Conjugation of gum Arabic and lentil protein hydrolysates through Maillard reaction: Antioxidant activity, volatile compounds, functional and sensory properties.

Lentil protein hydrolysates (LPH) and lentil protein hydrolysates cross-linked (LPHC) were grafted with gum Arabic (GA) through a wet Maillard reaction at 100°C for 2 h and called MLPH and MLPHC. The samples were assessed for absorption, degree of grafting (DG), surface hydrophobicity, antioxidant activity, molecular weight (MW) profile, chemical alteration, volatile compounds, functional and sensory properties. Results showed that Maillard grafting led to increase in absorption and DG (maximum value: MLPHC), and led to the reduction of the surface hydrophobicity and antioxidant activity (minimum value: MLPHC). MW profiles indicated that MLPH and MLPHC formed new bands at MW >250 kDa. Regarding the Fourier transform infrared spectroscopy (FTIR), Maillard conjugation led to the occurrence of peaks at 1759 and 1765 cm-1, while the intensities of amide I bands at 1637 and 1659 cm-1 and amide II bands at 1498 and 1495 cm-1 were decreased. Hydrolysis, cross-linking, and especially Maillard grafting provided well-balanced content of volatile components. Indeed, the proportions of alcohols, ketones, aldehydes, and acids were changed, thereby, the inherent grassy and planty tastes were diminished while new umami taste was developed. Maillard grafting led to significant improvement of functional properties, while MLPH and MLPHC indicated the highest emulsifying activity at pH 10.0 (73.76 and 70.12 m2/g, respectively) and stability (369.64 and 288.22 min), foaming capacity (88.57% and 142.86%) and stability (60.57% and 72%). Sensory analysis has demonstrated that umami taste was highly developed in MLPH and MLPHC, which can be well considered as meat proteins and flavor enhancers such as monosodium glutamate (MSG).

Augmenting Functional and Sensorial Quality Attributes of Kefir through Fortification with Encapsulated Blackberry Juice.

Kefir is a fermented dairy product claimed to confer many health-promoting effects, but its acidic taste is not appealing to some consumers. Therefore, the aim of this study was to enhance the functional and sensorial quality attributes of kefir through fortification with encapsulated blackberry juice (EBJ). The blackberry juice was successfully encapsulated via freeze-drying using lentil protein isolate (LPI) as the carrier. The encapsulated blackberry juice showed good physicochemical, functional, and morphological properties, as well as microbiological safety for use as a food additive. The kefir was fortified with EBJ in concentrations of 1, 2.5, 5, and 7.5% (w/w), stored for up to 28 days under refrigeration, and periodically evaluated. Parameters such as the viscosity, titrable acidity, and pH indicate that the kefir fortification did not affect its stability during storage. EBJ significantly increased the antioxidant properties of the kefir, depending on the fortification level. Additionally, all the fortified samples provided more anthocyanins than the daily recommended intake. Microbiological profiling demonstrated that good laboratory practice and hygiene were implemented during the experiments. Finally, the panelists showed that higher EBJ concentrations in the kefir resulted in greater overall acceptability, indicating that this encapsulate has the potential to be a substitute synthetic color additive in the dairy industry.

Optimization of complex coacervation parameters for the production of encapsulated black garlic using response surface methodology.

The purpose of this study was to optimize black garlic encapsulation parameters (core/coating ratio, extract concentration, and coacervate/maltodextrin [MD] ratio) using central composite design of the response surface methodology based on encapsulation efficiency (EE) (%). The optimum parameters were determined as 4.0 for the coating material/core ratio, 50% for the extract concentration, and 6.0 for the MD/coacervate ratio depending on the EE (%). The antioxidant activity values were determined as 101 and 134 µmol Trolox/100 g dry weight (DW) for the 2,2-diphenyl-1-picrylhydrazyl and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) methods, respectively, whereas the total phenolic content was 49 mg gallic acid equivalent/100 g DW for the encapsulated black garlic samples. S-Allyl-l-cysteine (SAC), γ-l-glutamyl-SAC (GSAC), γ-l-glutamyl-(S)-trans-1-propenyl-l-cysteine, and allicin were the organosulfur (OS) compounds determined in the samples. The SAC concentration of the encapsulated black garlic samples was determined as 22.36 mg/g, whereas the GSAC content was found at a lower concentration (0.33 mg/g) compared to SAC. The allicin content was quantified to be 0.31 mg/g. The encapsulated samples were also characterized by scanning electron microscopy (SEM) and Fourier transform infrared (FT-IR) spectroscopy. The FT-IR analysis revealed specific functional groups, including hydroxyl, carbonyl, and glycosidic linkage. The interaction between lentil protein isolate and pectin was strong enough to encourage capsule formation as visualized in the SEM images. This study shows the potential of black garlic coacervates as a functional ingredient for the food industry due to their stability, solubility, and preservation of OS and antioxidant compounds.

