Plant-based proteins: advanced extraction technologies, interactions, physicochemical and functional properties, food and related applications, and health benefits

Figures & data

Figure 1. The synthesis pathway of proteins in plants.

Table 1. Protein content and amino acids profile of some protein-rich plant.

Protein-rich plants	Protein percentage (Dry matter)	Available amino acids (g/100 g of protein)	References
Soybean (Glycine max)	42.95–46.32%	Alanine (3.59), arginine (6.67), aspartic acid (10.20), cystine (1.05), glutamic acid (17.45), glycine (3.60), histidine (2.30), isoleucine (4.25), leucine (6.78), lysine (5.33), methionine (1.13), phenylalanine (4.59), proline (4.96), serine (4.593), threonine (3.14), tryptophan (1.12), tyrosine (3.22), and valine (4.10).	(Zhou et al. 2022a; Kalman 2014)
Faba bean or broad bean (Vicia faba)	23.3–34.2%	Aspartic acid (12.16), threonine (3.67), serine (5.45), glutamic acid (18.68), proline (5.19), glycine (4.85), alanine (4.46), cystine (0.98), valine (4.78), methionine (1.57), isoleucine (3.28), leucine (7.56), tyrosine (3.05), phenylalanine (4.39), histidine (2.80), lysine (7.00), arginine (8.82), and tryptophan (1.31).	(Rahate, Madhumita, and Prabhakar 2021; Al-Gaby 1998; Skovbjerg et al. 2020)
Common beans (Phaseolus vulgaris L.)	18.0–33.0%	Lysine (10.90), leucine (10.23), isoleucine (4.23), threonine (3.75), valine (4.44), phenylalanine (4.50), histidine (1.82), methionine (0.83), glutamic acid (14.95), aspartic acid (11.93), arginine (7.01), serine (10.67), glycine (2.78), alanine (4.49), tyrosine (2.76), and cysteine (0.53).	(Flores-Sosa et al. 2020; Guzmán-Maldonado, Acosta-Gallegos, and Paredes-López 2000)
Mung bean (Vigna radiata L.) (Amino acids as (g/16 g N)	26.3–30.9%	Alanine (4.37), arginine (6.81), aspartic acid (11.85), cystine (0.37), glutamic acid (18.05), glycine (3.94), histidine (2.59), isoleucine (4.79), leucine (7.90), lysine (6.69), methionine (1.22), phenylalanine (5.50), proline (4.03), serine (4.86), threonine (2.82), tyrosine (2.93), and valine (5.95).	(Coffmann and Garciaj 2007)
Lentils (Lens culinaris) (Amino acids as (g/16 g N)	24.3–30.2%	Alanine (4.3), arginine (7.2), aspartic acid (11.5), glutamic acid (15.5), glycine (4.1), histidine (3.0), isoleucine (4.7), leucine (7.4), lysine (7.0), methionine + cystine (2.8), phenylalanine + tyrosine (8.0), proline (4.0), serine (4.6), threonine (3.8), tryptophan (0.7), and valine (5.2).	(Wang and Daun 2006)
Chickpeas (Cicer arietinum L.)	8.8–24.1%	Arginine (8.5), histidine (3.2), isoleucine (4.8), leucine (8.5), lysine (7.0), methionine (1.1), phenylalanine (5.3), threonine (3.5), tryptophan (1.1), valine (5.2), alanine (5.2), aspartic acid (11.5), cystine (0.6), glutamic acid (17.8), glycine (3.6), proline (4.1), serine (3.5), and tyrosine (2.8).	(Elsohaimy, Refaay, and Zaytoun 2015; Iqbal et al. 2006)
Lupin (Lupinus luteus) (Amino acids as (g/16 g N)	45.0–48.2%	Lysine (4.6), methionine + cystine (2.9), cystine (2.3), threonine (2.9), isoleucine (3.5), tryptophan (0.6), valine (3.3), leucine (7.2), histidine (2.4), phenylalanine + tyrosine (5.4), tyrosine (2.0), arginine (9.6), aspartic acid (9.9), serine (4.6), glutamic acid (21.9), proline (3.1), glycine (3.7), and alanine (3.0).	(Sujak, Kotlarz, and Strobel 2006)
