melting Monoacylglycerol and Candelilla Wax on Pea and Faba Bean Protein Foam‐Templated Oleogelation

AbstractUse of oleogels prepared from hydrocolloids has recently gained considerable attention as an alternative for trans and saturated fats. Lately, pulse proteins such as faba bean protein and pea protein have been successfully used to prepare oleogels using a foam‐templated approach. Although the pulse proteins are healthy oleogelators, high oil loss and low quality of cake baked using pulse protein‐stabilized oleogels due to its poor rheological properties challenged its use. The present study explored whether the addition of small amount of high‐melting monoglyceride (MAG) or candelilla wax (CW) can be used to improve the oil binding capacity, rheological properties, and baking qualities of pulse protein‐stabilized oleogels composed of 5% faba bean or pea protein concentrate with 0.25% xanthan gum foams. Different concentrations (0.5–3%) of MAG or CW were dissolved in canola oil at 80 °C, followed by addition into the freeze‐dried protein‐polysaccharide foams (pH 7) and quickly transferred to a refrigerator to facilitate the formation of oleogels. The crystallized additives were found to be reinforcing the protein foam network in the oleogels. With increase in concentration of CW and MAG, the oil binding capacity, firmness, cohesiveness, and storage moduli of the oleogels were increased. Oleogels with and without MAG or CW were then characterized and tested for their performance as a shortening replacer in model baked cakes. Findings showed improved textural properties of cake upon addition of MAG in the foam‐templated oleogels, however, compared to the shortening, negative effect on cake hardness and chewiness was still observed with the oleogels.

Consequences of heating under alkaline pH alone or in the presence of maltodextrin on solubility, emulsifying and foaming properties of faba bean protein

Faba bean (Vicia faba L.) has attracted interest as a source of plant proteins due to the high protein content, easy cultivation, and the excellent nitrogen-fixing capacity. However, application of faba bean protein is still negligible in food products primarily due to its low solubility and functionality. In the current study, impact of heating under alkaline pH (11.0) alone or in the presence of maltodextrin on physicochemical characteristics, solubility, emulsifying activity, and foaming properties of faba bean protein isolate powder (FBP) from a pilot processing was investigated. Heating at alkaline pH irreversibly disrupted the original large micron-sized aggregates in untreated FBP, along with formation of the smaller aggregates with higher surface hydrophobicity. In the presence of maltodextrin, a FBP-maltodextrin conjugate with high degree of glycation was formed by the heating at alkaline pH. The heating under alkaline pH either in the presence and absence of maltodextrin significantly improved the protein solubility from 43, 14, and 35% at pH 3.0, 6.0, and 7.0, respectively to more than 90%. Compared to the untreated FBP, the FBP-maltodextrin sample heated at pH 11.0 could produce emulsions that were stable against flocculation and phase separation for 15 days storage at pH 6–7 or in the presence of salt. Moreover, foaming capacity and stability of the FBP and FBP-maltodextrin samples heated at pH 11.0 was greatly improved. This study suggested that heating under alkaline pH has a great potential to improve the functional properties of FBP to enable its wide applications in food area.

A Novel Approach to Structure Plant-Based Yogurts Using High Pressure Processing.

Current plant-based yogurts are made by the fermentation of plant-based milks. Although this imparts fermented flavors and probiotic cultures, the process is relatively longer and often leads to textural issues. The protein content of these plant-based yogurts is also lower than their dairy counterparts. To overcome these challenges, this paper explores the high pressure processing (HPP) of plant protein ingredients as an alternative structuring strategy for plant-based yogurts. Using mung bean (MB), chickpea (CP), pea (PP), lentil (LP), and faba bean (FB) proteins as examples, this work compared the viscosity and viscoelastic properties of high pressure-structured (600 MPa, 5 min, 5 °C) 12% (w/w) plant protein gels without, and with 5% (w/w) sunflower oil (SO) to commercial plain skim and whole milk Greek yogurts and discussed the feasibility of using HPP to develop plant-based yogurts. HPP formed viscoelastic gels (G’ > G’’) for all plant protein samples with comparable gel strength (G’~102–103 Pa; tan δ~0.2–0.3) to commercial dairy yogurts. The plant protein gel strength decreased in the order: CP~CPSO~LP~LPSO > MBSO~PPSO~FB~FBSO > PP >> MB. Modest addition of sunflower oil led to little change in viscoelastic properties for all plant protein samples except for MB and PP, where gel strength increased with incorporated oil. The emulsion gels were also more viscous than the hydrogels. Nonetheless, the viscosity of the plant protein gels was similar to the dairy yogurts. Finally, a process involving separate biotransformation for optimized flavor production and high pressure processing for consistent texture generation was proposed. This could lead to high protein plant-based yogurt products with desirable texture, flavor, and nutrition.

