Structure and antioxidant activity of β-lactoglobulin-glycoconjugates obtained by high-intensity-ultrasound-induced Maillard reaction in aqueous model systems under neutral conditions

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

“…The band of β-Lg was located at approximately 18.4 kDa, which was in agreement with previous reports. [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.…”

“…[1,14,15] The effect of ultrasound is associated with cavitation, heating, dynamic agitation, shear stresses, and turbulence. [16] Previous research has indicated that ultrasound has a minimal effect on the secondary and tertiary structures of proteins and did not disrupt covalent bonds, and no change in secondary structure was detected in whey protein isolates treated with ultrasonication (24 kHz, 300 W cm -2 ).…”

“…[17] Similar results were obtained by another report, which showed that ultrasound caused no change in sulfhydryl content. [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.…”

The modifications of bovine β-lactoglobulin: Effects on its structural and functional properties

“…PEF treatment increased the thermal stability of BLG by 4 to 5 °C, as well as its gelation rate. 60 UV irradiation. 56 Ultrasound.…”

Effects of ultrasonic pretreatment and glycosylation on functional properties of casein grafted with glucose

“…In recent years, ultrasound technology, attracting considerable attention, has been widely used in the processing of food. Unique physical, mechanical, or chemical effects of high‐intensity ultrasonic waves are able to change material properties through generation of immense pressure, shear stresses, turbulence, dynamic agitation, and temperature gradient in the medium through which they propagate (Stanic‐Vucinic, Prodic, Apostolovic, Nikolic, & Velickovic, ). Some researchers have studied the effect of the United States on the proteins such as lysozyme (Cavalieri, Ashokkumar, Grieser, & Caruso, ), bovine serum albumin (Gülseren, Güzey, Bruce, & Weiss, ; Stathopulos et al, ), casein (Madadlou, Mousavi, Emam‐Djomeh, Ehsani, & Sheehan, ), whey protein isolates (Gordon & Pilosof, ), whey protein concentrates (Arzeni et al, ; Chandrapala, Zisu, Palmer, Kentish, & Ashokkumar, ), soy protein isolate (Hu et al, ), and black bean protein isolates (Jiang et al, ).…”