Enzymatic hydrolysis of ovalbumin and the functional properties of the hydrolysates

Abstract

Ovalbumin is the predominant protein in egg white and is widely used in cell culture. However, it also can be used to produce peptides with various functional properties. The objectives of this study were to hydrolyze ovalbumin using various enzyme, incubation time, and temperature combinations, and to compare the functional properties of the hydrolysates. Ovalbumin (20 mg/mL) was hydrolyzed with 1% of pepsin, trypsin, α-chymotrypsin, papain, and alcalase, singly or in combination at 37°C, and then the enzymes were inactivated at 100°C for 15 min. Hydrolyzing ovalbumin with pepsin (OAPe), pepsin + papain (OAPePa), pepsin + alcalase (OAPeAl), alcalase + trypsin (OAAlTr), and α-chymotrypsin (OACh) was also effective in producing peptides from ovalbumin, and the peptides produced had strong iron- and copper-binding capacities and antioxidant capability. However, the best treatment of all was the OAAlTr treatment, which showed the highest iron-chelating and antioxidant activities among the enzyme treatments (P < 0.05). Electrospray-ionization mass spectrometry (MS/MS) analysis identified numerous peptides (<5 kDa) from the OAPe, OAPeAl, OACh, OAAlTr, and OAPePa hydrolysates of ovalbumin, but the number and size of peptides varied widely depending on the treatments. The enzymatic hydrolysis significantly increased the functionality of ovalbumin, and the improvement depended upon the composition of peptides produced rather than the number of the peptides produced.

Optimization of the antioxiant peptides production from goat milk casein hydrolyzed by alcalase and papain using respons surface methodology

“…Instead, in the present study, DPPH free radical scavenging rate, Fe 2+ chelating ability, the superoxide radical scavenging activity reached values of 73.81±0.93%, 93.44±1.46% and 51.69 ± 1.17%, respectively. The results obtained in the present study also proved that the compound enzymatic hydrolysis is better than those of single enzyme (Abeyrathne et al, 2014). This is related to the specificity of enzymes, due to the different sites of each enzyme action, the peptide fragments generated are limited.…”

Ovalbumin Hydrolysates Inhibit Nitric Oxide Production in LPS-induced RAW 264.7 Macrophages

“…Lysozyme, ovomucin, and ovotransferrin were sequentially removed from the diluted egg white using the method developed by Abeyrathne et al (2014). Lysozyme was removed first from the egg white solution: Amberlite FPC 3500 resin (5 g/100 mL diluted egg white) was added to the diluted egg white solution and stirred overnight in a 4℃ walk-in cooler using an overhead stirrer set at 250 rpm (RW20 digital, IKA Works, Wilmington, NC, USA) to trap lysozyme.…”

“…Ovalbumin (OVA) has important functional properties that make it useful for gelling, foaming, and emulsifying of food products. Many studies have shown that the hydrolysates or peptides from OVA possess various bioactivities, including antioxidants (Abeyrathne et al, 2014), antihypertensive (Matoba et al, 1999), and antimutagenic effects (Vis et al, 1998). However, few studies have assessed the anti-inflammatory activity of OVA hydrolysates in relation to their inhibitory effects on the production of NO in immune cells.…”

Enzymolysis and glycosylation synergistic modified ovalbumin: functional and structural characteristics

“…[13] Limited enzymatic hydrolysis could reduce molecular weight, but exposured hydrophobic groups previously buried in the protein, [14][15][16] which might increase the protein foaming capacity and emulsifying properties. However, to the best of our knowledge, most papers have been reported to use enzymatic hydrolysis to produce EWP peptides [17][18][19] or reduce its allergenicity, [11] few reports about using enzymatic hydrolysis to improve the functional properties of EWP.…”