Functional Properties of Oat Protein Concentrates

2020 ◽  
Author(s):  
Adeola Alashi
Author(s):  
Francisco Henrique Pereira Neves Leal ◽  
Caroline de Almeida Senna ◽  
Larine Kupski ◽  
Gabriela da Rocha Lemos Mendes ◽  
Eliana Badiale‐Furlong

2020 ◽  
Vol 13 (12) ◽  
pp. 2145-2155
Author(s):  
Sofia Melchior ◽  
Sonia Calligaris ◽  
Giulia Bisson ◽  
Lara Manzocco

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.


LWT ◽  
2021 ◽  
Vol 135 ◽  
pp. 110234
Author(s):  
Shafa'atu Giwa Ibrahim ◽  
Wan Zunairah Wan Ibadullah ◽  
Nazamid Saari ◽  
Roselina Karim

2016 ◽  
Vol 12 (2) ◽  
pp. 195-201 ◽  
Author(s):  
Martin A. Mune Mune ◽  
Armand A. Bouba ◽  
Samuel R. Minka

Abstract Functional properties of Bambara bean protein concentrates (BPCs), as a function of extraction pH and NaCl concentration, were investigated. The results showed that protein content of the concentrates ranged between 69.27% and 74.40%. The addition of NaCl during protein extraction favourably affected water solubility index particularly at pH 10–11. Moreover, the maximum water absorption capacity (4.28 g/g) and oil-holding capacity (OHC) (2.50 g/g) were recorded at extraction pH 11 and in the absence of NaCl. It was also noticed that protein extraction at pH 8–10 was not recommended for applications where high OHC is required. BPCs presenting high emulsifying activity were prepared at NaCl concentration of 0.5 M and pH 7, and at pH 11 without NaCl. Finally, foaming ability (FA) increased with NaCl concentration, and the maximum FA was recorded at pH 7 (114%).


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