A Study on a Polymeric Foam Based on Pulse Proteins and Cellulose Fibrils.

Biofoams are a challenge for scientists in terms of innovation. Incorporation of cellulose fibrils (CF), might help improve the microstructure of foams, thus this study focuses on studying the impact of CF on the foaming properties and rheology of lentil protein (LP) foams at various pH and CF concentrations. Additionally, LP-CF mixtures were transformed into solid foams, and their microstructure, physical properties, and morphology were evaluated. CF concentration significantly impacted on LP-CF foam properties, primarily due to high viscosity values. Increased CF concentration resulted in improved FS values (up to 77 min) at all pH values. This is likely attributed to associative interactions and coacervates formation. Also, foam microstructure could be related to apparent viscosity, suggesting the role of viscosity in preserving the integrity of the wet foam structure during freezing and lyophilization processes. However, elevated viscosity values might negatively impact properties such as foaming capacity and produce denser microstructures. The microstructure and morphology analysis revealed that certain foams exhibited a sponge-like structure with open pores and semi-spherical shapes, supported by CF fibers extending and forming layers. However, the structure itself was irregular. While others exhibited non-uniform, irregular pore size, and shape, along with a denser structure. These findings contribute to understanding the behavior of LP-CF mixtures, although additional investigations on mechanical properties, biodegradability, and hydrophobicity are necessary to reach their full potential for various applications.

Formulation and Physical Stability of High Total Solids Lentil Protein-Stabilised Emulsions for Use in Plant Protein-Based Young Child Formulae.

The demand for high-quality plant protein products is increasing and the aim of this work was to evaluate the impact of increasing the total solids content on the formation and stability of lentil protein stabilised oil-in-water emulsions. A series of emulsions were formulated using different proportions of total solids: 23, 26, 29, 32, and 35% (w/v). The emulsions were formulated using three ingredients-lentil protein, sunflower oil, and maltodextrin-which made up 15.85, 27.43, and 56.72% (w/w) of the total solids, respectively. The changes in apparent viscosity, particle size distribution, and colour during thermal processing were evaluated, with the physical stability investigated using an analytical centrifuge. The apparent viscosity of the solutions increased with total solids content (25.6 to 130 mPa.s-1), as did redness colour intensity (a* value increased from 5.82 ± 0.12 to 7.70 ± 0.09). Thermal processing resulted in greater destabilisation for higher total solids samples, as evidenced by greater changes in particle size, along with decreased redness colour. These results bring a better understanding of high total solids plant protein emulsions and factors affecting their stability, which could be used for the development of cost-effective and sustainable processing solutions in the production of plant protein young child formulae.

Lentil Protein and Tannic Acid Interaction Limits in Vitro Peptic Hydrolysis and Alters Peptidomic Profiles of the Proteins.

In this study, the nature of lentil protein-tannic acid (LPTA) interaction and its effect on in vitro pepsin digestion were investigated. LPTA mixtures containing 1% w/v LP and 0.001-0.5% TA were prepared and characterized in terms of particle size, thermal properties, and secondary and tertiary structures. A 20-fold increase in particle size was observed in LPTA0.5% compared to LP control (without TA), indicating aggregation. Static quenching of tryptophan residues within the protein hydrophobic folds was observed. Increasing TA levels also enhanced protein thermal stability. Over 50% reduction in free amino groups of LPTA 0.5%, relative to LP, was observed after pepsin digestion. Cleavage specificity of pepsin and peptidomic profile of LP were modified by the presence of TA in LPTA 0.5%. This study showed that 0.5% w/v TA induced protein aggregation and reduced LP digestibility by hindering the accessibility of pepsin to the protein network, thus modifying the profile of released peptides.

Structure - Functionality of lentil protein-polyphenol conjugates.

