Comparative assessment of the effect of ultrasound treatment on protein functionality pre- and post-emulsification

O’Sullivan, Jonathan; Beevers, Jack; Park, Michael; Greenwood, R.; Norton, Ian T.

doi:10.1016/j.colsurfa.2015.07.065

Cited by 60 publications

(32 citation statements)

References 31 publications

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“…The secondary structural changes of 7S and 11S fractions might have resulted from ultrasonic cavitation, which could reduce the size of protein aggregates, rearrange protein molecules at the interface, and increase the protein hydrophobicity (O'Sullivan, Beevers, Park, Greenwood, & Norton, 2015;O'Sullivan, Murray, Flynn, & Norton, 2016). A decrease in the b-sheet component showed that the protein hydrophobic interaction sites were exposed, the surface hydrophobicity of the protein was enhanced (Stathopulos et al, 2004).…”

Section: Resultsmentioning

confidence: 97%

“…This phenomenon might be attributed to the fact that the high ultrasonic power, temperature and time accelerated protein moleculars motion, increased the chance of protein moleculars collision, and rearranged protein molecules at the interface. The protein molecules which had exposed to the surface of the molecules, were buried inside the molecules (Jiang et al, 2014;O'Sullivan, Beevers, Park, Greenwood, & Norton, 2015).…”

Section: Resultsmentioning

confidence: 99%

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Effects of ultrasound pre-treatment on the structure of β-conglycinin and glycinin and the antioxidant activity of their hydrolysates

et al. 2017

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Section: Resultsmentioning

confidence: 97%

Section: Resultsmentioning

confidence: 99%

Effects of ultrasound pre-treatment on the structure of β-conglycinin and glycinin and the antioxidant activity of their hydrolysates

et al. 2017

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“…The acoustic power and acoustic intensity for each tip as a function of ultrasonic amplitude is additionally presented in Table 1, and was determined calorimetrically by measuring the temperature gain as a function of treatment time under adiabatic conditions. The acoustic intensity, I a (W cm -2 ), was calculated as follows [36,37]:…”

Section: Ultrasonic Processing Conditions and Vessel Configurationmentioning

confidence: 99%

Characterisation of flow behaviour and velocity induced by ultrasound using particle image velocimetry (PIV): Effect of fluid rheology, acoustic intensity and transducer tip size

O’Sullivan

Espinoza

Mihailova

et al. 2018

Ultrasonics Sonochemistry

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Acoustic streaming phenomena of ultrasound propagation through liquid media was investigated experimentally employing particle image velocimetry (PIV). Parameters associated with the ultrasonic processor of ultrasonic amplitude (i.e., acoustic power) and transducer tip diameter (i.e., surface area), as well as, fluid rheology (i.e., water, glycerol solution and CMC solution), were studied for their effects on overall flow behaviour and fluid velocity. PIV yielded velocity gradient maps, demonstrating the acoustic streaming phenomena of ultrasound and its associated flow behaviour as a function of ultrasonic amplitude and fluid rheology, whereby increasing amplitude allowed for greater penetration of the acoustic-beam through the bulk of the fluid, and increasing fluid rheology yielded the converse effect. Moreover, upon impingement of the acoustic-beam with the base of vessel, vortex formation occurred, yielding a recirculation pattern. The maximum observed fluid velocities for water, glycerol solution and CMC solution were 0.329 m s, 0.423 m s, and 0.304 m s, respectively (large diameter sonotrode tip for an ultrasonic amplitude of 80%). Furthermore, shear rates were attained (maximum values of 24.25 s), and Reynolds numbers were determined in order to assess the degree of turbulence as a function of investigated parameters.

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“…1), but showed higher emulsifying activity. This indicated that the small molecular WPI-SY complexes had greater mobility to adsorb around the oil-water interfaces (O'Sullivan et al, 2015). The average particle size in phosvitin-resveratrol system had an opposite trend with its emulsifying activity (Duan et al, 2016).…”

Section: Resultsmentioning

confidence: 99%

Effects of pH Values on Physicochemical Properties and Antioxidant Potential of Whey Protein Isolate-safflower Yellow Complexes

Gao²,

et al. 2018

FSTR

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Influence of pH values on physicochemical characteristics and antioxidant activities of whey protein isolate (WPI)-safflower yellow (SY) complexes were investigated at 25℃ under the aerobic condition for 0, 3 and 6 d. Compared with WPI, WPI-SY had a less particle size at pH 3.5, 6.5, 7.5 and 8.5 from 0 to 6 days. Fluorescence intensity of WPI-SY complexes was appreciably less than WPI, which indicated that the partial tyrosine or tryptophan residues of whey protein had undergone certain changes. Compared with WPI and SY, thermal stability and emulsifying activity of WPI-SY complexes remarkably increased at different pH values. Meanwhile, antioxidant activities of WPI-SY complexes were higher than that of WPI or SY at pH ranged 4.5 to 9.5, kept for 3 and 6 d. Therefore, the interaction of WPI and SY at different pH values, could improve emulsifying activity of WPI and enhance antioxidant activity of SY.

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Comparative assessment of the effect of ultrasound treatment on protein functionality pre- and post-emulsification

Cited by 60 publications

References 31 publications

Effects of ultrasound pre-treatment on the structure of β-conglycinin and glycinin and the antioxidant activity of their hydrolysates

Effects of ultrasound pre-treatment on the structure of β-conglycinin and glycinin and the antioxidant activity of their hydrolysates

Characterisation of flow behaviour and velocity induced by ultrasound using particle image velocimetry (PIV): Effect of fluid rheology, acoustic intensity and transducer tip size

Effects of pH Values on Physicochemical Properties and Antioxidant Potential of Whey Protein Isolate-safflower Yellow Complexes

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