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 peak ) 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…
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The higher band intensities in sonicated samples are likely due to ultrasound-induced dissociation of soluble protein aggregates.
“likely due to ultrasound-induced dissocia tion of soluble protein aggregates (Khatkar et al., 2018)”
From Effects of ultrasonication on structure and gelation of plant proteins at different denaturation states (2027) · cites this paper as Khatkar et al., 2018
Proteins with different thermal states are expected to respond differently to ultrasound, resulting in distinct structural and functional properties.
“proteins with different thermal states are expected to respond differently to ultrasound, resulting in distinct structural and functional properties”
From Effects of ultrasonication on structure and gelation of plant proteins at different denaturation states (2027) · cites this paper as Khatkar et al., 2018
Cites
Bryant, C. M., & McClements, D. J. (1998) · Trends in Food Science & Technology · doi:10.1016/s0924-2244(98)00031-4 · Cited by 643 · see citing works
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Zhang, L., Wang, X., Hu, Y., Abiola Fakayode, O., Ma, H., Zhou, C., Hu, Z., Xia, A., & Li, Q. (2021) · Ultrasonics Sonochemistry · doi:10.1016/j.ultsonch.2021.105803 · Cited by 53 · see citing works
Zhu, M., Kasapis, S., & Dhital, S. (2027) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.113251
- Authors
- Khatkar, A. B., Kaur, A., Khatkar, S. K., & Mehta, N.
- ORCID
- Mehta, Nitin
- Venue
- Ultrasonics Sonochemistry
- Publisher
- Elsevier BV
- Published
- 2018-12
- Volume
- 49
- Pages
- 333-342
- ISSN
- 1350-4177
- Cited by
- 145
- References
- 1
- Language
- en
- Funders
- Punjab Agricultural University
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