ABSTRACT While the bioactivity of pulse protein hydrolysates is widely studied, the holistic impact of unit operations from flour to final powder remains unexamined. This study produced black bean hydrolysate powders using enzyme‐assisted extraction, direct steam injection (low temperature, LT: 130°C/15 s, or high temperature, HT: 145°C/4 s) and spray‐drying to evaluate their effects on bioactivity. Overall, the structural and physicochemical properties of the LT and HT samples were similar, with evidence of denaturation and aggregation through decreased intrinsic fluorescence intensity, increased surface hydrophobicity, and decreased surface charge at pH 4 compared to a non‐thermally treated, freeze‐dried control. Despite structural changes, protein solubility was similar (50%–51% at pH 4, 86%–94% at pH 7), as aggregates remained soluble in neutral conditions. Trypsin inhibitor activity was unaffected by thermal treatment (165–167 trypsin units inhibited/mg protein), but the in vitro protein digestibility of the LT (81%) and HT (83%) samples was significantly higher than the control (51%). Total phenolic content (58–63 mg GAE/g protein), antioxidant activities (ABTS/ORAC) (0.83–1.02 mg GAE/g protein), and antidiabetic activity (α‐glucosidase inhibition, 18%–19%) were mostly retained following direct steam injection and spray‐drying, but ACE‐inhibition activity decreased for HT (70% vs. 89%–93% for LT and control), signifying that antihypertensive peptides may have been degraded or irreversibly aggregated at higher processing temperatures. The results demonstrate that enzyme‐assisted extraction followed by industrially relevant thermal processing and drying is an effective method to generate bioactive black bean hydrolysate powders, supporting future commercialization of functional pulse ingredients for nutraceutical applications.
ABSTRACT Microalgae are promising protein sources, but improved extraction techniques are needed to ensure efficient and sustainable processing. The objective of this study was to investigate the effect of high‐pressure homogenization (HPH) parameters on the extraction of soluble protein from Nannochloropsis sp. Various combinations of processing parameters, such as extraction media (water vs. phosphate buffer (0.1 M, pH 7)), biomass concentration (2% vs. 8% w/v), HPH pressure (0–1500 bar), and pass/cycle number (1–3), were used. Increasing pressure, biomass concentration, or pass number did not always improve soluble protein yield, likely due to reduced disruption efficiency at higher solids loading and post‐release protein denaturation/aggregation during excessive processing. Under all pressures, protein yield at 2% (w/v) biomass in phosphate buffer decreased from two to three cycles despite greater membrane disruption, as confirmed by dual‐fluorescence microscopy, suggesting that excessive processing promoted post‐release protein denaturation/aggregation and interactions with other released intracellular materials, thereby reducing the soluble protein fraction. The maximum protein yield obtained at 1500 bar (after two cycles) was 80.35 ± 1.0 mg·g −1 DW, which corresponded to 25.5% recovery of the total biomass protein, and the cumulative soluble protein recovery, including the protein recovered during the washing step, reached 40.5%. The results establish an optimal HPH operating window that maximizes protein recovery while limiting the potential for excessive processing‐induced protein modification, providing a practical guideline for efficient and scalable microalgae protein extraction.
ABSTRACT This study investigated the effects of lupin species, pH, and protein concentration on the structural and functional properties of albumin, globulin, and glutelin protein fractions isolated from white ( Lupinus albus ) and blue ( Lupinus angustifolius ) lupin seeds. The globulin and glutelin fractions exhibited characteristic pH‐dependent U‐shaped solubility curves, with minimum solubility near pH 5. Amino acid analysis revealed that white lupin globulin (WLGlo) was the only fraction not limited in sulfur‐containing amino acids (methionine + cysteine: 107% amino acid score). Blue lupin glutelin (BLGlu) demonstrated high surface hydrophobicity (3924.1), in vitro protein digestibility (92.44%), and the highest intrinsic fluorescence intensity at pH 3, indicating a conserved but enzyme‐accessible protein conformation. Far‐UV circular dichroism analysis revealed that white lupin albumin (WLAlb) possessed the highest α‐helix content at pH 7 (23%) and pH 9 (18%), reflecting a more flexible conformation. Emulsions stabilized by WLGlo at pH 3, 7, and 9 had smaller oil droplet sizes (~4–7 μm) than most of the other protein fractions. All fractions displayed excellent foaming properties, with stability exceeding 85%, and glutelin fractions showing particularly good (50%–60%) foaming capacity at pH 5. These findings establish clear structure–function relationships and demonstrate the potential of lupin protein fractions as high‐performance ingredients for diverse food applications, with each fraction offering specific advantages based on nutritional quality, structural characteristics, and functional properties.