Lentil protein isolate (LPI) was conjugated with plant polyphenols (quercetin, rutin, ellagic acid), and the structural and functional characteristics of the conjugates were determined in comparison with the proteins and pure polyphenols. The interaction between polyphenols and protein was achieved by a grafting method at pH 9.0 in the presence of atmospheric oxygen. Surface plasmon resonance measurements showed polyphenols' direct interaction with LPI, with the order of binding strength quercetin > ellagic acid > rutin. The degree of conjugation also followed the same order. Structural analysis of the conjugates was performed using FTIR, intrinsic fluorescence, and surface hydrophobicity. A significant improvement in DPPH radical scavenging and ferric reducing antioxidant power of the conjugates was observed compared to the polyphenols. However, there was a decrease in the surface activity of the conjugates compared to LPI. Such conjugation provides a novel way to combine the advantages of using plant protein and polyphenols in developing a novel food ingredient.

Comparative Study of the Structural and Functional Properties of Membrane-Isolated and Isoelectric pH Precipitated Green Lentil Seed Protein Isolates.

The demand for isolated seed proteins continues to increase but functionality in food systems can be greatly dependent on the extraction method. In this work, we report the physicochemical and functional properties of lentil seed proteins isolated using various protocols. Lentil flour was defatted followed by protein extraction using isoelectric pH precipitation (ISO) as well as NaOH (MEM_NaOH) and NaCl (MEM_NaCl) extractions coupled with membrane ultrafiltration. The MEM_NaCl had significantly (p < 0.05) higher protein content (90.28%) than the ISO (86.13%) and MEM_NaOH (82.55%). At pH 3-5, the ISO was less soluble (2.26-11.84%) when compared to the MEM_NaOH (25.74-27.22%) and MEM_NaCl (27.78-40.98%). However, the ISO had higher yield and protein digestibility (48.45% and 89.82%) than MEM_NaOH (35.05% and 77.87%) and MEM_NaCl (13.35% and 77.61%), respectively. Near-UV circular dichroism spectra showed that the MEM_NaOH had loose tertiary conformation at pH 3, 5, 7 and 9 while ISO and MEM_NaCl had more compact structures at pH 7 and 9. The three protein isolates formed better emulsions (lower oil droplet sizes) at pH 7 and 9 when compared to pH 3 and 5. In contrast, foaming capacity was better at pH 5 than pH 3, 7, and 9.

ß-Glucan Interaction with Lentil (Lens culinaris) and Yellow Pea (Pisum sativum) Proteins Suppresses Their In Vitro Digestibility.

In this study, ß-glucan interaction with lentil and yellow pea proteins and the effect on in vitro protein digestibility were investigated. Proteins were mixed with ß-glucan at mass ratios of 1:0.5, 1:1, and 1:2. The interaction between ß-glucan and the proteins was demonstrated by the decrease in transmittance and surface charge and the increase in particle size of the complexes. Bright-field microscopy showed the formation of aggregates between the biopolymers, although increased molecular size was not observed by discontinuous native polyacrylamide gel electrophoresis. Fluorescence microscopy indicated that ß-glucan formed aggregates with lentil proteins, while the interaction with yellow pea proteins appeared as distinct phases of protein within the ß-glucan network. The in vitro protein digestibility of lentil and pea protein decreased by 27.3 and 34.5%, respectively, in the presence of a ß-glucan mass ratio of 1:2. The findings confirm the possibility to modulate protein digestibility by changing the physical characteristics of a food matrix.

Nutritional and anti-nutritional properties of lentil (Lens culinaris) protein isolates prepared by pilot-scale processing.

Lentil (Lens culinaris) is a high-protein crop with a promising potential as a plant-based protein source for human nutrition. This study investigated nutritional and anti-nutritional properties of whole seed lentil flour (LF) compared to lentil protein isolates (LPIs) prepared in pilot-scale by isoelectric precipitation (LPI-IEP) and ultrafiltration (LPI-UF). Fermentable oligosaccharides, disaccharides, monosaccharides, and polyols (FODMAPs) profiles showed significant reductions in total galacto-oligosaccharides (GOS) contents by 58% and 91% in LPI-IEP and LPI-UF, respectively, compared to LF. Trypsin inhibitor activity (TIA) levels based on dry protein mass were lowered by 81% in LPI-IEP and 87% in LPI-UF relative to LF. Depending on the stage of digestion, the in vitro protein digestibility (IVPD) of LPIs was improved by 35-53% compared to LF, with both products showing a similar long-term protein digestibility to that of bovine serum albumin (BSA). This work supports the use of purified LPI products as a novel source of high quality protein for food applications.

