The effect of ultrasound treatment on the structural, physical and emulsifying properties of dairy proteins

O’Sullivan, Jonathan; Arellano, M.; Pichot, R.; Norton, Ian T.

doi:10.1016/j.foodhyd.2014.05.011

Cited by 168 publications

(65 citation statements)

References 44 publications

(58 reference statements)

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“…It can be inferred that the aggregation of β‐lactoglobulin may be partially resulted from noncovalent interactions, such as electrostatic and hydrophobic interactions (Arzeni et al., ). Similar results had been obtained in the SDS‐PAGE studies of WPC, dairy proteins, and β‐lactoglobulin as reported previously (Chandrapala et al., ; O'Sullivan, Arellano, Pichot, & Norton, ).…”

Section: Resultssupporting

confidence: 90%

Ultrasound‐induced changes in structural and physicochemical properties of β‐lactoglobulin

Zhao

et al. 2018

Food Science & Nutrition

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Effect of ultrasound treatment on the physicochemical properties and structure of β‐lactoglobulin were investigated. β‐Lactoglobulin was treated with ultrasound at different amplitudes, temperatures, and durations. The surface hydrophobicity and free sulfhydryl group of β‐lactoglobulin were significantly increased after ultrasound treatment (p < .05). The maximal surface hydrophobicity and free sulfhydryl group were 5,812.08 and 5.97 μmol/g, respectively. Ultrasound treatment changed the physicochemical properties of β‐lactoglobulin including particle size (from 1.21 ± 0.05 nm to 1.66 ± 0.03 nm), absolute zeta potential (from 15.47 ± 1.60 mV to 27.63 ± 3.30 mV), and solubility (from 84.66% to 95.17%). Ultrasound treatment increased α‐helix and β‐sheet structures of β‐lactoglobulin. Intrinsic fluorescence intensity of ultrasound‐treated β‐lactoglobulin was increased with shift of λmax from 334 to 329 nm. UV absorption of β‐lactoglobulin was decreased with shift of λmax from 288 to 285 nm after ultrasound treatment. There were no significant changes in high‐performance liquid chromatography and protein electrophoretic patterns. These findings indicated that ultrasound treatment had high potential in modifying the physiochemical and structural properties of β‐lactoglobulin for industrial applications.

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Section: Resultssupporting

confidence: 90%

Ultrasound‐induced changes in structural and physicochemical properties of β‐lactoglobulin

Zhao

et al. 2018

Food Science & Nutrition

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“…O'Sullivan et al . () also observed an increase in size of egg white protein aggregation associated with thermal aggregation during US treatment.…”

Section: Resultsmentioning

confidence: 69%

Effect of High Intensity Ultrasound on the Gel and Structural Properties ofCtenopharyngodon idellusMyofibrillar Protein

Wen

Zhang

et al. 2016

Journal of Food Biochemistry

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Effect of ultrasound (US) treatment at 0–800 W on the gel properties of Ctenopharyngodon idellus myofibrillar protein (MP) was first evaluated by analyzing the textural properties, water‐holding capacity (WHC) and whiteness. Particle size, fluorescence spectra, free sulfhydryl (SH) groups and microstructure were measured to investigate the structure changes. The MP gel treated with US at 600 W gave the best gel properties, including the highest gel strength, hardness, gumminess, chewiness, WHC and whiteness. Compared with untreated gel, the gel network structure of MP gel treated by US was also more denser and uniform. The reduced particle size, narrowed particle distribution, decreased free SH content and intrinsic fluorescence, as well as improved surface hydrophobicity caused by US treatment indicated the unfolding and disaggragation of MP, which could also be the possible mechanism of improved gel properties. Practical Applications The gelation characteristics of myofibrillar protein (MP) are largely responsible for the textural and functional properties of fish products, and are especially important for the quality of surimi. The poor gel properties of Ctenopharyngodon idellus MP largely limited its application in food industry. This research found that high intensity US at 200–800 W, especially at 600 W, could greatly improve the gel properties of C. idellus MP, which can provide a promising alternative to modify the gel properties of MP, and promote the application of C. idellus MP in food industry.

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“…The dissociation and aggregation of protein subunits play an important role in the microstructure, with consequent changes of functional properties such as rheology, emulsification and gelation (Durand, Gimel, & Nicolai, 2002;Nicorescu et al, 2010;O'Sullivan, Arellano, Pichot, & Norton, 2014). Li, Wang, Hu, and Liao (2014) reported that more intense high pressure CO 2 treatment caused the dissociation of larger aggregates and further aggregation in the smaller aggregates, which resulted in the change of polyphenol oxidase activity of thaumatin-like protein.…”

Section: Introductionmentioning

confidence: 99%

Changes in the structure and dissociation of soybean protein isolate induced by ultrasound-assisted acid pretreatment

et al. 2017

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The effect of ultrasound treatment on the structural, physical and emulsifying properties of dairy proteins

Cited by 168 publications

References 44 publications

Ultrasound‐induced changes in structural and physicochemical properties of β‐lactoglobulin

Ultrasound‐induced changes in structural and physicochemical properties of β‐lactoglobulin

Effect of High Intensity Ultrasound on the Gel and Structural Properties ofCtenopharyngodon idellusMyofibrillar Protein

Changes in the structure and dissociation of soybean protein isolate induced by ultrasound-assisted acid pretreatment

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