ABSTRACT Microalgae, such as Tetradesmus obliquus , have gained attention as sustainable alternative protein sources for food. This study aimed to compare three protein extraction strategies: (P A ): ball milling followed by solubilization, (P B ): ball milling, solubilization, and isoelectric precipitation, and (P C ): ball milling combined with ultrasound, solubilization, and precipitation. We also aimed to establish the relationship between processing conditions, protein structural modifications, thermal behavior, and techno‐functional properties of the resulting products. Compared to the other samples, the P B extract exhibited the highest protein content (52.65% on a dry weight basis), although it demonstrated a lower protein recovery yield. In contrast, the P C extract achieved the highest extraction yield, corresponding to 21.1% of the total protein in the biomass. Structurally, P C exhibited a more ordered secondary structure, whereas P A exhibited a less‐ordered profile. Differential scanning calorimetry revealed greater thermal stability for P C , with a denaturation enthalpy of 136.6 J·g −1 , indicating stronger intermolecular interactions after ultrasound‐assisted processing and precipitation, which directly influenced its functional behavior. The P C exhibited lower water‐holding capacity (0.71 ± 0.06 g water/g protein), higher oil‐holding capacity (1.98 ± 0.20 g oil/g protein), and superior emulsifying performance, with creaming index values between 44.6% and 57.6% (vol/vol) and emulsifying activity index ranging from 47.2 to 89.4 m 2 /g at 1% (wt/wt) concentration across pH 3.0–9.0. The main finding of this study is the clear processing–structure–function relationship established for T. obliquus proteins, identifying P C strategy as the most effective method for producing protein‐rich concentrates with potential applications as functional food ingredients.
ABSTRACT This study explored the nutrient composition, protein profile, physicochemical and emulsifying properties of commercial yeast protein ingredients, including a Saccharomyces cerevisiae protein concentrate (YPC) and a Candida utilis biomass (YB), with a view to enabling their use in food applications. YPC and YB exhibited low solubility in water across the pH range of 2–9 due to the high density of the yeast cells, in which most of the proteins are located. Investigation of the emulsifying properties of these ingredients, using model oil‐in‐water systems (1–5 wt% protein, 10 wt% oil, pH 6.8), showed that while emulsion formation could be attributed to the soluble phase, comprising proteins and potentially other surface‐active compounds, the presence of yeast cells improved stability over 30 days of refrigerated storage through a steric mechanism. A protein‐to‐oil ratio greater than 1:10 prevented oil droplet coalescence, and the inclusion of a food‐grade stabilizer, such as gellan gum (0.15 wt%), to increase the viscosity of the continuous phase, provided colloidal stability throughout the storage period for all emulsions. Differences were observed in the properties of the emulsions produced using YPC and YB, which may be explained by their cell size and morphology, the composition of the cell wall, and the soluble protein concentration and profile. Taken together, the results show that commercial yeast protein ingredients can form physically stable oil‐in‐water emulsions when appropriate protein‐to‐oil ratios and continuous phase viscosity are employed.
ABSTRACT Cheese functionality emerges from the hierarchical organization of its components, in which casein micelles assemble into a heterogeneous, weakly bonded network that entraps fat and water in a structured manner. Replicating this in cheese analogues remains challenging, as most systems rely on fundamentally different ingredients and structuring routes. In this review, structure formation in dairy cheese and plant‐based cheese analogues is analyzed following a multi‐length scale perspective, from molecular interactions to mesoscale organization and macroscale functionality. Particular emphasis is placed on the distinction between bottom‐up assembly, characteristic of natural dairy cheese, and top‐down structuring, typical of processed cheese and cheese analogues based on plant polysaccharides and/or proteins. Dairy cheese forms through the destabilization and aggregation of casein micelles into dynamic, particulate networks, whose connectivity, heterogeneity, and interaction strength govern properties such as hardness, meltability, and stretchability. In contrast, cheese analogues are primarily structured through processing‐induced gelatinization, aggregation, and phase organization, often resulting in markedly different microstructures and rigid networks with limited melt and stretch behavior. By comparing these structuring routes, this review highlights that differences in functionality arise not only from composition but also from how components are organized at the mesoscale. Design strategies for cheese analogues are therefore discussed in terms of achieving mesoscale equivalence, either by tailoring top‐down processing to mimic dynamic network behavior or by developing bottom‐up assembly approaches using precision fermentation‐based or plant‐derived building blocks. This structure‐driven perspective provides a framework for the rational design of next‐generation cheese analogues with improved functional performance.