The combined treatment with lentil protein hydrolysate and a mixed training protocol is an efficient lifestyle intervention to manage cardiovascular and renal alterations in obese Zucker rats.

PURPOSE: Functional and structural changes in cardiovascular and renal systems resulting from obesity and metabolic syndrome represent a severe risk to human health. Lifestyle interventions such as combining healthy diet with adequate physical exercise protocols are good strategies to manage these pathologies. In this research, the effects of lentil protein hydrolysate administration, combined or not with a mixed training protocol, on insulin resistance, cardiovascular and renal functionality were studied in the obese Zucker rat experimental model. METHODS: Thirty-two rats (16 lean and 16 obese subdivided in sedentary and trained animals) were administered lentil protein hydrolysate, whereas another 32 subdivided in the same experimental design were administered placebo. The experiment lasted for 8 weeks. At the end of the experimental period, insulin resistance and different parameters of cardiovascular and renal functionality were measured. RESULTS: The individual or combined interventions with lentil protein hydrolysate and mixed training protocol were efficient at counteracting some of the metabolic, cardiovascular and renal alterations characterizing the obese Zucker rat. Specifically, lentil protein hydrolysate decreased hyperphagia, amplitude of QRS complex, plasma ACE and selectin E expression in aorta, while increasing urinary volume and pH. Exercise showed beneficial actions on HOMA-IR, QRS amplitude, QTc interval, urinary volume, kidney weight and Mn-SOD activity. Interestingly, most of the mentioned benefits of exercise were more consistent when protein hydrolysate was also administered. CONCLUSION: The interesting synergies between the two interventions assessed qualify them as alternative therapeutic strategies to treat cardiovascular and kidney diseases associated to the metabolic syndrome.

Application of high-pressure homogenization (HPH) to modify functional, structural and rheological properties of lentil (Lens culinaris) proteins.

The ability of high-pressure homogenization (HPH) to modify the functional, structural and rheological properties of lentil protein isolate (LPI) suspensions were investigated. Protein patterns remained unchanged with HPH treatment. Particle size significantly decreased up to 100 MPa treatment and size distribution was mono-modal after 50 MPa. Microstructural images revealed that increasing pressure from 50 to 150 MPa caused further unfolding of protein particles, which well supported to water solubility, emulsifying, foaming and particle size results. LPI suspensions had shear thinning behavior and results were well fitted to Ostwald de-Waele model (R2 ≥ 0.989). Apparent viscosity and homogenization pressure were modeled with exponential and sigmoidal functions (R2 ≥ 0.983). However, weak gel-like structure was observed from all samples due to G' > G″, and higher homogenization pressures than 50 MPa caused more pronounced gelation after 51.78 °C. These results stated that HPH treatment has a good potential to modify the functional, structural and rheological properties of LPI suspensions.

Effect of molecular mass and degree of substitution of carboxymethyl cellulose on the formation electrostatic complexes with lentil protein isolate.

The electrostatic interaction between lentil protein isolate (LPI) and carboxymethyl cellulose (CMC) of different molar mass (MM; 90 and 250 kDa) and degree of substitution (DS; 0.7, 0.9 and 1.2%) was examined during a turbidimetric pH acid-titration over a pH (8.0-1.5) and mixing ratio (LPI: CMC; 1:1-10:1) rang. For LPI-CMC (0.7% DS, 250 kDa) at a 1:1 ratio, pHs linked soluble (pHc) and insoluble complexes (pHϕ1) being formed, maximum coacervation (pHopt) and the dissolution of complexes (pHϕ2) occurred at pHs of 6.8, 2.6, 2.1 and 1.7, respectively. As the mixing ratio increased, pHc and pHϕ2 remained unchanged; however, pHϕ1 and pHopt shifted to higher pHs until plateauing at a 4:1 mixing ratio. Molecular mass and DS had no significant effect on critical pHs but did have an impact on the size and number of complexes formed. The maximum optical density at pHopt was found to decrease from 0.495 to 0.406 as the DS increased from 0.7% to 1.2% on the CMC (constant at 250 kDa), suggesting that complexes were likely smaller as they scattered less light. As the MM of CMC decreased from 250 to 90 kDa (at 0.7% DS), maximum optical density increased from 0.495 to 0.527, respectively. Confocal laser scanning microscopy preformed at pHopt showed an increasing number of aggregates as the DS or MM of CMC decreased. From isothermal titration calorimetry (ITC), larger enthalpy values in LPI-CMC with increased DS and MM were observed.