Kidney bean	15.2–23.8%	Threonine (4.74), valine (5.04), cysteine (0.66), methionine (1.22), isoleucine (4.35), leucine (8.48), tyrosine (3.57), phenylalanine (5.84), histidine (2.94), lysine (7.18), tryptophan (1.06), aspartic acid (12.70), serine (6.58), glutamic acid (16.50), proline (3.86), glycine (4.07), alanine (4.45), and arginine (6.77).	(Mbithi-Mwikya et al. 2000)
Pinto bean (Phaseolus vulgaris L.) (a variety of common beans)	18.0–22.0%	Lysine (6.2), histidine (2.9), arginine (6.2), aspartic acid (7.9), threonine (2.7), serine (3.7), glutamic acid (12.0), proline (3.4), glycine (3.7), alanine (4.0), cystine (1.0), valine (4.5), methionine (1.1), isoleucine (4.1), leucine (7.6), tyrosine (3.2), and phenylalanine (4.8).	(Audu and Aremu 2011)
Peanuts or groundnut (Arachis hypogaea L.)	22.0–30.0%	Glutamic acid (24.0), aspartic acid (12.8), serine, glycine (5.11), histidine (5.28), arginine (2.56), threonine (9.95), alanine (2.12), proline (4.97), tyrosine (5.16), valine (2.97), methionine (4.16), cysteine (1.81), isoleucine (0.28), leucine (3.18), phenylalanine (7.24), and lysine (3.19).	(Elsohaimy, Refaay, and Zaytoun 2015; Andersen et al. 1998)
Fenugreek seed (Trigonella foenum graecum)	25.0–38.6%	Histidine (1.60), threonine (8.00), valine (5.47), methionine (0.77), phenylalanine (2.39), isoleucine (5.97), leucine (9.37), lysine (5.17), tyrosine (3.70), cysteine (0.74), aspartic acid (11.68), glutamic acid (19.98), serine (2.75), glycine (4.60), arginine (7.57), alanine (3.57), and proline (0.97).	(Feyzi et al. 2015)
Horse gram (Macrotyloma uniflorum)	17.9–25.3%	Threonine (4.27), valine (5.97), cysteine (1.92), methionine (2.78), isoleucine (4.21), leucine (9.82), tyrosine (4.14), phenylalanine (5.47), histidine (2.57), lysine (5.87), tryptophan (1.23), aspartic acid (7.15), serine (5.64), glutamic acid (22.59), proline (5.78), alanine (5.80), and arginine (4.82).	(Palanisamy et al. 2012)
Alfalfa seeds (Medicago sativa)	15.3–32.27%	Alanine (5.66), arginine (3.70), aspartic acid (10.30), cystine (1.86), glutamic acid (2.16), glycine (4.99), histidine (5.62), isoleucine (6.72), leucine (7.86), lysine (6.58), methionine (5.03), phenylalanine (3.07), proline (5.20), serine (6.00), threonine (4.81), tryptophan (5.66), tyrosine (3.68), and valine (4.99).	(Sahni, Sharma, and Surasani 2020)
Almonds (Prunus dulcis L.)	10.0–35.0%	Asparagine (20.39), glutamic acid (43.14), serine (9.74), glycine (17.82), histidine (2.93), arginine (15.48), threonine (5.45), alanine (14.99), proline (10.06), tyrosine (4.84), valine (9.97), methionine (2.43), cysteine (0.54), isoleucine (6.20), leucine (15.24), phenylalanine (8.99), and lysine (11.87).	(Sathe et al. 2002)
Quinoa (Chenopodium quinoa Willd.)	12.33–23.71%	Histidine, (2.76), leucine (4.60), isoleucine (1.30), lysine (17.13), methionine with cystine (1.70), phenylalanine with tyrosine (9.34), threonine (1.47), and valine (2.03), alanine (5.34), glycine (9.60), proline (0.10), serine (2.57), tyrosine (2.88), glutamic (12.80), aspartic (8.54), and arginine (0.03).	(Elsohaimy, Refaay, and Zaytoun 2015; Abugoch et al. 2008)