ABSTRACT Sensory profile of plant‐based meat alternatives (PBMAs) has remained a major barrier to their widespread adoption. The major issues in the sensory profile of PBMAs include the presence of off‐odor volatile compounds, bitter taste non‐volatile compounds, and the inability of plant‐based ingredients to mimic the overall meaty flavor of conventional meat products. These sensory challenges can be addressed through treatment of raw materials prior to extrusion of PBMAs. Potential applications of fermentation and enzymatic (hydrolysis and crosslinking) modifications as pre‐treatments before extrusion cooking to improve the sensory profile of PBMAs were reviewed. Fermentation and enzymatic modifications can effectively address PBMA's flavor issues by masking off‐flavors, degrading off‐odor aldehydes into corresponding alcohols and esters, synthesizing umami flavor precursors, and degrading bitter non‐volatile compounds. Additionally, these pre‐treatments modify protein molecular structure, thereby altering techno‐functionality and influencing fibrous structure formation during extrusion. However, pre‐treatment effectiveness in modifying the flavor and texture profile of PBMAs relies greatly on process optimization as the incorrect choice of microorganisms and enzymes as well as pre‐treatment conditions may lead to the formation of undesirable sour and bitter tastes, respectively. Furthermore, the extensive hydrolysis and formation of small peptides may sometimes hinder the development of fibrous structure formation during extrusion cooking. Overall, fermentation and enzymatic treatments are promising technologies that should be further explored alongside extrusion cooking for the production of next‐generation extruded PBMAs with improved sensory characteristics.
ABSTRACT This comparative study investigated the intensities of taste, aroma, flavor, and trigeminal attributes of pressure‐cooked and pureed samples of three faba bean cultivars, Malik (regular tannin, regular vicine/convicine), Fabelle (regular tannin, low vicine/convicine), and Snowbird (low tannin, regular vicine/convicine) with and without the seed coat. Cultivar differences significantly influenced the intensities of sour, earthy, and green aromas, astringency, and sour and green flavors in whole bean purees. In cotyledon purees, cultivar effects were evident for astringency, bitter taste, and brothy flavor, but not for aroma attributes, suggesting that seed coat components may play a key role in faba bean aroma. Snowbird, a low tannin cultivar, exhibited the highest bitter taste and astringency in its cotyledon puree, compared to those of regular tannin cultivars Malik and Fabelle. While Snowbird's whole bean puree had lower astringency than Malik, it was significantly more astringent than Fabelle. These findings challenge the conventional belief that condensed tannins in the seed coat are the primary contributors to bitterness in faba beans. The results show that condensed tannins contribute more to astringency, while vicine/convicine compounds, located in the cotyledons, might play a role in both astringency and bitterness. The findings of this study have direct implications for the food industry, particularly in guiding the selection of faba bean cultivars for product development with predictable sensory profiles.
ABSTRACT Sorghum, an ancient grain, is generating much interest in the plant‐based diversified protein market. Sorghum's major protein is the alcohol‐soluble kafirin, whose hydrophobicity and limited functionality have posed challenges for extraction and protein quality using conventional methods. The current work evaluated a blended solvent approach (ethanol: alkali) to improve sorghum protein yield and properties. Ground, undefatted or defatted pearled sorghum (UPS or DPS) and sorghum protein meal from wet‐milling (control; WSPM) were each extracted with anhydrous ethanol:0.1 N NaOH (1:1.2, v:v) at 50°C and 250 rpm for 2 h, centrifuged, membrane filtered, then freeze‐dried. Protein recovery, composition, and functional properties were determined. Sorghum samples contained predominantly kafirins (> 30%) and glutelins (ca. 20%). Ethanol‐alkali extraction had high protein recoveries (78%–83%) and produced high‐purity (87%–97%) protein extracts, with WSPM having the greatest protein content. Starting UPS and DPS protein solubility index (PSI) values (30%) were five‐fold greater than that of WSPM. Protein isolates showed markedly improved solubility, with PSI of 99% for UPS or DPS and 20% for WSPM. Solubility‐pH profile affirmed UPS and DPS protein isolates are significantly more soluble than WSPM protein isolate at pH > 6.0. DPS and WSPM protein produced substantial foam (100 mL), but only DPS showed moderately stable foam (64% remaining foam after 15 min). Emulsification activity for the sorghum protein extracts were similar at pH 7.0 and pH 10.0, but WSPM protein emulsions were the most stable. This work demonstrated extraction using ethanol: alkali can produce sorghum protein with enhanced yield and utility as a diversified plant‐based protein.
