Pea protein isolates used in protein-rich foods are typically produced by alkaline extraction and isoelectric precipitation and undergo thermal treatments that can modify protein structure, aggregation, and functionality. This study examines the calcium-binding capacity of heat-denatured pea globulins and the colloidal behavior of the resulting calcium–protein complexes. Protein dispersions ( 2

Plant proteins exhibit wide variability in emulsifying behavior due to differences in composition, molecular structure, and processing history. This study investigated the relationship between intrinsic physicochemical properties and emulsifying behavior of eleven commercial protein isolates and concentrates derived from bovine milk, soy, canola, faba bean and pea. Key properties including solubility, surface hydrophobicity (SH), molecular weight distribution (MWD), and zeta-potential of the protein ingredients were characterized and evaluated in relation to emulsion droplet size. Among these parameters, MWD showed a moderate correlation with emulsion droplet size (R² = 0.64), while SH and zeta potential exhibited no meaningful correlation (R² < 0.1). When MWD and SH were evaluated together, a clearer trend and separation emerged. Plant proteins with both high molecular weight and low surface hydrophobicity showed a tendency to form heavily flocculated emulsions. This flocculation likely resulted from slower interfacial adsorption and incomplete surface coverage, leading to droplet flocculation at early stages of emulsification. Under a specific set of formulation and processing conditions, emulsions prepared with alkaline-extracted pea and faba protein had smaller droplet size than their air-classified counterparts, likely due to their lower MWD and modified interfacial behavior induced by alkaline treatment. These findings show that the combination of MWD and SH could be useful in understanding the emulsifying behavior of commercial plant protein ingredients and helping in the screening and formulation of plant protein ingredients for food and beverage applications.

Faba bean ingredients are rich in proteins and good sources of calcium (Ca), although containing phytic acid (PA) molecules. PA, a polyphosphate compound, can affect the bioavailability of minerals/proteins through complex formation. This study evaluates the impact of two extraction processes, Alkaline Extraction-IsoElectric Precipitation (AE-IEP) and Sequential Extraction (SE), on the ability of faba bean globulin systems to bind added calcium ions. Increasing concentrations of CaCl2 were introduced into 2.5% (w/v) protein dispersions at pHs 4.5, 5.5, 6.5, and 7.5, and free Ca monitored. Near the isoelectric point of globulin (pH similar to 4-5), Ca binding capacity was found to be low. At higher pHs, significant Ca chelation occurred, initially attributed to free PA binding sites, resulting in the formation of insoluble complexes and subsequent protein precipitation. The AE-IEP globulin fraction exhibited a higher Ca binding capacity than the SE globulin, attributed to its higher PA and lower initial Ca concentrations.

This study delves into the practical implementation of humane entrepreneurship (HumEnt) through an extensive case study of a Swiss small and medium-sized enterprise (SME) operating in the winter sports industry. This particular SME showcases several distinctive traits that align with what we can define as its humane entrepreneurial orientation. The primary objective of this case study is to analyze how the HumEnt model is applied within the SME's overarching corporate strategy and business model. Furthermore, this article introduces a three-dimensional positioning matrix, synthesizing insights from two prevailing approaches in the HumEnt literature. This matrix offers a more holistic framework for comprehending the HumEnt model in depth.

The rise of empowerment leadership, particularly in relation to corporate social responsibility (CSR), has garnered increasing attention in recent years. As work relationships evolve to promote better work-life balance, understanding these dynamics has become crucial for retaining employees, especially in the post-COVID-19 era. In France, small and medium-sized enterprises (SMEs) are particularly affected, struggling to retain workers in high-demand sectors. This article explores the practical connections between empowerment leadership and three key factors: CSR image, work-life balance, and job satisfaction. Through research conducted with young professionals in the BETIC sector (engineering and consulting firms), the findings offer actionable insights for SMEs seeking to improve employee retention by aligning leadership practices with broader social and organizational responsibilities, in particular through empowering leadership and CSR.

Pulses are rich in proteins and a good source of calcium. However, antinutritional compounds such as phytic acid can bind to proteins and minerals to form complexes, reducing their digestibility and bioavailability, respectively. This study investigated interactions and potential complex formation between phytic acid, calcium, and proteins in pea and faba bean concentrate dispersions. The solubility of the 3 compounds was measured at pH 6.5, 7.0 and 7.5. Formation of complexes was investigated by chelating calcium upon EDTA addition or by removing proteins via ultrafiltration. Protein profiles were compared using Size Exclusion Chromatography (SEC). For both pea and faba bean, protein solubility increased with increasing pH. Phytic acid solubility was minimum at pH 7.0, while simultaneously calcium solubility was maximum. Protein solubility increased with EDTA addition compared to the control at pH 6.5 (pea and faba bean) and 7.0 (pea), supporting the presence of insoluble binary complexes between calcium and proteins. The concomitant rise in phytic acid solubility for pea (pH 6.5 and 7.0) highlighted the formation of either insoluble binary (phytic acid to calcium) or ternary complexes. Also, the formation of soluble protein complexes with phytic acid and, possibly, with calcium was highlighted. Small amounts of soluble ternary complexes were observed at pH 7.5. SEC results showed an increase in globulin's (especially legumin) solubility after calcium chelation; this demonstrated the formation of insoluble complexes mediated by calcium. This study highlighted that the different protein fractions from pulses must be considered separately in their ability to establish complexes with calcium and phytic acid.