Chia seeds (Salvia hispanica L.)	15.62–26.47%	Arginine (2.0), phenylalanine (1.16), histidine (0.61), isoleucine (0.74), leucine (1.42), lysine (0.93), methionine (0.67), threonine (0.54), valine (0.79), alanine (0.94), aspartic acid (1.28), cystine (0.42), glutamic acid (2.87), glycine (0.91), proline (1.28), and serine (0.94).	(Nitrayová et al. 2014)
Black cumin (Nigella sativa) (Nigella cake)	16.10–21.66%	Aspartic acid (10.05), threonine (3.95), serine (3.80), glutamic acid (22.40), proline (6.07), glycine (6.86), alanine (4.21), cystine (1.17), valine (5.10), methionine (1.45), isoleucine (3.98), leucine (6.92), tyrosine (3.35), phenylalanine (4.00), histidine (2.83), lysine (3.91), arginine (9.18), and tryptophan (0.77).	(Al-Gaby 1998; Oubannin et al. 2022)
Hemp seeds (Cannabis sativa L.)	20.17–25.06%	Isoleucine (3.99), leucine (6.63), lysine (4.16), methionine (1.39), cysteine (0.17), tyrosine (3.67), phenylalanine (4.57), threonine (4.57), valine (4.98), histidine (2.81), aspartic acid (9.41), glutamic acid (16.14), serine (5.18), glycine (3.99), arginine (9.91), alanine (4.50), and proline (4.53).	(Wang et al. 2008)
Finger millet (Eleusine coracan)	5.0–8.0%	Threonine (4.15), valine (6.20), cysteine (1.13), methionine (2.62), isoleucine (4.17), leucine (10.24), tyrosine (4.28), phenylalanine (5.37), histidine (2.47), lysine (2.58), tryptophan (1.45), aspartic acid (5.76), serine (5.41), glutamic acid (24.11), proline (6.26), glycine (3.33), alanine (6.14), and arginine (4.33).	(Mbithi-Mwikya et al. 2000)
Oats (Avena sativa)	12.4–24.4%	Lysine (5.2), histidine (3.1), arginine (7.8), aspartic acid (9.9), threonine (3.5), serine (4.8), glutamic acid (26.9), proline (5.8), cystine (2.6), glycine (5.5), alanine (5.5), valine (5.7), methionine (3.3), isoleucine (4.1), leucine (7.8), tyrosine (4.4), phenylalanine (5.7).	(Pomeranz, Robbins, and Briggle 1971)
Maize (Zea mays L.) (Corn meal)	8.68–12.55%	Aspartic acid (6.43), threonine (2.60), serine (4.90), glutamic acid (20.83), proline (8.85), glycine (4.68), alanine (7.68), cystine (1.88), valine (4.64), methionine (1.35), isoleucine (3.84), leucine (10.91), tyrosine (3.95), phenylalanine (4.86), histidine (2.65), lysine (2.93), arginine (5.48), and tryptophan (0.54).	(Al-Gaby 1998; Langyan et al. 2022)
Brown rice (Oryza sativa L.) (Brown rice protein isolate)	6.8–11.2%	Alanine (4.47), arginine (6.32), aspartic acid (6.94), cystine (1.70), glutamic acid (13.91), glycine (3.53), histidine (1.82), isoleucine (3.47), leucine (6.41), lysine (2.42), methionine (2.27), phenylalanine (4.41), proline (2.88), serine (3.91), threonine (2.92), tryptophan (1.17), tyrosine (4.26), and valine (4.56).	(Juliano, Antonio, and Esmama 1973; Kalman 2014)
Amygdalus pedunculata Pall seeds	28.6%	Aspartic acid (9.68), threonine (1.92), serine (3.18), glutamate (21.7), proline (3.72), glycine (4.17), alanine (3.60), cystine (0.76), and valine (3.25), isoleucine (2.85), leucine (5.76), tyrosine (2.13), phenylalanine (4.69), lysine (1.54), histidine (1.91), tryptophan (0.85), arginine (8.82), and methionine (0.48).	(Li et al. 2020a)

Figure 2. The potential environmental factors affecting the physicochemical and functional properties of proteins.

Figure 3. The potential interactions between (A) protein-polyphenol and (B) protein-polysaccharides.

Table 2. Description, advantages, and limitations of protein extraction methods.