ABSTRACT The demand for plant‐based dairy alternatives needs functional ingredients that support robust fermentation. This study compares native quinoa protein isolate (QpI) and its enzymatic hydrolysate (QpH) as nitrogen sources for Lactiplantibacillus plantarum WCFS1. Comprehensive characterization revealed that enzymatic hydrolysis converted the high‐molecular‐weight, β‐sheet‐rich proteins of QpI into peptides (QpH) with molecular weights below 5000 Da. While both substrates supported high final cell densities comparable to the control medium (MRS) (~10.5 Log CFU/mL), they induced longer lag phases, indicating a metabolic adaptation cost. Bacteria grown in QpH exhibited significantly enhanced cell membrane integrity, with propidium iodide incorporation reduced to 17.1% compared to ~23.6% for QpI and control cultures. This protective effect, independent of final pH, is attributed to the intrinsic bioactivity of the quinoa‐derived peptides. These findings demonstrate that QpH is not merely a nutrient source but a superior functional ingredient that actively enhances the physiological robustness of probiotic bacteria. This has significant implications for developing high‐viability, plant‐based fermented foods and probiotics, positioning quinoa protein hydrolysate as a key component for next‐generation functional products.
ABSTRACT Protein fibrillation has emerged as a promising strategy to enhance structural and functional properties of various protein‐based matrices, owing to the unique thin, elongated, β‐sheet‐rich structures of fibrils that impart superior texture, stability, and encapsulation functionalities. This review critically examines the formation of protein fibrils, highlighting the kinetic mechanisms, effects of protein sources, and their influence on fibril morphology and functionality. Special emphasis is placed on fibril synthesis from by‐product protein streams, which aligns with circular economy principles by reducing waste and production costs while extending fibril applications to both food and non‐food domains, including packaging and bioplastics. Challenges associated with fibril instability at food‐relevant pH conditions are discussed in detail, alongside emerging stabilization strategies such as complexation with polysaccharides, polyphenols, and physical treatments such as dialysis. This review presents protein fibrils as highly tunable and scalable sustainable biomaterials with considerable potential to advance both food and polymer industries.
The increasing demand for animal‐based protein has led to biodiversity loss, deforestation, pollution, and extensive land use, mainly due to the rising production of soybean meal and fish meal used to feed livestock. Some edible insects, such as the black soldier fly, mealworm, and cricket, have emerged as a new sustainable source of protein. This review highlights that these edible insects can replace a significant portion of soybean meal and fish meal in monogastric animals (pigs and chickens) and aquaculture (fish and crustaceans). Their protein content, amino acid profile, and digestibility often meet the nutritional requirements of these animals. However, some indispensable amino acids require special attention. Overall, edible insect meals can be compared to those made from soybeans and fish. They can partially or fully replace these traditional protein sources in livestock farming.
This study investigates the formulation and functionality of composite gels made from seaweed (SW), rice protein (RP), and date insoluble fiber (DIF), focusing on the effects of pH (4, 6, and 8) and monovalent cations (K + via KCl). Three formulations, SW, SW + RP, and SW + RP + DIF, were evaluated for physicochemical, textural, and structural properties. The incorporation of rice protein decreased gel hardness but increased adhesiveness and springiness, indicating enhanced elasticity and cohesive strength. The addition of date fiber further modified the texture by increasing hardness, likely due to matrix reinforcement by fiber particles. No syneresis was observed in any formulation. The addition of K + significantly increased gel hardness and moisture content, indicating the formation of stronger, more water‐retentive networks. Rheological and microstructural analyses confirmed that K + induced the formation of brittle gels with larger pores, whereas formulations without K + produced softer, less brittle gels with more compact and uniform structures. Color properties were also influenced by the addition of rice protein and date fiber, as well as pH, reflecting compositional, and pigment effects. From a sustainable protein perspective, this study demonstrates the potential of combining seaweed, rice protein, and fiber‐rich by‐products to create functional, plant‐based gel systems. The approach supports circular economy principles by utilizing renewable ingredients and food processing residues, offering viable alternatives to synthetic gelling agents and animal‐derived proteins.