Modifying Faba Bean Protein Concentrate Using Dry Heat to Increase Water Holding Capacity.

We investigated the effect of dry-heat treatment on the properties of faba bean protein concentrate using soy protein concentrate as a benchmark. While soy protein—widely used as an ingredient in meat replacers—is recovered through a wet fractionation, protein recovery from starch bearing pulses like faba bean can be done via dry fractionation. This process does not require drying or heating steps and therefore, keeps the original protein functionality intact. This results in differences in properties such as water binding capacity of the protein fraction. Faba bean protein concentrate was dry-heated at temperatures from 75–175 °C, which resulted in higher water-holding capacity and less soluble protein, approaching values of soy protein concentrate. These changes were due to partial denaturation of protein, changing the structure of the protein, and exposing hydrophobic sites. This led to protein aggregation, as observed by light microscopy. Only noncovalent bonds caused the decrease of solubility of dry-heated faba bean protein concentrate. We conclude that dry-heating of dry fractionated faba bean protein can change the functional properties of the protein fraction to desired properties for certain applications. The effect is similar to that on soy, but the underlying mechanisms differ.

Use of precision-fed cecectomized rooster assay and digestible indispensable amino acid scores to characterize plant- and yeast-concentrated proteins for inclusion in canine and feline diets.

Increased consumer interest in high-quality and novel protein sources has driven the demand for the inclusion of protein-rich ingredients in companion animal diets. Novel protein concentrates, with protein contents of at least 50%, have been used to satisfy these consumer demands. However, minimal information is available regarding the macronutrient composition and protein quality of these ingredients that is needed for proper formulation of pet foods. Therefore, the objectives of this study were to determine the macronutrient and amino acid compositions, standardized amino acid digestibility according to the precision-fed rooster assay, and protein quality using digestible indispensable amino acid score (DIAAS like) of pea protein (PP), potato protein (POP), faba bean protein (FBP), soy protein concentrate (SPC), and dried yeast (DY). Precision-fed rooster assays were conducted using cecectomized roosters to calculate standardized amino acid digestibility and true metabolizable energy corrected for nitrogen (TMEn). For all five protein concentrates, all essential amino acids were highly digestible (88.0% to 96.3%, dry matter basis) with differences (P < 0.05) in only lysine, methionine, and tryptophan digestibilities. The TMEn values were highest for POP (4.22 kcal/g) and DY (3.61 kcal/g). The DIAAS-like values for adult dogs indicated that methionine was the first-limiting amino acid in all protein concentrates except POP, where the first-limiting amino acid was tryptophan. Using Association of American Feed Control Officials (AAFCO)-recommended values for adult cats, DIAAS-like values for methionine were lowest (P < 0.05) for FBP at 81.5%, with all other amino acids for all protein concentrates over 100%. The National Research Council (NRC)-recommended allowances for adult cats indicated that DIAAS-like methionine values for PP (92.7%) and FBP (73.8%) were significantly lower (P < 0.05) with these being the first-limiting amino acids, with the remaining amino acids above 100% for the other protein concentrates. The protein quality and high essential amino acid digestibility of these protein concentrates indicate that they would be viable protein sources in canine and feline diets. However, additional complementary protein sources should be included to meet the requirements of all essential amino acids.

EVALUATION OF FOAM-MAT DRYING BEHAVIOUR OF CRAB APPLE (MALUS FLORIBUNDA) FRUIT JUICE AND POWDER QUALITY

Malus floribunda (MF) is an ornamental plant and the fruits with its red flesh have potential to be used as natural food colorant. In this study, the effects of faba bean protein concentrate (FB) and maltodextrin (MD) levels on MF juice foam stability was evaluated. In addition, the effects of drying conditions (temperature/power) on drying kinetics and powder quality (powder flow properties, colour, and anthocyanin content) were determined. The foam stability was significantly dependent on the FB level (P &amp;lt;0.05), but MD addition didn’t have any significant effect (P &amp;gt;0.05). Drying period was reduced with foam-mat drying compared to control, and the average Carr index values were found between 17.3-26.0%, while the Hausner ratios were between 1.21-1.35. The redness and lightness values of foam-mat dried powders were comparably higher than the control and MD-added sample at every drying condition (P &amp;lt;0.05), although the anthocyanin content decreased with increasing drying temperatures.

Preparation and Characterization of Emulsion Gels from Whole Faba Bean Flour.

