2018
DOI: 10.1016/j.ijbiomac.2017.12.167
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Application of ultrasound treatment for improving the physicochemical, functional and rheological properties of myofibrillar proteins

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Cited by 288 publications
(180 citation statements)
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“…When HIU (100 and 300 W) is applied directly to beef myofibrillar proteins for 10, 20, and 30 min, the pH of the protein extract also increases from the first 10 min of sonication. In the case of myofibrillar proteins, the pH increment has recently been attributed to a denaturation of proteins and the production of free radicals that interact with protein side chains, resulting in a decrease of protein acidic groups (Amiri, Sharifian, & Soltanizadeh, ).…”
Section: Resultsmentioning
confidence: 99%
“…When HIU (100 and 300 W) is applied directly to beef myofibrillar proteins for 10, 20, and 30 min, the pH of the protein extract also increases from the first 10 min of sonication. In the case of myofibrillar proteins, the pH increment has recently been attributed to a denaturation of proteins and the production of free radicals that interact with protein side chains, resulting in a decrease of protein acidic groups (Amiri, Sharifian, & Soltanizadeh, ).…”
Section: Resultsmentioning
confidence: 99%
“…The formation of foam is related to the surface hydrophobicity and structural flexibility of the proteins (Amiri et al , ). Figure c demonstrates that ultrasound treatment significantly increased the FC and FS of the treated BBPI compared to the native BBPI, and this result might be related to the exposure of hydrophobic regions and a reduction of interfacial tension via unfolding of the BBPI molecules, which would be consistent with the FT‐IR data (Fig.…”
Section: Resultsmentioning
confidence: 99%
“…The G' of the native and treated BBPI gels decreased during the initial heating process, indicating the gel networks might not have been completely formed. During the later heating process, the G' of treated BBPI gels sharply increased, and this was probably due to the ultrasound treatment inducing opening of the protein chain and, subsequently, improving the formation of junction zones via hydrogen bonding (Amiri et al , ). During the holding period (90 °C, 20 min), a significant increase in the strength of the gels was observed, and the network transformed from a viscous sol to elastic gel.…”
Section: Resultsmentioning
confidence: 99%
“…Ultrasonication is a novel method used to accelerate the thawing of frozen food . Ultrasonication uses wave energy at a frequency (20 kHz) higher than the human hearing threshold and can be classified into two frequencies: high‐frequency, low‐intensity (100 kHz to 1 MHz, power < 1 W cm −2 ); and low‐frequency, high‐intensity (20–100 kHz, 10 < power < 100 W cm −2 ) …”
Section: Introductionmentioning
confidence: 99%