The surging interest in pulse proteins is driven by their sustainability, nutritional advantages, and consumer preferences, which have established them as key components in the evolving plant protein landscape. However, challenges persist in effectively utilizing protein isolates or concentrates due to their limited functionality, unpleasant taste, and the presence of anti‐nutritional compounds. This review explores pulse protein processing methods to address these challenges. This comprehensive review provides an in‐depth understanding of pulse protein processing, covering pretreatments such as defatting, fermentation, and germination; advancements in extraction‐precipitation methods, including deep eutectic solvent extraction, fermentation‐ and heat‐based precipitation; and post‐processing operations, including washing and drying of the extracted proteins. By providing an in‐depth understanding of each protein processing step from seed milling to protein drying, this review aims to foster the development of high‐quality pulse protein ingredients for future food manufacturing.
Unrefined pea ( Pisum sativum ) flour is a promising food material that can either serve as a functional standalone ingredient or as the starting material to extract functional proteins and starches. This observational study used rapid screening of 650 pea accessions, which span a domestication range from wild species to modern cultivars, to select 20 representative samples based on near‐infrared spectral differences, capturing broad compositional diversity and illustrating how intrinsic physicochemical and protein functional traits influence their suitability in foods. To investigate the intrinsic variability, the physicochemical properties (surface charge, thermal properties, particle size), functional characteristics (solubility, interfacial tension), and visual characteristics were analyzed. Small variations in surface charge conditions were found at pH 5 and 7, whereas the charge varied from 2.7 ± 1.4 to 11.5 ± 1.4 mV at pH 3. However, high variations were found in protein solubility that ranged from 28.4% ± 5.1% to 92.2% ± 1.5% at pH 7, and differences in protein characteristics were also identified in thermal denaturation temperatures that ranged from 85.2°C ± 0.2°C to 99.6°C ± 0.8°C. These observations were confirmed through microstructural characterizations that also showcased the intrinsic color and size differences of the main constituents (starch granules and protein bodies). The findings of this study indicate that there are significant variations in the physicochemical and functional properties of different pea flours, which have considerable potential for the food industry. This highlights the importance of selecting the appropriate pea raw materials for optimal results in various food applications.
The search for sustainable and multifunctional protein ingredients has driven interest in underutilized legumes such as adzuki bean, a crop rich in protein, polyphenols, and bioactive compounds yet underexplored in modern food applications. This study developed adzuki bean protein (ABP) via alkaline extraction (pH 8–10) and isoelectric precipitation (pH 4.0–4.5), evaluating process efficiency, nutritional attributes, and multifunctionality potential. Notably, the natural low‐fat content of adzuki bean enabled protein extraction without defatting or organic solvents, featuring a more sustainable process. Extraction at pH 9.0 with precipitation at pH 4.5 achieved the most favorable balance of protein content (84.5%), yield (75%), and recovery (62%). Amino acid analysis confirmed a balanced profile with high levels of essential amino acids, including branched‐chain amino acids, lysine, methionine, and tryptophan, comparable to soy protein. Additionally, ABP exhibited a natural red hue and significant antioxidant activity (TPC up to 222.6 μmol GAE/g; DPPH up to 110.3 μmol TE/g), highlighting its dual nutritional and functional value. Techno‐functional analyses demonstrated strong oil‐holding capacity, emulsification, gelation, and foam stability, positioning ABP as a clean‐label alternative to conventional proteins. Sensory evaluation indicated neutral taste and umami‐enhancing potential. Application in a plant‐based jerky prototype delivering comparable protein to meat jerky but reduced sodium and cholesterol, and high dietary fiber, demonstrated practical feasibility. Further supported by intrinsic color and oxidative stability over 1 year storage at 25°C, ABP emerges as a scalable, value‐added ingredient with distinctive multifunctional properties that enable clean‐label innovation and supply chain diversification to advance health‐conscious product development.
