High‐intensity ultrasound enhances the immunoglobulin (Ig)G and IgE binding of ovalbumin

Abstract

High-intensity ultrasound can increase the potential allergenicity of OVA. Therefore, high-intensity ultrasound processing of some egg products alone may improve the risk of an allergenic reaction in egg allergy patients to some extent. © 2016 Society of Chemical Industry.

Structural and oxidative modifications, and antioxidant activity of β-lactoglobulin treated by ultraviolet light-C and ultrasound

“…[3,10,15] As shown in Figure 1, no significant changes were observed in the electrophoretic behaviour of β-Lg after ultrasound treatment compared with the control, indicating that β-Lg was still present after exposure to ultrasound without a change in molecular weight induced by protein degradation. Similar results have been obtained in the SDS-PAGE studies of ultrasonication-treated β-Lg, [21] ovalbumin, [19] and black bean protein isolate. [27] The band intensity of β-Lg had slightly decreased after UV-C treatment, especially the 30-min UV-C treatment (Figure 1).…”

“…[1] In contrast, ultrasound can modify the secondary structure of β-Lg and lead to increases in surface hydrophobicity [15] and the propensity of whey protein concentrate to aggregate. [18] However, the free sulfhydryl content, surface hydrophobicity, and ultraviolet absorption of ovalbumin were gradually increased when the ultrasound power was increased from 200 to 600 W. [19] These different results are due to the different protein compositions, pH, and ultrasonication conditions. Nevertheless, the relationship between the potential antioxidant activity and the conformational modification of ultrasound-treated β-Lg has yet to be explained.…”

“…[36] However, ultrasound treatment also causes an increase in the surface hydrophobicity for soy protein isolate (SPI) and ovalbumin. [19,27] The Ho of the ultrasound-treated samples increased due to protein unfolding or decreased due to protein aggregation/partial denaturation of proteins, [27] which was closely related to the protein type and composition, as well as the ultrasound conditions.…”

“…Increased FSH contents were also reported in α-casein after UV-C treatment and in ovalbumin treated with ultrasound. [12,19] Like pulsed light or heat denaturation process, UV-C or ultrasound may induce structure modifications including protein unfolding, which leads to an increase of the exposed hydrophobic groups and a reduction of S-S bonds. [34] The decrease in TSH suggested that β-Lg became progressively denatured and unfolded as heating time increased.…”

“…The procedures for sample preparation and data processing were based on a previous method with slight modifications. [19] β-Lg powder (2 mg) was mixed with KBr, ground, and then pressed into a pellet. Spectral measurements were carried out with a resolution of 4 cm -1 in the wavenumber region of 4,000-400 cm -1 .…”