2018
DOI: 10.1016/j.foodhyd.2018.06.044
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Manipulating interfacial behavior and emulsifying properties of myosin through alkali-heat treatment

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Cited by 47 publications
(9 citation statements)
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“…Due to its intrinsic hydrophobic character, the myosin tail has been regarded as the dominant unit for interfacial adsorption in emulsion systems [9] . However, because of its unique periodic charge distribution, it tends to assemble into filaments through intermolecular electrostatic interactions, hindering its development at the oil–water interface [46] . The fact that the α-helical content decreased following HIU treatment highlights the HIU-induced disintegration of the helical structures, disrupting the electrostatic balance between rods, concomitantly suppressing the assembly of filamentous myosin polymers.…”
Section: Resultsmentioning
confidence: 99%
“…Due to its intrinsic hydrophobic character, the myosin tail has been regarded as the dominant unit for interfacial adsorption in emulsion systems [9] . However, because of its unique periodic charge distribution, it tends to assemble into filaments through intermolecular electrostatic interactions, hindering its development at the oil–water interface [46] . The fact that the α-helical content decreased following HIU treatment highlights the HIU-induced disintegration of the helical structures, disrupting the electrostatic balance between rods, concomitantly suppressing the assembly of filamentous myosin polymers.…”
Section: Resultsmentioning
confidence: 99%
“…The dynamic interfacial tension was monitored at 25 °C using a drop profile tensiometer (Teclis Tracker, France) as reported (Li et al ., 2018b). Solutions of the MPs were diluted to 0.02 mg/mL, and loaded into a test cell, whereas the purified soy oil‐water interface was determined using a U‐shaped needle.…”
Section: Methodsmentioning
confidence: 99%
“…Compared with the raw emulsion, the CL protein emulsions with different ISP treatments showed different and good droplet distributions, which were related to the adsorption ability of the CL protein at the oil–water interface. This might be because different ISP treatments boosted stronger intramolecular electrostatic repulsions, which resulted in more extensive unfolding and a higher protein hydrophobicity [ 31 ], and protein hydrophobic groups can adsorb strongly to the oil–water interface to improve the emulsifying properties of the ISP CL protein. Meanwhile, disorganized the protein adsorption of a relatively smaller particle size might result in steric hindrance to stabilize the emulsion [ 9 ].…”
Section: Resultsmentioning
confidence: 99%