Abstract:Consumers’ attitudes toward more plant-based components
in their diet has greatly driven the exploration of functional plant
proteins. The aim of this study was to systematically investigate
the structural and functional properties, nutritional and aromatic
profiles, and in vitro digestion of protein fractions from the underexploited
lentil grain. Albumin (LA), globulin (LG), and its subunits legumin
(LL) and vicilin (LV) were fractionated from red lentil flour through
alkaline extraction–isoelectric precipita… Show more
“…The increase in measurement pH from 4.5 to 7.0 increased the absolute zeta potential (more negative) of all fractions and extracts. Of the fractions, only the GLO fraction exhibited appreciable surface charge at pH 4.5, which suggests that the isoelectric points of the ALB, PRO, and GLU fractions were around pH 4.5-5 in accordance with previous literature for the isoelectric points of lentil proteins (Chang et al, 2022;Jarpa-Parra et al, 2014). At pH 7.0, the PRO fraction had the highest absolute value for surface charge (À39 mV), followed by the ALB (À23 mV), GLU (À24 mV), and GLO (À18 mV) fractions.…”
Section: Secondary Structure and Physicochemical Propertiessupporting
Lentil proteins are gaining popularity as food ingredients, serving both functional and nutritional purposes. To better understand the properties of lentil proteins extracted using commercially relevant methods (alkaline and enzymatic), sequential fractionation by solubility (Osborne fractionation) was performed and the physicochemical, thermal, and functional properties of the extracts were characterized. Fractionation revealed that 43% of lentil proteins were water‐soluble (ALB, albumin‐rich), 37% salt‐soluble (GLO, globulin‐rich), 14% alkaline‐soluble (GLU, glutelin‐rich), and 3% ethanol‐soluble (PRO, prolamin‐rich). Protein extraction yields of 81% and 87% were achieved by alkaline (pH 9.0, 50 °C, 1:10 solids‐to‐liquid ratio, 60 min) and enzymatic extraction (same conditions with 0.5% (w/w) Alkaline Protease), respectively. Proteomic analysis allowed for the identification of 129 proteins among all extracts, and the ALB and GLO fractions exhibited similar protein profiles as the alkaline‐extracted proteins. The secondary structure of the protein fractions was dominated by β‐sheets (20%–35%) and unordered structures (45%–48%). Surface hydrophobicity and absolute zeta potential were negatively correlated (R2 = 0.82, p < 0.05). ALB and GLO fractions had higher denaturation temperatures than the alkaline/enzymatically‐extracted proteins, potentially due to partial denaturation. ALB and GLO fractions also had the highest solubility and emulsification capacities. Under acidic conditions, enzymatically‐extracted proteins exhibited better solubility (58 vs. 33%), emulsification (499 vs. 403 g oil/g dry sample), and similar foaming capacity (57%–69%) compared to alkaline‐extracted proteins. This study showed that alkaline and enzymatically extracted lentil proteins share physicochemical and functional characteristics with water‐ and salt‐extracted proteins, demonstrating the efficacy of these single‐stage extraction strategies in achieving high yields and desirable functionality.
“…The increase in measurement pH from 4.5 to 7.0 increased the absolute zeta potential (more negative) of all fractions and extracts. Of the fractions, only the GLO fraction exhibited appreciable surface charge at pH 4.5, which suggests that the isoelectric points of the ALB, PRO, and GLU fractions were around pH 4.5-5 in accordance with previous literature for the isoelectric points of lentil proteins (Chang et al, 2022;Jarpa-Parra et al, 2014). At pH 7.0, the PRO fraction had the highest absolute value for surface charge (À39 mV), followed by the ALB (À23 mV), GLU (À24 mV), and GLO (À18 mV) fractions.…”
Section: Secondary Structure and Physicochemical Propertiessupporting
Lentil proteins are gaining popularity as food ingredients, serving both functional and nutritional purposes. To better understand the properties of lentil proteins extracted using commercially relevant methods (alkaline and enzymatic), sequential fractionation by solubility (Osborne fractionation) was performed and the physicochemical, thermal, and functional properties of the extracts were characterized. Fractionation revealed that 43% of lentil proteins were water‐soluble (ALB, albumin‐rich), 37% salt‐soluble (GLO, globulin‐rich), 14% alkaline‐soluble (GLU, glutelin‐rich), and 3% ethanol‐soluble (PRO, prolamin‐rich). Protein extraction yields of 81% and 87% were achieved by alkaline (pH 9.0, 50 °C, 1:10 solids‐to‐liquid ratio, 60 min) and enzymatic extraction (same conditions with 0.5% (w/w) Alkaline Protease), respectively. Proteomic analysis allowed for the identification of 129 proteins among all extracts, and the ALB and GLO fractions exhibited similar protein profiles as the alkaline‐extracted proteins. The secondary structure of the protein fractions was dominated by β‐sheets (20%–35%) and unordered structures (45%–48%). Surface hydrophobicity and absolute zeta potential were negatively correlated (R2 = 0.82, p < 0.05). ALB and GLO fractions had higher denaturation temperatures than the alkaline/enzymatically‐extracted proteins, potentially due to partial denaturation. ALB and GLO fractions also had the highest solubility and emulsification capacities. Under acidic conditions, enzymatically‐extracted proteins exhibited better solubility (58 vs. 33%), emulsification (499 vs. 403 g oil/g dry sample), and similar foaming capacity (57%–69%) compared to alkaline‐extracted proteins. This study showed that alkaline and enzymatically extracted lentil proteins share physicochemical and functional characteristics with water‐ and salt‐extracted proteins, demonstrating the efficacy of these single‐stage extraction strategies in achieving high yields and desirable functionality.
“…Due to its excellent antioxidant capabilities, carrageenan has been employed as the substrate for edible films in recent years [66] . Furthermore, the structure of proteins is closely related to these physicochemical properties (e.g., antioxidant properties, aromatic profile, and in vitro digestibility) [67] , [68] . Also, the antioxidant capacity of the UMP/LBG group was 19.71% higher than that of the UMP.…”
“…The banding transition in the prefabricated gel of different MRN/GAD samples (MRN/GAD3–MRN/GAD7) was measured through gel electrophoresis [20] , [21] . Briefly, 120 μL of various MPN samples (MRN/GAD3–MRN/GAD7, 2.4 g/L) were utilized to dilute 30 μL of high-concentration sample buffer.…”
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