Faba bean protein has good functionalities, but it is little used in the food industry. This study identified a challenge from unfavourable starch gelation when utilizing faba bean for producing protein-based emulsion gel foods, and developed processing methods to overcome that. Two types of protein-based emulsion gel foods, namely yogurt and tofu analogue products, were prepared. The processing methods in this study involved steps of thermal pre-treatment of the beans, dehulling, milling, adding plant oil, homogenization, prevention of starch gelation, and inducing protein gelation. Two methods for preventing starch gelation were studied, namely starch removal and hydrolysis. The gel texture, water-holding capacity, and structural properties of the gel products were evaluated. Both starch-gelation prevention methods produced yogurt and tofu analogue products having typical emulsion gel properties. Hydrolysis of starch was favourable for producing the yogurt analogue, because the hydrolysate compounds improved the gel strength and viscosity. Moreover, it utilized the whole flour, meaning all the nutrients from the cotyledon were used and no side-stream was created. In contrast, starch removal was slightly better than hydrolysis for producing the tofu analogue, because the hydrolysate lowered the gel strength and water-holding capacity of the products. It is both possible and ecologically sustainable to utilize whole faba bean flour for making emulsion gel products.

Effect of thermal processing on cholesterol synthesis, solubilisation into micelles and antioxidant activities using peptides of Vigna angularis and Vicia faba

Bioactive peptides are generally obtained from plant protein hydrolysates. These peptides possess physiological activities, such as lowering blood cholesterol. In the current study, proteins from adzuki bean (Vigna angularis) and faba bean (Vicia faba) were thermally processed, and low molecular weight peptides (<3 kDa) were isolated to assess their efficacy for inhibiting cholesterol synthesis and its solubilisation. High-performance liquid chromatography (HPLC) results showed higher peptide concentrations after thermal processing. Inhibition of cholesterol solubilisation into micelles and 3-hydroxy-3-methylglutaryl coenzyme-A reductase (HMG Co-AR) catalytic activity was evaluated. After processing, the faba bean peptides showed significantly (p < 0.05) increased inhibition of cholesterol solubilisation into micelles (45.1 ± 1.6%), whereas peptides from the native faba bean protein exhibited significantly increased (p < 0.05) inhibition of HMG Co-AR catalytic activity (84.1 ± 2.7%) compared with the adzuki bean and thermally processed peptides. After processing, the adzuki bean peptides showed significantly reduced scavenging activity compared with peptides obtained from the native protein. This study is the first report demonstrating that the peptides from adzuki and faba beans inhibit cholesterol homeostasis via distinctive ways and act as antioxidants.

Are Faba Bean and Pea Proteins Potential Whey Protein Substitutes in Infant Formulas? An In Vitro Dynamic Digestion Approach.

Infant formulas (IFs) are used as substitutes for human milk and are mostly based on cow milk proteins. For sustainability reasons, animal protein alternatives in food are increasingly being considered, as plant proteins offer interesting nutritional and functional benefits for the development of innovative IFs. This study aimed to assess how a partial substitution (50%) of dairy proteins with faba bean and pea proteins influenced the digestibility of IFs under simulated dynamic in vitro digestion, which were set up to mimic infant digestion. Pea- and faba bean-based IFs (PIF and FIF, respectively) have led to a faster aggregation than the reference milk-based IF (RIF) in the gastric compartment; that did not affect the digesta microstructure at the end of digestion. The extent of proteolysis was estimated via the hydrolysis degree, which was the highest for FIF (73%) and the lowest for RIF (50%). Finally, it was apparent that in vitro protein digestibility and protein digestibility-corrected amino acid score (PDCAAS)-like scores were similar for RIF and FIF (90% digestibility; 75% PDCAAS), but lower for PIF (75%; 67%). Therefore, this study confirms that faba bean proteins could be a good candidate for partial substitution of whey proteins in IFs from a nutritional point of view, provided that these in vitro results are confirmed in vivo.

Comparison of Faba Bean Protein Ingredients Produced Using Dry Fractionation and Isoelectric Precipitation: Techno-Functional, Nutritional and Environmental Performance.