Extraction method	Description	Advantages	Limitations	References
Conventional alkaline extraction (CAE)	In the alkaline process, the broken polished materials are allowed to soak in sodium hydroxide (different concentrations) solution at a temperature (25–95 °C), and extraction time (24 h). After subsequent centrifugation, which was always performed in 2000–15,000 g for 10 min. Applicable on an industrial scale.	High extraction yield (about 95% protein yield). The easy extraction process, where don’t need expensive machines. Low cost. Compatibility with downstream applications.	Long processing time. The pollution of the environment is due to acidic and alkaline wastewater. Poor solubility of protein concentrate and protein isolate when rehydrated. Racemization and denaturation of extracted protein. Formation of dehydro and cross-linked amino acids. Low physicochemical, functional, and nutritional properties.	(Zhao et al. 2023b; Liu et al. 2008)
Subcritical and supercritical water	Sub-supercritical water technology is a thermochemical approach that uses water as a reaction medium. With temperatures and pressures ranging from 100–374 °C and 1 to 22.1 MPa, respectively, the characteristics of water under subcritical thermodynamic conditions are distinct. Water exhibits the properties of a non-polar solvent in supercritical conditions and acts as an intermediary between the gas and liquid phases, where the physicochemical properties of water are affected by changes in temperature and pressure values ranging from ambient to supercritical.	An environmentally friendly alternative to extracting protein with flammable organic solvents. Extraction/separation time is short. High extraction yield. It can be suitably scaled up for industrial applications. The extracted protein showed high physicochemical, functional, and nutritional properties. The high solubility of protein concentrate and protein isolate when rehydrated.	High pressure degrades the quaternary structure of proteins. High pressure and temperature can collectively hydrolyze protein into small fragments and subsequently into free amino acids. Proteins denatured through exposure to high pressure at room temperature. Sub-supercritical water technology is a little bit expensive.	(Zhu et al. 2010; Park, Jeong, and Chun 2019b; Di Domenico Ziero et al. 2020)
Membrane ultrafiltration extraction	Ultrafiltration is a type of membrane technology that can separate high-molecular-weight components like proteins and suspended particles from low-molecular-weight components like mono- and disaccharides, amino acids, inorganic acids, and salts. The pore size of ultrafiltration membrane ranges from about 5 to 100 nm which retains molecules in the range of molecular weight of 10 kDa − 1 MD and is ideally used to concentrate macromolecules such as proteins and polymer molecules. The efficiency of the process can be controlled by control of the operational parameters, which can affect the structure and functionality of proteins in the final product.	Nontoxic method The mild operating conditions and the high selectivity. Less denatured protein than traditional disappointing precipitation. It can separate and recover proteins based on molecular weight. High extraction yield (88–90 % dry basis). High solubility and digestibility of extracted protein when rehydrated. High physicochemical, functional, and nutritional properties.	The increased energy expenditure that’s required for an ultrafiltration facility to operate and higher energy expenditures mean higher costs. The nonspecific binding of proteins to the semipermeable membrane and the compartment of the ultrafiltration device affects the properties of amino acids with high lipophilicity. The membrane clogs due to the precipitates formed by the final product. Membrane contamination means higher costs.	(Navarro-Lisboa et al. 2017; Cassini et al. 2010; Zhao et al. 2023b; Eckert et al. 2019)
Pressurized liquids extraction	Pressurized liquid extraction, also known as accelerated solvent extraction, is a relatively recent automated extraction technique that uses a combination of elevated temperature (50–200 °C) and pressure (500–3000 psi) to keep the solvent in liquid states to obtain protein in a short time (5–10 min).	Nontoxic. Environmentally friendly and efficient method. It is a fully automatic extraction technology. High protein yield and low solvent consumption. It can process multiple samples in the same batch with low reagent usage. Short extraction time.	Racemization and denaturation of extracted protein. The extract is a dilute aqueous solution, which invariably requires further extraction, thus increasing the cost. The high cost of the equipment, as well as rigorous optimization of extraction parameters, namely, temperature and pressure.	(Hernández-Corroto et al. 2020; Guzmán-Lorite, Marina, and García 2022)
