Enzymolysis and glycosylation synergistic modified ovalbumin: functional and structural characteristics

Figures & data

Figure 1. Analysis of the emulsifying properties and foaming properties of the modified protein.

Table 1. Three evaluated indices of OVA, hydrolyzed OVA and modified OVA.

Indices	OVA	Hydrolyzed OVA	Modified OVA
Water binding capacity (g/g)	1.56 ± 0.01^a	3.64 ± 0.09^b	5.82 ± 0.13^c
Oil binding capacity (mL/g)	3.53 ± 0.12^a	4.35 ± 0.11^b	6.83 ± 0.15^c
Gel strength (g)	593 ± 4.36^a	654 ± 4.73^b	871 ± 6.24^c

Values are means ± SD.

Letters indicate significant (p < 0.05) difference within the same column.

Figure 2. Thermal properties of OVA.

Figure 3. SDS-PAGE of OVA before and after hydrolyzed and glycosylated modification. Lane 1, ovalbumin; Lane 2, hydrolyzed ovalbumin; Lane 3, modified ovalbumin; Lane Mark, standard protein markers.

Figure 4. UV spectra (a) and FTIR spectra (b) of OVA.

Figure 5. Scanning electron microscopy image of OVA: (a) native OVA (300×), (b) hydrolyzed OVA (100×), (c) modified OVA (100×), (d) modified OVA (500×).