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.

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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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Enzymatic hydrolysis led to improve functional properties and biological activity of protein by-products, which can be further used as protein ingredients for food and feed applications. The effects of proteolytic enzyme modification of egg-yolk protein preparation (YP) and white protein preparation (WP), obtained as the by-products left during the course of lecithin, lysozyme, and cystatin isolation on their biological and functional properties, were evaluated by treating a commercial Neutrase. The antihypertensive and antioxidative properties of YP and WP hydrolysates were evaluated based on their angiotensin-converting enzyme (ACE)-inhibitory activity and radical scavenging (DPPH) capacity, ferric reducing power, and chelating of iron activity. The functionality of obtained hydrolysates was also determined. Neutrase caused a degree of hydrolysis (DH) of YP and WP by-products: 27.6% and 20.9%, respectively. In each of them, mixture of peptides with different molecular masses were also observed. YP hydrolysate showed high levels of antioxidant activity. The scavenging capacity, ferric reducing power, and chelating capacity were observed at the level: 0.44 μmol/L Trolox mg−1, 177.35 μg Fe2+ mg−1, and 549.87 μg Fe2+ mg−1, respectively. YP hydrolysate also exhibited significant ACE-inhibitory activity, in which the level was 59.2 μg. Protein solubility was significantly improved as the DH increased. WP hydrolysate showed high water-holding capacity of 43.2. This study indicated that YP and WP hydrolysates could be used in foods as natural antioxidants and functionality enhancers.

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Barley and lentil proteins have good emulsifying and foaming capacity, which make them suitable ingredients in many food formulations. The aim of this research was to develop protein-enhanced foods based on barley and lentil proteins using doughnut as a food model. In enriched doughnut formulations, barley proteins were used to substitute for 20% of the wheat flour (doughnuts labeled as barley doughnut, barley/lentil doughnut [BLD], and vegan doughnut [VD]) and lentil proteins were used as an egg replacer (in BLD and VD doughnuts). A VD formulated with barley and lentil proteins to replace egg white protein and milk was also tested. The physicochemical parameters, proximate composition, and sensory qualities of the prepared doughnuts were studied and compared with the control doughnut (CD) containing egg white and milk. The protein-enriched doughnuts showed better cooking characteristics with reduced cooking loss and diameter reduction compared to the control. In addition, they had a higher protein and β-glucan content. During the storage-stability test, the doughnuts containing lentil and barley proteins showed higher values for hardness, chewiness, and gumminess compared to the control. However, the sensory scores for appearance, flavor, and overall liking were rated more favorable toward the CD. It is also noticed that the fat content and caloric values increased for some protein-enriched doughnut formulations. Considering the consumers' demand of high-protein convenient snack foods, the doughnuts prepared with barley and lentil proteins may have potential for commercialization with some improvements.