Deep eutectic solvents (DESs) extraction	DESs are a type of ionic fluid that typically consists of two or three chemicals that are capable of self-association to form a eutectic mixture with a melting point lower than each ingredient (they typically become liquid at temperatures below 150 °C). DES is composed of a quaternary ammonium salt or metal salt (e.g., choline chloride (ChCl)) and a hydrogen bond donor whose melting point is much lower than that of either component alone.	Biodegradability, sustainability, low volatility, low vapor pressure, low toxicity, non-flammability, and chemical tunability are the characteristics of DESs. The high extraction efficiency of 70.2–93.95% under the optimal conditions. The extracted proteins were non-denatured. The high solubility of protein when rehydrated.	High viscosity hinders the dissolution of proteins and affects the solvent mass transfer phenomena, heat transfer rate, and conductivity. Poor extraction selectivity and inefficient back-extraction method. Some materials used to prepare DESs had mild cytotoxicity such as ChCl-oxalic acid.	(Hernández-Corroto et al. 2020; Guzmán-Lorite, Marina, and García 2022; Zhou et al. 2022b; Wei et al. 2023)
Reverse micelles (RMs) extraction	RMs are self-organized aggregates formed by surfactants in the organic solvent, and nanometer-sized (1–10 nm) water pools are formed by the solubilization of water in their polar cores. Surfactant molecules are arranged with a polar portion on the inside, which can solubilize water, and a polar portion on the outside, which is in touch with the organic solvent. They are also called water-in-oil emulsions. Proteins can be easily retrieved from water matrixes during micelle production and precipitated, purified, and processed for a variety of uses.	RMs are easy to implement. Low cost due to the recovery of surfactant and nonpolar solvents. Convenience and excellent potential in scaling up. Proteins can be solubilized in the water pool of reverse micelles during the extraction. Less protein denaturation and better functional properties. A high ionic strength stripping solution can be used to recover the denatured proteins easily without unfavorable interaction of ionic reverse micelles.	Higher water and energy consumption Poor backward extraction efficiency Loss of surfactant and proteins due to white color insoluble complex forming on the two-phase interface Low purity of the end protein product. The most widely used system consists of sulfosuccinic acid bis (2-ethylhexyl) ester sodium salt and isooctane which are not approved for food use.	(Sun and Bandara 2019; Sánchez-Velázquez et al. 2023)
High-voltage electrical discharge (HVED)	HVED is a non-thermal process that has been used for the treatment of waste products from the food industry in the last few years. HVED is a cutting-edge method that injects energy into an aqueous solution between submerged electrodes. HVED can be used as an extraction method, where it can disrupt the cellular walls and increase the overall mass transfer of the cellular content.	Low environmental burden. The efficiency of cell destruction is extremely high, thus high protein yield and low solvent consumption. Low operating temperature and temperature rise, thus less denaturation of extracted protein with good functional properties. High bio-functional properties of protein.	Many free radicals would be produced during the high voltage discharge, which could lead to oxidized protein, impacting the structure and functions of the protein. These radicals may also oxidize the protein and consequently decrease the yield. HVED has only been applied on a laboratory scale and pilot scale.	(Li, Fan, and Xi 2019a; Mikhaylin 2023)
Enzymatic-assisted extraction (EAE)	EAE is based on the enzymes’ ability to hydrolyze the components of the cell wall and disrupt the structural integrity of the plant cell wall EAE presents applicability to extract proteins from plants, wastes, and by-products by increasing plant cell wall permeability. EAE uses specific enzymes to disrupt the cell wall of source material to improve its extraction yield.	EAE increased the extraction yield and protein content by 2.2–12% compared to CAE alone. Reduced solvent usage with lower energy consumption. Nontoxic treatment to increase extraction efficiency. EAE is an environmentally friendly green processing technique. Faster extraction with a high extraction rate. Amenable to scale up.	The enzymes used in the extraction process are very expensive. Requires an optimization process to minimize enzyme dosage to achieve a high recovery yield. When an enzyme is inactivated or separated, it can need an additional step. Variations in enzyme activity between batches may have certain adverse effects. Product transformation.	(Eckert et al. 2019; Hadidi, Aghababaei, et al. 2023)
