Characterization of heat-stable whey protein: Impact of ultrasound on rheological, thermal, structural and morphological properties

Abstract

Ultrasound, an emerging non-thermal technique, has potential to modify the functionality of bio-molecules like protein. In the present study, the impact of ultrasound on whey protein (WP) was assessed with functional, rheological, heat coagulation and transition temperature, SDS-PAGE, FTIR spectra, scanning electron microscopy and transmission electron microscopy. The results of this study showed that the raw WP had broad bimodal particle size distribution while after ultrasonication, modified WP exhibited narrower distribution along with smaller particle size (0.683 ± 0.225 μm) compared to untreated WP (2.453 ± 0.717 μm). The solubility of WP also increased after ultrasonication (72.22 ± 0.68% to 79.21 ± 1.08%). During the rheological evaluation, both the samples exhibited Newtonian behaviour but, the modified WP exhibited dramatically higher storage modulus (G') throughout the temperature profile compared to raw WP mainly due to enhanced proteins aggregation during heating which revealed more elastic and stronger gel. The modified WP exhibited significantly higher (about 6-times) heat stability compared to raw WP which signified that after ultrasonication the WP can withstand higher temperature during processing for longer time. The results were also confirmed by higher transition temperature (T) of modified WP (93.32°) compared to untreated WP (81.93 °C). The SDS-PAGE profile of raw and modified WP showed that the ultrasound significantly decreased the bands density of low molecular weight molecules (β-lactoglobulin and α-lactalbumin). FTIR spectra also showed noticeable difference between the secondary structure component of raw and modified WP. Finally, the structural micrographs of raw and modified WP from SEM and TEM analysis also confirmed the adequacy of modification of WP employing non-thermal techniques. The modified WP revealed smaller, regular and more homogenous and ordered structures compared to untreated sample.

Improvement of quality and flavor of salted egg yolks by ultrasonic assisted cooking

“…3 a) [52] . The retardation of thermal denaturation after ultrasound treatment was also observed in whey and quinoa proteins [53] , [54] . This was possibly due to more stable network microstructure and aggregation were formed as water and lipids released from SEYs [50] , [51] , [53] .…”

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“…The FT-IR spectra of raw and oxidized quinoa protein were evaluated by a Nicolet-6700 FT-IR Spectrometer (Thermo Electron Scientific Instruments Corporation, USA) [24] . The freeze-dried sample (1 mg) was thoroughly mixed and grounded with potassium bromide (100 mg) in the agate mortar.…”

Effect mechanism of ultrasound pretreatment on fibrillation Kinetics, physicochemical properties and structure characteristics of soy protein isolate nanofibrils

“…According to the method of Laemmli [35] and Khatkar et al [36] , SDS-PAGE was performed on a discontinuous buffer system using 10% separating gel and 5% stacking gel. 60 μL sample (2 mg/mL) was mixed with 120 μL 2 × loading buffer, and the mixture was treated in a boiling water bath for 5 min.…”