2022
DOI: 10.1016/j.ultsonch.2022.105993
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Recent advances in modified food proteins by high intensity ultrasound for enhancing functionality: Potential mechanisms, combination with other methods, equipment innovations and future directions

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Cited by 42 publications
(68 citation statements)
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“…Subsequently, with the increase of ultrasonic power, the gel strength tended to decrease. UT mainly affects the gel network formed between protein molecules by promoting protein folding and unfolding, within a certain ultrasonic power range, the formation of ultrasound induced disulfide bonds may contribute to the formation of protein-protein aggregation, resulting in a gel network with better gel strength ( Chen et al, 2022 ). However, the decrease of gel strength indicates that excessive ultrasound power may cause damage to the gel network, which is attributed to the protein damage caused by high intensity ultrasound shock wave and strong mechanical vibration, resulting in the formation of weak gel network.…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…Subsequently, with the increase of ultrasonic power, the gel strength tended to decrease. UT mainly affects the gel network formed between protein molecules by promoting protein folding and unfolding, within a certain ultrasonic power range, the formation of ultrasound induced disulfide bonds may contribute to the formation of protein-protein aggregation, resulting in a gel network with better gel strength ( Chen et al, 2022 ). However, the decrease of gel strength indicates that excessive ultrasound power may cause damage to the gel network, which is attributed to the protein damage caused by high intensity ultrasound shock wave and strong mechanical vibration, resulting in the formation of weak gel network.…”
Section: Resultsmentioning
confidence: 99%
“… Valdez-Hurtado et al (2019) found that ultrasound also greatly improved the gel properties of squid. In addition, it has been reported that ultrasound can increase the contact point and contact probability between enzyme and protein, and further promote the role of enzyme ( Chen et al, 2022 ). Hu et al (2015) successfully increased the degree of enzymatic cross-linking TGase cross-linked SPI with high intensity ultrasound (20 kHz, 400 W).…”
Section: Introductionmentioning
confidence: 99%
“…The dried S. rugosoannulata mushrooms were crushed by a pulverizer (80 mesh), and a liquid concentrate of S. rugosoannulata mushroom was prepared at 50 g/L for ultrasonic treatment to obtain the mushroom peptide matrix. The probe ultrasound and bath ultrasound were developed by the Institute of Food Physical Processing of Jiangsu University, and the equipment used was the same as that reported by Chen [20] . Ultrasonic treatment was administered at 300 W/L ultrasonic power density, 20/28 kHz synchronous dual frequency, for 20 min.…”
Section: Methodsmentioning
confidence: 99%
“…Ultrasound technology plays an important role in the preparation and increase in activity of peptides [15] , [16] , [17] . Ultrasound technology accelerates protein hydrolysis by inducing protein structure expansion and exposing protein cleavage sites, which provides a new method for deeply developing protein resources and assists in the preparation of bioactive peptides [18] , [19] , [20] .…”
Section: Introductionmentioning
confidence: 99%
“…Dual and triple frequency ultrasound have two and three ultrasonic waves with different frequency respectively. Superposition of waves can generate homogeneous ultrasound field with higher cavitational effect and waveform with wider range to avoid the formation of standing waves [ 18 ] when compared with mono frequency ultrasound. It can intensify the mass transfer and result in more sensitive protein structure to the enzymes.…”
Section: Introductionmentioning
confidence: 99%