Dry fractionated faba bean protein-rich flour (FPR) produced by milling/air classification, and faba bean protein isolate (FPI) produced by acid extraction/isoelectric precipitation were compared in terms of composition, techno-functional properties, nutritional properties and environmental impacts. FPR had a lower protein content (64.1%, dry matter (DM)) compared to FPI (90.1%, DM), due to the inherent limitations of air classification. Of the two ingredients, FPR demonstrated superior functionality, including higher protein solubility (85%), compared to FPI (32%) at pH 7. Foaming capacity was higher for FPR, although foam stability was similar for both ingredients. FPR had greater gelling ability compared to FPI. The higher carbohydrate content of FPR may have contributed to this difference. An amino acid (AA) analysis revealed that both ingredients were low in sulfur-containing AAs, with FPR having a slightly higher level than FPI. The potential nutritional benefits of the aqueous process compared to the dry process used in this study were apparent in the higher in vitro protein digestibility (IVPD) and lower trypsin inhibitor activity (TIA) in FPI compared to FPR. Additionally, vicine/convicine were detected in FPR, but not in FPI. Furthermore, much lower levels of fermentable oligo-, di- and monosaccharides, and polyols (FODMAPs) were found in FPI compared to FPR. The life cycle assessment (LCA) revealed a lower environmental impact for FPR, partly due to the extra water and energy required for aqueous processing. However, in a comparison with cow’s milk protein, both FPR and FPI were shown to have considerably lower environmental impacts.

Utilization of pulse protein-xanthan gum complexes for foam stabilization: The effect of protein concentrate and isolate at various pH

The present study examines the foaming behavior of pea and faba bean protein concentrates and isolates and explores the impact of pH and protein-polysaccharide complexation on overrun and foam stability. Foams were prepared with 5 wt% proteins with and without 0.25 wt% xanthan gum (XG) at pH 3, 5, 7 and 9. Most foams were unstable without XG. With XG foaming properties of protein concentrates were better than isolates. Irrespective of protein type and content, all protein-XG foams at pH 3 destabilized due to large insoluble complexes, however, at pH 5 foams were stable due to smaller size of insoluble complexes. Both the protein concentrate-XG foams were stable at pH 7 and 9 due to optimum viscosity and surface tension of the soluble complexes. Overall, the study revealed that the overrun and stability of pulse protein foams can be significantly improved by adding XG and controlling their intermolecular interactions as a function of pH.

Faba bean protein in reduced fat/cholesterol mayonnaise: extraction and physico-chemical modification process.

Effect of faba bean enzymatic protein extraction process parameters were investigated at different ultrasound powers (200, 300 and 400W), sonication times (15, 25 and 35min), enzyme dosages (0.15, 0.3 and 0.45%) and enzyme treatment times (15, 25 and 35min). Physico-functional characterization of the protein samples through solubility, zeta potential, color, fat adsorption, emulsifying and foaming capacity measurements suggested faba protein as a promising substituent to egg yolk powder in reduced fat mayonnaise formulation. Reduced-fat mayonnaise formulation containing different faba protein/egg yolk powder ratios were prepared and characterized through rheological analyses as well as emulsion stability, texture, color and microstructural evaluations. The formulations containing equal compositions of faba bean protein and egg yolk powder (0.375%) and also the one with 0.5% faba bean protein and 0.25% egg yolk powder were finally suggested to substitute the conventional formulation.

Actividades antioxidante e inhibitoria de la ECA de hidrolizados obtenidos a partir de proteínas de lupino y haba mediante hidrólisis enzimática y fermentación

Introduction: Legumes and pseudocereals protein hydrolysates have been recognized as having improved potential health-promoting properties as compared with native proteins. Objectives: 1) Produce bioactive hydrolysates from lupin and faba bean proteins by enzymatic hydrolysis (EH) and solid-state fermentation (SF), 2) compare the angiotensin converting enzyme (ACE)-inhibitory and antioxidant activities of the hydrolysates and 3) evaluate the effect of in vitro gastrointestinal digestion on the antioxidant and antihypertensive activities of the hydrolysates. Methodology: Hydrolysates from proteins of faba bean (Vicia faba) and lupin (Lupinus gredensis) were obtained by EH using Flavourzyme and SF by Aspergillus niger. The antioxidant and ACE-inhibitory activities of the hydrolysates were assessed. Results: All the hydrolysates presented DPPH radical scavenging activity, with IC50 ranging from 1.23-2.08 mgprotein·mL-1. Only EH and SF hydrolysates obtained from lupin proteins had ACE-inhibitory activity (IC50: 2.39 and 14.08 mgprotein·mL-1, respectively). Radical scavenging activity hydrolysates was significantly reduced after in vitro gastrointestinal digestion, while ACE-inhibitory activity showed variable behavior. Study limitations: Specific molecules responsible for the in vitro health-promoting properties should be identified. Originality: Relevant information is provided on health-promoting attributes of faba bean and lupin hydrolysates obtained by EH and SF. Conclusions: EH and SF improved the health-promoting properties of faba bean and lupin native proteins.