This article explores the practical impact of humane entrepreneurship on small and medium-sized enterprises (SMEs), demonstrating how adopting a humane entrepreneurial orientation (HEO) can significantly enhance financial performance, employee engagement, and environmental sustainability. It provides valuable insights for business leaders and policy makers by showcasing how integrating humancentric approaches into business strategies not only drives profitability but also strengthens organizational commitment and social responsibility. The article emphasizes the practical benefits of HEO for SMEs, while calling for further research to assess its broader applicability across different industries and regions.

In this paper, we quantify weak protein-protein interactions in solution using cross-interaction chromatography (CIC) and surface plasmon resonance (SPR) and demonstrate that they can be modulated by the addition of millimolar concentrations of free amino acids. With CIC, we determined the second osmotic virial cross-interaction coefficient (B23) as a proxy for the interaction strength between two different proteins. We perform SPR experiments to establish the binding affinity between the same proteins. With CIC, we show that the amino acids proline, glutamine, and arginine render the protein cross-interactions more repulsive or equivalently less attractive. Specifically, we measured B23 between lysozyme (Lys) and bovine serum albumin (BSA) and between Lys and protein isolates (whey and canola). We find that B23 increases when amino acids are added to the solution even at millimolar concentrations, corresponding to protein/ligand stoichiometric ratios as low as 1:1. With SPR, we show that the binding affinity between proteins can change by 1 order of magnitude when 10 mM glutamine is added. In the case of Lys and one whey protein isolate (WPI), it changes from the mM to the M range, thus by 3 orders of magnitude. Interestingly, this efficient modulation of the protein cross-interactions does not alter the protein's secondary structure. The capacity of amino acids to modulate protein cross-interactions at mM concentrations is remarkable and may have an impact across fields in particular for specific applications in the food or pharmaceutical industries.

Many bio-hydrogels are prepared thanks to the addition of divalent ions. These gels usually exhibit partial ionic selectivity, a feature is leveraged to instigate an osmotic flow during the gelation process across a range of bio-hydrogels. A simple experimental setup consisting a glass capillary filled by the reactant solution is taken as an advantage, brought into contact with a reservoir of calcium chloride. Direct observation allows to characterize the gelation kinetics, the permeability and the selectivity of several gels, including some made of protein aggregates, pectin, and alginate. It is shown that these intrinsic properties, coupled with appropriate gelation kinetics, intricately govern the osmotic flow induced by the chemical potential difference of the calcium chloride ions imposed during gel formation, consistent with the Kedem-Kashalsky equation. The forming gel acts as a semi-permeable membrane for calcium chloride ions. The consequences of this osmotic flow are of potentially great interest since it triggers an increase of the gel concentration close to its boundary, opening the road to their spontaneous structuration. The formation of this dense shell is well accounted for the combination of a mass balance and a kinetic model. During ion-induced gelation, osmotic flows occur and spontaneously generate a concentration gradient. This phenomenon is due to the partially selective nature of the gel that forms, which acts as a semi-permeable membrane. A simple model based on the Kedem-Katchalsky equations is proposed to quantitatively capture gel structuring and shows that it is strongly coupled to gelation kinetics. image

Methylcellulose is commonly used in meat analogues for binding ingredients. In this study, we compared the binding properties of a methylcellulose hydrogel (5% w/w) to a novel, clean-label binder based on a mixture of pea protein and sugar beet pectin ( r = 2:1, 22.5% w/w, pH 6.0) with and without laccase addition in a burger type meat analogue. It was shown that the pea protein–pectin binder glued vegetable protein particles and fat mimic particles together prior to cooking and frying, thereby improving forming of the mass into burger patties. Furthermore, sensory analysis revealed that the cohesiveness of the fried burger patties was better when the protein–pectin binder was used. However, the used binder system did not affect the hardness of the burger patties indicating that the binders rather affected the coherence of the structural elements. Burgers with solid fat particles were rated better in terms of appearance as compared to emulsified fat particles, since the former were not visible. This study is useful to better understand meat analogue product design for a higher acceptance among consumers.

Food binders must be sticky to glue different components together. This study evaluated the impact of homogenization of pea proteins on the stickiness of pea protein – apple pectin mixtures. A reduction in protein particle size was suggested to improve adhesion and cohesion by increasing reactive surface area, resulting in a sticky material. In addition, impact of concentrating methods, namely freeze-drying and vacuum evaporation, on concentrating the homogenized pea protein dispersions was investigated. A reduced particle size of pea proteins upon homogenization led to an increased stickiness of the biopolymer matrix when the proteins were vacuum evaporated as demonstrated by a tack test. This was attributed to a firmer and more cohesive bulk structure demonstrated by rheological, confocal laser scanning microscopy and visual observations. Vacuum evaporation prevented re-aggregation of protein particles compared to freeze-drying since less water was expelled during vacuum evaporation. These results provide new insights into tuning stickiness of biopolymer mixtures.

