Background and objectives
Faba bean proteins isolates did not show sufficient functional properties for food applications due to poor solubility. Enzymatic treatments and ultrafiltration may improve solubility and functional properties of faba bean protein. The aim of the present work was to investigate the effect of different proteases (pepsin, trypsin, flavourzyme® 500 L, neutrase® 0.8 L), hydrolysis time and ultrafiltration technique on the physicochemical and functional characteristics of faba bean protein.
Findings
The protein solubility increased from 24.4% to 88.8% at pH 7 and 81.0% at pH 5 by pepsin hydrolysis (15 min). Their foaming capacity (FC) increased from 31.2% to 122.2% at pH 5 and 66.7% to 131.2% at pH 7 and the oil holding capacity (OHC) increased from 6.12 to 8.21 g/g by pepsin hydrolysis. Fraction I (Mw > 10 kDa) and II (Mw: 5–10 kDa) obtained after pepsin hydrolysis and ultrafiltration demonstrated further improved foaming and oil holding capacity and much improved emulsifying capacity.
Conclusions
Enzymatic hydrolysis and ultrafiltration provided a strategy to significantly improve faba bean protein solubility and functional properties.
Significance and novelty
Faba bean protein hydrolysates and ultrafiltration fractions are good sources of protein with excellent solubility and functionality.
Bioactive peptides derived from food have been increasingly popular due to their therapeutic properties. Of particular importance are peptides with a multidirectional activity that can be used in the treatment and prevention of diet-related diseases. This paper attempts to utilize a by-product of phospholipid extraction from egg yolk as a source of peptides with a broad spectrum of biological activity. In addition, in this research we used a non-commercial enzyme obtained from Asian pumpkin, which has not been sufficiently researched in terms of its ability to release biopeptides from food proteins. In the present study the biological properties of peptides, derived from egg-yolk protein by-products (YP) remaining after phospholipid extraction, and their four synthetic analogs were investigated with regard to their antioxidant (radical scavenging capacity, Fe 2+ chelating effect, reducing power (FRAP)) and antidiabetic (a-glucosidase and DPP-IV inhibitory activities) properties. One of them, with the sequence LAPSLPGKPKPD, exhibited the highest antioxidant activity (free radical scavenging activity (6.03 mM Trolox eq per mg protein); FRAP (296.07 mg Fe 2+ per mg protein)). This peptide also revealed the strongest DPP-IV (361.5 mmol L À1 ) and a-glucosidase (1065.6 mmol L À1 ) inhibitory activities, a novel multifunctional effect for peptides from an egg-yolk hydrolysate.
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