Physicochemical and functional properties of albumin, globulin and glutelin fractions of green lentil seed

Osemwota, Etinosa C.; Alashi, Adeola M.; Aluko, Rotimi E.

doi:10.1111/ijfs.15608

Cited by 24 publications

(10 citation statements)

References 63 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The low distribution of protein in the prolamin fraction (3%) aligns with the findings of Bhatty et al (1976) (3.1% prolamin); the authors remarked that these proteins are likely lowmolecular weight nitrogenous compounds. Interestingly, Osemwota et al (2022) reported that the glutelin fraction was the primary protein class in lentils; however, the fractionation sequence employed was slightly different compared to the present work, as the first extraction media was 2% NaCl and the supernatant was dialyzed against water to obtain the albumin fraction (supernatant) and globulin fraction (precipitate). The saline-insoluble residue was then extracted with 70% ethanol (prolamin fraction), and the ethanolinsoluble residue was extracted with 0.05 M NaOH (glutelin fraction) (Osemwota et al, 2022).…”

Section: Protein Distribution and Extractabilitymentioning

confidence: 85%

“…The PRO and GLU fractions had no discernable thermal transition, likely due to the low protein content of the PRO fraction and possible denaturation of the GLU fraction due to the highly alkaline extraction pH ($pH 12) (Ma & Harwalkar, 1984). Notably, Osemwota et al (2022) did observe a thermal transition for lentil glutelins, but the transition enthalpy was relatively low compared to the other fractions, which indicates a high degree of denaturation (Arntfield & Murray, 1981). The AE and EE protein extracts exhibited thermal transitions at lower temperatures compared to the Osborne fractions, which could be attributed to partial unfolding of the proteins under alkaline extraction conditions (pH 9.0) (Lee, Htoon, Uthayakumaran, & Paterson, 2007).…”

Section: Thermal Propertiesmentioning

confidence: 99%

See 1 more Smart Citation

Unveiling the contribution of Osborne protein fractions to the physicochemical and functional properties of alkaline and enzymatically extracted green lentil proteins

Dias,

Yang,

Pham

et al. 2024

Sustainable Food Proteins

View full text Add to dashboard Cite

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.

show abstract

Section: Protein Distribution and Extractabilitymentioning

confidence: 85%

Section: Thermal Propertiesmentioning

confidence: 99%

Unveiling the contribution of Osborne protein fractions to the physicochemical and functional properties of alkaline and enzymatically extracted green lentil proteins

Dias,

Yang,

Pham

et al. 2024

Sustainable Food Proteins

View full text Add to dashboard Cite

show abstract

“…The two predominant fractions of lentil storage proteins, albumin and globulin, account for approximately 11% and 40% of the total protein content, respectively [Neves & Lourenço, 1995]. The share of glutelins in the protein pool is also significant [Osemwota et al, 2022]. All the essential amino acids were determined in the amino acid profile of the lentil proteins [Liu et al, 2022;Osemwota et al, 2022].…”

Section: Introductionmentioning

confidence: 99%

“…The share of glutelins in the protein pool is also significant [Osemwota et al, 2022]. All the essential amino acids were determined in the amino acid profile of the lentil proteins [Liu et al, 2022;Osemwota et al, 2022]. Their content was balanced well and only the contents of tryptophan and sulfur-containing amino acids (methionine and cysteine) were slightly lower than Food and Agriculture Organization/World Health Organization (FAO/WHO) requirement patterns.…”

Section: Introductionmentioning

confidence: 99%

Antioxidant Capacity of Lentil Flour Hydrolysates Obtained with Pancreatin

Sulewska¹,

Rybarczyk-Płońska²,

Karamać³

2022

Pol. J. Food Nutr. Sci.

View full text Add to dashboard Cite

Lentil is a valuable protein-rich crop, the health-promoting value of which can be further enhanced by its protein hydrolysis. In the present study, lentil flour was treated with pancreatin and the antioxidant capacity of the obtained hydrolysates with different degrees of hydrolysis (DH, 4-20%) was determined and compared with that of flour. The molecular weight (MW) distribution of the lentil proteins and their products of hydrolysis was analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Size exclusion-high performance liquid chromatography (SE--HPLC) was deployed to show the profile of low MW compounds of the hydrolysates. Additionally, total phenolic contents were determined with the Folin-Ciocalteu's phenol reagent. The hydrolysates had higher antiradical activity against DPPH • , Trolox equivalent antioxidant capacity (TEAC) measured by the assay with ABTS •+ , ferric reducing antioxidant power (FRAP), and ability to bind Fe 2+ compared to lentil flour. Between the hydrolysates, the highest DPPH • scavenging activity (EC 50 of 0.298 mg/mL), TEAC (98.6 µmol Trolox/g), FRAP (109.2 µmol Fe 2+ /g), antioxidant capacity of lipid-soluble compounds (ACL) determined by photoluminescence method (4.32 µmol Trolox/g), and Fe 2+ chelating activity (80% at hydrolysate concentration of 0.3 mg/mL) were found for those with low DH (4-8%), which contained some subunits of proteins, polypeptides, and peptides with a wide MW range (0.556-66.0 kDa). The total phenolic content increased with increasing DH. In conclusion, the antioxidant capacity of lentil flour can be significantly improved by the limited hydrolysis of its proteins with pancreatin, as a result of the release of polypeptides and peptides with a wide range of MW. Thus modified lentil flour may be addressed and explored in future research as a functional food ingredient.

show abstract

“…An in‐depth analysis of the physicochemical composition of protein fractions included green lentil seed (Osemwota et al ., 2022), two common bean cultivars (Rossi et al ., 2022) and cowpea used in gluten‐free extruded snacks (HewaNadungodage et al ., 2021). Research related to the modelling of techno‐functional properties, on the contrary, focused on the analysis of the pasteurisation effect on the stability of soybean and peanut membrane proteins (Wu et al ., 2022), the effect of malting and roasting on the functional and nutritional properties of chickpea proteins (Kaur & Prasad, 2022), the influence of the germination process on the functional properties of soybeans and soy milk (Hu et al ., 2021), and the combination of pea proteins with guar gums to improve emulsifying properties.…”

mentioning

confidence: 99%