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.
THE INTERACTION OF PROTEINS WITH CONJUGATE PAIRS OF MOLECULES OR IONS; BOVINE PLASMA PROTEINS VERSUS A 9-AMINOACRIDINE