Gelation of faba bean proteins - Effect of extraction method, pH and NaCl

The effect of extraction method, pH and NaCl addition on rheological properties and microstructure of heat-induced faba bean protein gels was evaluated. Gels formed at pH 7 (no NaCl) of alkaline-extracted protein had the densest and finest network structure and highest stress and strain at fracture. The high density of nodes and small pores in the protein network could contribute to those mechanical properties. In contrast, storage modulus (G′) and Young's modulus were lowest for protein gels at pH 7. The gels formed at pH 5 had high G′ and Young's modulus, whereas stress and strain at fracture were lower, especially for gels formed from alkaline-extracted protein. Gels formed at pH 5 with 2% NaCl had two types of internal gel network, caused by a change in solubility of 7S globulins. When the protein powder was dissolved in water, particle size was dependent on the extraction method, with alkaline extraction giving much larger protein particles than soaked extraction.

Assembling of the interfacial layer affects the physical and oxidative stability of faba bean protein-stabilized oil-in-water emulsions with chitosan

This study investigated how different ways of assembling of faba bean protein isolate (FBPI) and chitosan (CH) affected the oil-in-water emulsion stability. Emulsions were prepared either by a soluble FBPI-CH complex to make EMC, or by FBPI first and then added non-interactive CH to make EMN, or by FBPI first and then added a secondary layer of CH via electrostatic attraction to make EML. A control emulsion EMFB was prepared by only FBPI. All emulsions contained 5% (w/v) oil and 0.5% (w/v) FBPI. EMC/EML/EMN contained 0.05% (w/v) CH. The emulsion stability was monitored at 37 °C for 7 days. EML not only showed better physical stability as indicated by the changes in droplet size, Turbiscan stability index, and microstructure (by confocal microscopy), but also exhibited superior oxidative stability as indicated by lipid oxidation products (less conjugated dienes and secondary oxidation products) and protein oxidation biomarkers (less tryptophan loss and carbonyls formation). This might be attributed to that CH enhanced formation of a layer-by-layer (LBL) interfacial structure, which increased the interfacial layer thickness/compactness and maintained the interfacial protein adsorption. In contrast, EMC demonstrated worse stability, albeit with thicker interfacial layer due to CH. This could be explained by the lower surface hydrophobicity and surface charge of soluble FBPI-CH complex. The free aqueous CH also impaired physical stability and promoted oxidation, as shown in EMN. In conclusion, CH improves the oxidative and physical stability of FBPI-containing emulsion when added as a LBL model.

In vitro static digestion reveals how plant proteins modulate model infant formula digestibility.

Infant formulas (IFs) are the key nutritional source for infants who cannot be breastfed. There is currently a growing interest in these sensitive products in order to control their quality and to design their composition with regard to nutritional balance. In a context of sustainable development and increasing growth of the world population, it seems essential to search for alternative to animal protein in food today. Plant proteins offer interesting nutritional and functional benefits thanks to the latest improvement through research and development. In this context, five model IFs were developed with identical composition, except that 50% of the proteins were either whey proteins in the "milk-reference IF", pea, faba bean, rice or potato proteins in the four "plant IFs" tested. The IFs were evaluated using an in vitro static gastro-intestinal model simulating infant conditions. The protein hydrolysis degree (DH) and the amino acid bioaccessibility (AAB) were used as indicators of protein digestibility. Results showed that both DH and AAB were very similar between the milk-reference IF, pea and faba bean IFs, but significantly lower for the rice and potato IFs. This study provides new insights into the impact of protein sources on IF digestibility.

Plant proteins partially replacing dairy proteins greatly influence infant formula functionalities

Infant formulas (IFs) can be defined as substitutes for human milk, which are mostly based on cow milk proteins. For sustainability reasons, alternative to animal proteins in food have to be considered. Plant proteins offer interesting nutritional and functional benefits for the development of innovative IFs. However, the behaviour of these proteins during processing and storage must ensure the physical stability and ability to reconstitution of IF powders, and that needs to be tested. This work aimed to study how a partial substitution of dairy proteins by plant proteins may influence the functional properties of 1st age IFs. Three IFs were developed at a semi-industrial scale using two different processing routes. The IFs composition was identical, except that 50% of the proteins were whey proteins in the “reference IF” (RIF), and pea or faba bean proteins in the “plant IFs” (PIF and FIF, respectively). After reconstitution, the three IFs result in similar stable emulsions with equivalent free fat release. In comparison to RIF, PIF and FIF were difficult to disperse, conducting to remaining insoluble particles. Thus, the protein source greatly influences IFs properties, and process parameters need to be adapted for each formulation to meet IFs quality criteria.