2018
DOI: 10.1002/jsfa.9073
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Aggregation and conformational changes of silver carp myosin as affected by the ultrasound–calcium combination system

Abstract: The combination system reported in the present study was beneficial for myosin unfolding, facilitating intermolecular interactions between Ca and myosin. Ultrasound treatment promoted myosin aggregation via the induction of Ca and reduced the critical concentration of Ca required to aggregate myosin. In the fish processing industry, this combination system can enhance the gelation properties of surimi-based products. © 2018 Society of Chemical Industry.

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Cited by 13 publications
(5 citation statements)
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“…Appropriate ultrasound increased H 0 , which reached the maximum value at 360 W/20 min ultrasound pretreatment, and H 0 was 1.61 times higher than that of the control group ( P < 0.05). An et al [40] study also showed that the H 0 of silver carp myosin increased considerably after ultrasonic treatment, indicating that the conformation of silver carp myosin changed further. The α-helix structure unfolds under the high pressure and shear force produced by ultrasound, the protein conformation changes, and the myosin aggregates break, which will expose more hydrophobic groups [37] .…”
Section: Resultsmentioning
confidence: 90%
“…Appropriate ultrasound increased H 0 , which reached the maximum value at 360 W/20 min ultrasound pretreatment, and H 0 was 1.61 times higher than that of the control group ( P < 0.05). An et al [40] study also showed that the H 0 of silver carp myosin increased considerably after ultrasonic treatment, indicating that the conformation of silver carp myosin changed further. The α-helix structure unfolds under the high pressure and shear force produced by ultrasound, the protein conformation changes, and the myosin aggregates break, which will expose more hydrophobic groups [37] .…”
Section: Resultsmentioning
confidence: 90%
“…The difference in turbidity for combination-treated myosin might derive from the difference in the existence form of myosin with different NaCl concentrations. According to Liu et al [ 17 ], the decreased turbidity might be associated with the reduced particle size. HIU was expected to disrupt the myosin assemblies in the low-salt environment (0.1 mol/L NaCl) [ 22 ], while HIU was able to disrupt the myosin aggregates due to shear force at ≥ 0.3 mol/L NaCl; as a result, the particles scattered light weakly.…”
Section: Resultsmentioning
confidence: 99%
“…Preparation of combination-treated (HIU and NaCl) samples was performed as described by Liu et al [ 17 ]. Briefly, 25 mL of myosin solution with different NaCl concentrations (0.1, 0.3, 0.5 mol/L) was placed in a 50 mL centrifuge tube, followed by subjecting to HIU treatment using an ultrasound processor (Ningbo Scientz Biotechnology Co., Ltd., Ningbo, China) equipped with a spherical probe (0.6 cm of diameter).…”
Section: Methodsmentioning
confidence: 99%
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“…The properties of myofibrillar proteins, especially myosin, play a crucial part in all technological processes involving heat treatments (Zhou et al, 2014;Zhou et al, 2018). Previous studies have focused on the thermal gelation in pork, chicken and rabbit (An et al, 2018;Brewer et al, 2005;Chin et al, 2009;Xue et al, 2018). The properties of myosin gels have been widely studied with regard to different parts of the animal, animal breeds and ionic strengths (Hollung et al, 2014;Xue et al, 2018), but the age has been minimally researched.…”
Section: Introductionmentioning
confidence: 99%