This study provides a systematic evaluation of the allergenic potential of almond hulls using a combination of immunoblotting and proteomic approaches. Laboratory‐prepared almond hulls from multiple Prunus dulcis cultivars were analyzed to identify intrinsic allergenic proteins and assess potential cross‐reactivity with other Prunus species. Immunoblot analysis revealed a consistently reactive ~75 kDa protein across all almond hull cultivars. Besides, additional IgE‐reactive bands were recognized by plasmas from Prunus fruit‐allergic patients, indicating cross‐reactivity mediated by conserved panallergens such as profilins and pathogenesis‐related protein type 10 (PR‐10)/Bet v 1‐like proteins. Mass spectrometric analysis of laboratory‐prepared almond hulls identified several PR‐10/Bet v 1‐like proteins sharing 25%–53% sequence similarity with homologs from peach, apricot, and cherry, confirming the presence of intrinsic almond hull proteins with potential allergenic relevance. In contrast, proteomic analysis of pilot‐scale processed Nonpareil almond hull food powder revealed a more complex allergen profile, including the detection of amandin (Pru du 6) and profilin (Pru du 4), likely introduced through mixed‐in kernel residues or cross‐contact with almond kernels during industrial hulling/shelling. The combined data demonstrate that almond hulls contain both intrinsic proteins capable of cross‐reactivity and kernel‐derived allergens introduced through processing. These findings provide foundational evidence to guide the safe utilization of almond hulls in food systems while emphasizing the need for allergen management strategies to minimize contamination and ensure consumer safety.
ABSTRACT Swift global transition toward sustainable food systems led to increasing demand for alternative protein sources capable of replicating the nutrition and sensory attributes of animal meat. Plant‐based meat analogues (PBMAs) are central to this shift, driven by consumer interest in environmental management, health, and ethical considerations. This review examines the comparative functionality and processing behavior of major plant proteins: soy, pea, and wheat, and a diverse range of emerging sources such as faba bean, lentil, chickpea, and mung bean. Particular emphasis is placed on their structural composition, amino acid balance, and key functional properties including gelation, emulsification, and water‐ and oil‐holding capacities that govern texture, juiciness, and mouthfeel. High‐moisture extrusion (HME), widely used technology for PBMA production, is discussed with a focus on how heat, shear, and moisture induce protein unfolding, alignment, and cross‐linking to create fibrous, meat‐like structures while influencing digestibility and amino acid availability. Protein blending strategies are highlighted as tools to improve texture, nutritional quality, and processing performance while reducing dependence on allergenic or monoculture‐prone crops. Ingredient innovations such as hydrocolloids, modified starches, and tannin‐mediated protein modification are reviewed for their roles in enhancing structural integrity, moisture retention, and flavor, and for mitigating anti‐nutritional factors. The article presents a comprehensive framework for optimizing PBMA by integrating insights from food chemistry, processing, engineering, and sustainability science. The synthesis of ingredient functionality, extrusion dynamics, and sensory outcomes offers a pathway toward the development of next‐generation meat analogs that are nutritionally balanced, environmentally responsible, and broadly acceptable to consumers.
ABSTRACT The objective of this work was to generate and characterize complexes of quinoa proteins (QP) with either resveratrol (RSV) or tocopherol (TOC) whose dimensions fell into the nanoscale. The QP‐based nanocomplexes characterization was carried out jointly with encapsulation efficiency determination. Fourier‐Transform Infrared Spectroscopy (FTIR) showed no covalent bond formation and indicated that the protein's secondary structure was modified. Transmission Electron Microscopy (TEM) images and Dynamic Light Scattering (DLS) measurements confirmed that the addition of bioactive compounds did not substantially alter the protein's original size. A consistent particle diameter of 100 nm was observed in both types of nanocomplexes with and without RSV and TOC. The antioxidant capacity of nanocomplexes was analyzed after an in vitro simulated digestion process, showing an increase in this property postdigestion. These nanocomplexes hold great potential as functional ingredients.
Lupin, an underutilized legume belonging to the Fabaceae family, demonstrates a huge potential as an alternative protein source by contributing to food security and environmental resilience in the face of climate change. This work highlights the potential of lupin protein as a preferred substitute for soy protein in plant‐based food applications. A critical assessment of the protein extraction methods for lupin and their influence on the physicochemical and nutritional properties of the extracted lupin protein was determined. Furthermore, the structural and physicochemical properties of lupin proteins compared to those of soybean were examined. Despite its high protein content and excellent amino acid profile, the poor functional properties of lupin protein in comparison to soy posed a major limitation for its use in food formulations. Based on this observation, the effect of novel and non‐thermal processing on lupin protein was further determined. Findings revealed increasing utilization of lupin protein for novel foods, but limited success in the adoption of lupin protein in the mainstream plant protein sector, attributed largely to the presence of anti‐nutritional factors, allergens, and inferior organoleptic qualities. Therefore, by offering process‐induced improvement of the functional properties, a wider application of lupin protein in food products could address the protein diversity challenge.
