Biological and functional properties of proteolytic enzyme‐modified egg protein by‐products

Abstract

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.

Effect of heat treatment and enzymatic protein hydrolysis on the degree of hydrolysis and physicochemical properties of edible bird’s nest

“…The solubility of NB60H and AH obtained were similar to those reported for egg albumin (89.8%) (Sathivel et al, 2004) and for egg-yolk protein hydrolysate (87.6%) (Pokora et al, 2013). Nevertheless, the solubility of NB60H and AH were higher than those of milk protein concentrate (45.8%) and milk protein hydrolysate (70.4 -83.3%) (Banach et al, 2013) as well as egg-white protein hydrolysate (68.12%) (Sun et al, 2013).…”

“…However, Amiza et al (2013) reported that the WHC of silver catfish frame hydrolysate at DH 43% was significantly lower compared to those of DH 55% and DH 68%. However, WHC of non-hydrolysed EBN samples obtained in this study was similar to that of egg-white protein hydrolysate (17.28 mL/g), while hydrolysed EBN samples showed comparable WHC to egg-yolk protein hydrolysate (5.12 mL/g) (Pokora et al, 2013), whey protein concentrate (3.77 mL/g) and calcium caseinate (6.11 mL/g) (Carvalho-Silva et al, 2013). Nevertheless, WHC of EBN samples in this study was much higher than those reported for whey protein isolate and hydrolysate (1.82 mL/g and 2.63 mL/g, respectively) (Carvalho-Silva et al, 2013) and fish protein hydrolysates (Wasswa et al, 2007).…”

Production and Identification of Biologically Active Peptides Derived from By-product of Hen Egg-Yolk Phospholipid Extraction

“…The peptides obtained by hydrolysis with unconventional aspartyl proteinase from Y. lipolytica JII1c were characterized by much lower free radical scavenging activity (about 4.5-5.5 times lower than activity of other hydrolysates) and ACE-inhibitory activity. Similarly to our results, hydrolysis of the egg-yolk protein by-product with using various proteases including neutrase, porcine pepsin and protease from C. ficifolia, led to the production of peptides with varied antioxidant and antihypertensive activity (Zambrowicz et al 2015a, b;Eckert et al 2014;Pokora et al 2013). In addition, simultaneous ability of enzymatic hydrolysates to scavenge of DPPH radicals and to inhibit of ACE have been demonstrated in other study (Davalos et al 2004;Lu et al 2010;Zambrowicz et al 2015b).…”

Physicochemical Properties of Egg White Powder from Eggs of Different Types of Bird

“…The egg white solution was then centrifuged at 2330 x g for 30 min. The supernatant was filtered through filter paper, and the volume was measured [13]. WHC was calculated using the following formula:…”