Physicochemical, anti‐nutritional and functional properties of air‐classified protein concentrates from commercially grown Canadian yellow pea ( Pisum sativum ) varieties with variable protein levels

Pea protein concentrates and isolates are important raw materials for the production of plant-based food products. To select suitable peas (Pisum sativum L.) for protein extraction for further use as food ingredients, twelve different cultivars were subjected to isoelectric precipitation and spray drying. Both the dehulled pea flours and protein isolates were characterized regarding their chemical composition and the isolates were analyzed for their functional properties, sensory profiles, and molecular weight distributions. Orchestra, Florida, Dolores, and RLPY cultivars showed the highest protein yields. The electrophoretic profiles were similar, indicating the presence of all main pea allergens in all isolates. The colors of the isolates were significantly different regarding lightness (L*) and red-green (a*) components. The largest particle size was shown by the isolate from Florida cultivar, whereas the lowest was from the RLPY isolate. At pH 7, protein solubility ranged from 40% to 62% and the emulsifying capacity ranged from 600 to 835 mL g−1. The principal component analysis revealed similarities among certain pea cultivars regarding their physicochemical and functional properties. The sensory profile of the individual isolates was rather similar, with an exception of the pea-like and bitter attributes, which were significantly different among the isolates.

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Enzymatic and extrusion pretreatments of defatted rice bran to improve functional properties of protein concentrates

International Journal of Food Science & Technology ◽

10.1111/ijfs.15017 ◽

2021 ◽

Author(s):

Francisco Henrique Pereira Neves Leal ◽

Caroline de Almeida Senna ◽

Larine Kupski ◽

Gabriela da Rocha Lemos Mendes ◽

Eliana Badiale‐Furlong

Keyword(s):

Functional Properties ◽

Rice Bran ◽

Protein Concentrates ◽

Defatted Rice Bran

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Type and Amount of Legume Protein Concentrate Influencing the Technological, Nutritional, and Sensorial Properties of Wheat Bread

Applied Sciences ◽

10.3390/app11010436 ◽

2021 ◽

Vol 11 (1) ◽

pp. 436

Author(s):

Nastasia Belc ◽

Denisa Eglantina Duta ◽

Alina Culetu ◽

Gabriela Daniela Stamatie

Keyword(s):

Wheat Bread ◽

Soy Protein Concentrate ◽

Protein Concentrate ◽

Total Change ◽

Protein Concentrates ◽

Overall Acceptability ◽

Protein Levels ◽

Legume Protein ◽

Bread Properties

Plant protein concentrates are used to enhance the nutritional quality of bread and to respond to the demand of consumers with respect to increased protein intake. In the present study, bread samples were produced using pea protein concentrate (PP) and soy protein concentrate (SP) substituting wheat flour by 5%, 10%, and 15%. The protein levels were between 1.2- and 1.7-fold (PP) and 1.1- and 1.3-fold (SP) higher than the control bread. The incorporation of 10% and 15% PP allowed for the achievement of a “high protein” claim. Water absorption was correlated with the protein contents of the breads (r = 0.9441). The decrease in bread volume was higher for the PP than SP incorporations, and it was highly negatively correlated with the protein content (r = −0.9356). Soy breads had a softer crumb than pea breads. The total change in crumb colour was higher in the PP than SP breads. The soy breads had an overall acceptability between 6.3 and 6.8, which did not differ (p > 0.05) from the control. PP breads were statistically less liked (p < 0.05). The results underlined that the choice of the type and amount of protein concentrates influenced the bread properties differently.

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Functional properties of protein fractions obtained from commercial yellow field pea (Pisum sativum L.) seed protein isolate

Food Chemistry ◽

10.1016/j.foodchem.2011.03.116 ◽

2011 ◽

Vol 128 (4) ◽

pp. 902-908 ◽

Cited By ~ 120

Author(s):

Abayomi P. Adebiyi ◽

Rotimi E. Aluko

Keyword(s):

Pisum Sativum ◽

Functional Properties ◽

Seed Protein ◽

Protein Isolate ◽

Field Pea ◽

Protein Fractions ◽

Pisum Sativum L

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Functional Properties of Lupin Seed (Lupinus mutabilis) Proteins and Protein Concentrates

Journal of Food Science ◽

10.1111/j.1365-2621.1982.tb10110.x ◽

1982 ◽

Vol 47 (2) ◽

pp. 491-497 ◽

Cited By ~ 188

Author(s):

S. K. SATHE ◽

S. S. DESHPANDE ◽

D. K. SALUNKHE

Keyword(s):

Functional Properties ◽

Protein Concentrates ◽

Lupin Seed ◽

Lupinus Mutabilis

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Functional properties of the α-chain of a major legumin subunit of Pisum sativum legumin

Nahrung/Food ◽

10.1002/(sici)1521-3803(199802)42:01<2::aid-food2>3.3.co;2-t ◽

1998 ◽

Vol 42 (01) ◽

pp. 2-6

Author(s):

S. Dudek ◽

J. Gueguen ◽

J.-P. Krause ◽

K.D. Schwenke

Keyword(s):

Pisum Sativum ◽

Functional Properties ◽

Α Chain

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Understanding the impact of moderate-intensity pulsed electric fields (MIPEF) on structural and functional characteristics of pea, rice and gluten concentrates

Food and Bioprocess Technology ◽

10.1007/s11947-020-02554-2 ◽

2020 ◽

Vol 13 (12) ◽

pp. 2145-2155

Author(s):

Sofia Melchior ◽

Sonia Calligaris ◽

Giulia Bisson ◽

Lara Manzocco

Keyword(s):

Electric Fields ◽

Functional Properties ◽

Structural Changes ◽

Pulsed Electric Fields ◽

Moderate Intensity ◽

Intramolecular Rearrangement ◽

Structural Modifications ◽

Protein Concentrates ◽

Protein Nature ◽

The Impact

Abstract Aim The effect of moderate-intensity pulsed electric fields (MIPEF) was evaluated on vegetable protein concentrates from pea, rice, and gluten. Methods Five percent (w/w) suspensions of protein concentrates (pH 5 and 6) were exposed to up to 60,000 MIPEF pulses at 1.65 kV/cm. Both structural modifications (absorbance at 280 nm, free sulfhydryl groups, FT-IR-spectra) and functional properties (solubility, water and oil holding capacity, foamability) were analyzed. Results MIPEF was able to modify protein structure by inducing unfolding, intramolecular rearrangement, and formation of aggregates. However, these effects were strongly dependent on protein nature and pH. In the case of rice and pea samples, structural changes were associated with negligible modifications in functional properties. By contrast, noticeable changes in these properties were observed for gluten samples, especially after exposure to 20,000 pulses. In particular, at pH 6, an increase in water and oil holding capacity of gluten was detected, while at pH 5, its solubility almost doubled. Conclusion These results suggest the potential of MIPEF to steer structure of proteins and enhance their technological functionality.

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