Ultrasound-assisted extraction (UAE)	UAE is a sophisticated extraction technique that takes advantage of the acoustic cavitation effect, which is caused by the formation of acoustic cavitation in the solvents and the collapse of asymmetrical micro-bubbles, which generates a tremendous amount of energy, resulting in micro jets, shock waves, high shear force, and heat. With the aid of cavitational, turbulence, and shear forces created within a material by powerful oscillating pressure waves produced by ultrasound technology, plant tissues can be damaged, and proteins can be easily isolated. High-intensity sonication (10–1000 W/cm2) is used for extraction and processing applications.	UAE has been shown to reduce processing times and lower costs. Low environmental burden. Less denaturation of protein due to the low operating temperature and temperature rise. UAE increased the extraction yield of protein (86.1–91.2%). UAE improved physical, chemical, functional, and nutritional modifications of protein isolate and concentrate. High solubility, foam capacity, and foam stability of the extracted protein. High water and oil holding capacity. High product purity.	High energy consumption. Consumption of toxic organic solvents in the extract. Denaturation of proteins at higher pH. High capital investment. High rejection of CO2. UAE can be used in pilot scale only up to date. Ultrasound-induced radicals can oxidize protein, affecting the structure and functions of the protein. Long-time use of the probe can lead to erosion of the metal tip into the protein solution; thus, a metal part can be present in the protein solution	(Liu et al. 2019; Hadidi, Aghababaei, et al. 2023; Prandi et al. 2022)
Microwave-assisted extraction (MAE)	Microwaves are electromagnetic radiation that varies in the range of 0.3–300 GHz and are usually extracted at 2.5–75 GHz in natural products. MAE is the process that uses microwave energy to heat solvents in contact with a sample allowing for the partitioning of analytes from the sample matrix into the solvent. The solvent concentration, the plant material, and the applied microwave power all play a significant role in the efficiency of microwave energy.	Ease of use. Low solvent volume. High protein solubility. High protein digestibility. Higher rate of extraction, where MAE enhanced the protein extraction yield by 33.18% compared to CAE alone. Higher-quality products. Lower CO2 emissions compared to Soxhlet or solvent extraction with stirring. High potential for scale-up.	Expensive equipment. Dielectric properties of the solid material to absorb microwaves. Microwave-induced radicals can oxidize protein, affecting the structure and functions of the protein. Dielectric properties of the solid material to absorb microwaves. Higher extraction time because it needs a clean-up step and waiting time for the extraction vessels to cool down.	(Varghese and Pare 2019; Hadidi, Aghababaei, et al. 2023; Prandi et al. 2022)
High pressure-assisted extraction (HPAE)	HPE operates at low temperatures (often up to 60 °C) and high pressures (typically 100–600 MPa) to extract compounds quickly while using small amounts of organic solvents and providing retrievals comparable to other extraction processes. HP-treatment can modify peptide profiles of various plant and animal-based protein foods.	Environmentally friendly. Nontoxic treatment. Enhances the mass transfer process. Increases extraction efficiency. Reduces extraction time and decreases solvent consumption. HP improved the functional, structural, rheological and antioxidant properties of the protein. HPA treatment increased protein solubility, water, and oil holding capacity. Low thermal degradation Microorganisms’ inactivation. Applicable on an industrial scale.	High equipment cost. Complexity. High energy consumption. Formation of unwanted by-products. This extraction approach can result in the deprotonation of charged groups as well as the breakdown of salt bridges and hydrophobic interactions, leading to protein structural alterations and denaturation.	(D'Alessio et al. 2023; Al-Ruwaih et al. 2019)
Pulse electric field-assisted extraction (PEF)	PEF is a nonthermal technique that could improve the yield and quality of isolated proteins. It is the method’s homogeneity because it treats all tissues (the electric field is diffused through all cells), as opposed to other approaches that just treat the surface. PEF processing includes applying voltage pulses between two electrodes (0.1–80 kV/cm) to treat plant materials or bio-suspensions. This procedure is a real green extraction method due to only distilled water is used during PEF treatment. When a certain electrical potential is reached, electrical breakdown and local structural changes in cell membranes occur, increasing permeability and allowing the protein to pass to the surrounding solution.	An environmentally friendly alternative to extracting protein with flammable organic solvents. Energy consumption is low. PEF is applied for a very short time (10^−4 and 10^−2 s), thus there is little heating effect on the sample (ΔT < 10 °C). Environmentally friendly technique. Less denaturation of the extracted protein. PEF may also manage the degree of membrane destruction, which would influence the selectivity of extraction. High protein solubility. High bio-functional properties of protein. Enhancing extraction yield.	Reversibility of the membrane changes. The efficiency of the method depends on electric field strength and electrode gap. The existence of bubbles during treatment could result in operational problems and non-uniform treatment. High cost of the equipment, which implies a high initial investment. Commercial PEF units are not widely available in many regions worldwide.	(Bou et al. 2022; Yu et al. 2015; Taha et al. 2022)

Figure 4. Potential applications of plant-based proteins in food and related products and their biological activities.

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