A bacon-type meat analogue consists of different structural layers, such as textured protein and a fat mimetic. To obtain a coherent and appealing product, a suitable binder must glue those elements together. A mixture based on pea protein and sugar beet pectin (r = 2:1, 25% w/w solids, pH 6) with and without laccase addition and a methylcellulose hydrogel (6% w/w) serving as benchmark were applied as binder between textured protein and a fat mimetic. A tensile strength test, during which the layers were torn apart, was performed to measure the binding ability. The pea protein–sugar beet pectin mixture without laccase was viscoelastic and had medium and low binding strength at 25 °C (F ≤ 3.5 N) and 70 °C (F ≈ 1.0 N), respectively. The addition of laccase solidified the mixture and increased binding strength at 25 °C (F ≥ 4.0 N) and 70 °C (F ≈ 2.0 N), due to covalent bonds within the binder and between the binder and the textured protein or the fat mimetic layers. Generally, the binding strength was higher when two textured protein layers were glued together. The binding properties of methylcellulose hydrogel was low (F ≤ 2.0 N), except when two fat mimetic layers were bound due to hydrophobic interactions becoming dominant. The investigated mixed pectin–pea protein system is able serve as a clean-label binder in bacon-type meat analogues, and the application in other products seems promising.

Nowadays, legumes are considered as a good source of plant-based proteins to replace animal ones. They are more favorable regarding environmental aspects and health benefits, therefore many people consider moving toward a greener diet. Interestingly, recent consumer trends are promoting pea and faba bean as alternatives to soybean. Both are rich in protein and a good source of essential nutrients and minerals (calcium). However, these advantages can be partially impaired due to their high phytic acid content. This natural polyphosphate is a major antinutrient in plant-based foods, as it can bind minerals (particularly calcium) and proteins, thereby reducing their digestibility and subsequent bioavailability. Indeed, complexes formed are insoluble and limiting the absorption of nutrients, thus lowering the nutritional value of pulses. To understand and overcome these issues, the present review will refine specific mechanisms involved in assemblies between these three essential compounds in legumes as soluble/insoluble binary or ternary complexes. Molecular interactions are influenced by the environmental medium including pH, ionic strength and molar concentrations modulating the stability of these complexes during protein extraction. Protein/phytic acid/calcium complexes stability is of high relevance for food processing affecting not only structure but also functional and nutritional properties of proteins in legume-based foods.

BACKGROUND Binders in plant-based meat analogues allow different components such as extrudate and fat particles to stick together. Typically, binders then are solidified to transform the mass into a non-sticky, solid product. As an option for a clean label binder possessing such properties, the solidification behavior of pea protein - pectin mixtures (250 g kg-1 , r = 2:1, pH 6) was investigated upon heating, and upon addition of calcium, transglutaminase, and laccase, or by combinations thereof. RESULTS Mixtures of (homogenized) pea protein and apple pectin had higher elastic moduli and consistency coefficients and lower frequency dependencies upon calcium addition. This indicated that calcium physically crosslinked pectin chains that formed the continuous phase in the biopolymer matrix. The highest degree of solidification was obtained with a mixture of pea protein and sugar beet pectin upon addition of laccase that covalently crosslinked both involved biopolymers. All solidified mixtures lost their stickiness. A mixture of soluble pea protein and apple pectin solidified only slightly through calcium and transglutaminase, probably due to differences in the microstructural arrangement of the biopolymers. CONCLUSION The chemical makeup of the biopolymers and their spatial distribution determines solidification behavior in concentrated biopolymer mixtures. In general, pea protein - pectin mixtures can solidify and therefore have the potential to act as binders in meat analogues. This article is protected by copyright. All rights reserved.

To understand and limit the unpleasant oral sensation of astringency felt during the consumption of pea-based drinks, we investigated the interaction between mixtures of salivary and pea proteins, as compared to mixtures where HEPES buffer (at pH 6.8) was used as a negative control for saliva. Since astringent compounds have the ability to bind with salivary proteins, mixes of freshly collected whole unstimulated saliva and a pea protein isolate (PPI) (a dispersion at 3.5% w/v) were prepared in ratios 95:5 and 1:1 saliva:PPI, to allow different stoichiometries to occur in the mouth. Samples were incubated at 37 degrees C during 30 min, after centrifugation at 16000g during 20 min to separate pellet from supernatant. Using techniques such as SEC, Native-PAGE and LC-MS, 7 pea proteins were identified as being capable of forming aggregates with at least 7 saliva proteins, some of which have been previously connected to astringency.