Effect of pH on the formation of electrostatic complexes between lentil protein isolate and a range of anionic polysaccharides, and their resulting emulsifying properties.

This research investigated the effect of pH on forming electrostatic complexes between lentil protein isolate (LPI) and a range of anionic polysaccharides [carboxymethyl cellulose (CMC), gum Arabic (GA), alginate (AL), and ι-carrageenan (CAR)] at 4:1 LPI-polysaccharide mixing ratio, and their resulting emulsifying abilities. Maximum optical densities were found to be 0.486, 0.716, 0.310, and 0.190 for LPI-CMC, LPI-GA, LPI-AL, and LPI-CAR, respectively indicating the level of aggregate size and growth. LPI-CAR emulsion displayed the highest emulsion stability (ES) because of its higher continuous phase and emulsion viscosities, lower mean droplet sizes, and negatively charged droplets. They also formed much smaller complexes within solution due to their high negative charge. All other LPI-polysaccharide systems formed less stable emulsions than LPI alone due to the larger sizes of both complexes and oil droplets.

Influence of process (extrusion/thermo-compression, casting) and lentil protein content on physicochemical properties of starch films.

Starch films often present high water sensitivity, affecting their barrier and mechanical properties. The effects of processing technique, extrusion/thermo-compression and casting, and lentil protein concentration (0, 0.75 wt.% and 1.5 wt.%) on biodegradable starch films were investigated. Extrusion/thermo-compression process increased in 90% the mechanical resistance of starch films produced following the casting methodology and decreased their moisture content, water solubility and water vapor permeability in 35%, 23%, and 50%, respectively. In the presence of the protein, the mechanical properties (Young modulus and stress at break) and the water tolerance improved due to the crosslinking phenomenon prompted between the protein and the polymeric backbone, being these effects more pronounced on the extruded formulations. All samples resulted thermal stable until 240 °C and biodegraded in compost in 5 weeks. This work revealed that extrusion/thermo-compression process and proteins as crosslinking of starch are two alternatives to improve the drawbacks of starch-based materials.

Reduction of off-flavours and the impact on the functionalities of lentil protein isolate by acetone, ethanol, and isopropanol treatments.

The changes of flavour profiles in lentil protein isolate (LPI) in response to organic solvent treatments (acetone, ethanol, and isopropanol; 35-95% v/v), and the resulting impacts on the isolate colour and physicochemical and functional attributes were investigated. The major constituents of volatile compounds were aldehydes (∼46.59%) and (E,E)-3,5-octadien-2-one (∼31.79%) in the untreated LPI. Acetone treatment greatly raised ketones by ∼79.59%. In contrast, ethanol and isopropanol, except at 95% (v/v), significantly lowered total volatile compounds and had higher protein contents (∼84.55%) than the others (∼76.98%); surface charge, surface hydrophobicity, solubility and emulsion stability of these LPIs were examined. LPIs obtained from 75% (v/v) ethanol and isopropanol treatments showed slightly lower solubility but improved surface hydrophobicity to produce emulsions with a similar stability as compared with the untreated LPI. Overall, ethanol and isopropanol treatments (75% v/v) produced high quality off-flavour-reduced LPIs which may be used in various food systems.

Stability and in vitro release behaviour of encapsulated omega fatty acid-rich oils in lentil protein isolate-based microcapsules.

The objective of this study was to investigate the use of a lentil protein isolate-based microcapsule design as a platform for entrapping different types of omega fatty acid-rich oil (e.g. canola, fish and flaxseed oils) and to characterise differences in the physical properties (e.g. moisture content, water activity, colour, wettability, particle size, surface oil and entrapment efficiency), storage stability and in vitro release behaviour of the entrapped oils. All microcapsules displayed similar physical properties regardless of the core material. Free fatty acid content, peroxide value, 2-thiobarbituric acid reactive substances and accelerated oxidation test were investigated between the free and encapsulated oils to determine protective effects from microencapsulation and found the wall material provided the greatest protective effect to the fish oils relative to the others. Based on an in vitro release assay, it was proposed that different intrinsic properties of fatty acids (e.g. polarity, conformation, chain length and number of double bonds) led to different release properties under simulated conditions. For instance, more encapsulated canola oil (∼8.9%) was released within simulated gastric fluid, whereas more encapsulated fish oil (∼73.4%) was released within simulated gastrointestinal fluids. Overall, the capsule design used in this study could be potentially used as a universal platform to deliver more healthy oils.

Effect of lentil proteins isolate concentration on the formation, stability and rheological behavior of oil-in-water nanoemulsions.

The formation, stability and rheology of 5wt% oil-in-water nanoemulsions as a function of lentil protein isolate concentration (0.5-5wt%) at pH 3.0 was investigated for 28days. All nanoemulsions, except 1wt% protein, showed bimodal droplet size distribution where the larger diameter peak was ascribed to protein aggregates and entrapped oil droplets. The average droplet size for all nanoemulsions measured from the lower diameter peak ranged from 161 to 357nm, which did not change over 28days. Stable flowable nanoemulsions were formed at 1-2wt% protein concentrations. Nanoemulsions with 3 and 5wt% protein formed strong non-flowable gels which showed a two-step yielding behavior during strain-sweep rheology, indicating gel formation by interconnected clusters of proteins and oil droplets. This study demonstrated that lentil protein has a potential to be utilized as an emulsifier in nanoemulsions, as well as in the formation of emulsion gels at higher protein concentrations.

Impact of pH on molecular structure and surface properties of lentil legumin-like protein and its application as foam stabilizer.

The capacity of a protein to form and stabilize foams and emulsions depends on its structural characteristics and its physicochemical properties. The structural properties of lentil legumin-like protein including molecular weight, hydrodynamic size, surface charge and hydrophobicity, and conformation were studied in relation to its air-water interfacial behaviors. Kinetics study suggested that the foaming stability was closely related to the surface conformation of the protein that strongly affected adsorption and re-organization of the protein layer at the air-water interface. Foams prepared at neutral pH showed dense and strong networks at the interface, where combination of the α-helix secondary structure, medium hydrodynamic molecular size, and balance between solubility/hydrophobicity all contributed to the formation of such strong protein network at the interface. At pH 5.0, the protein formed a dense and thick network composed of randomly aggregated protein particles at the air-water interface. Whereas at pH 3.0, the unordered structure increased intra-protein flexibility producing a less compact and relaxed interface that reduces elasticity modulus with time and reduced foam resistance against collapse. This research revealed that lentil legumin-like protein could form long-life foams at mild acidic and neutral pH. The potential for use of lentil protein as a novel foaming plant-based stabilizer is demonstrated in food and non-food applications where stable, long-life foams are required.

Savinase, the most suitable enzyme for releasing peptides from lentil (Lens culinaris var. Castellana) protein concentrates with multifunctional properties.

The aim of this study was to produce multifunctional hydrolysates from lentil protein concentrates. Four different proteases (Alcalase, Savinase, Protamex, and Corolase 7089) and different hydrolysis times were evaluated for their degree and pattern of proteolysis and their angiotensin I-converting enzyme (ACE) inhibitory and antioxidant activities. Alcalase and Savinase showed the highest proteolytic effectiveness (P ≤ 0.05), which resulted in higher yield of peptides. The hydrolysate produced by Savinase after 2 h of hydrolysis (S2) displayed the highest ACE-inhibitory (IC50 = 0.18 mg/mL) and antioxidant activity (1.22 µmol of Trolox equiv/mg of protein). Subsequent reverse-phase HPLC-tandem mass spectrometric analysis of 3 kDa permeates of S2 showed 32 peptides, mainly derived from convicilin, vicilin, and legumin containing bioactive amino acid sequences, which makes them potential contributors to ACE-inhibitory and antioxidant activities detected. The ACE-inhibitory and antioxidant activities of S2 were significantly improved after in vitro gastrointestinal digestion (P ≤ 0.05). Multifunctional hydrolysates could encourage value-added utilization of lentil proteins for the formulation of functional foods and nutraceuticals.