2022
DOI: 10.1016/j.lwt.2022.114190
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Effects of lysine and arginine addition combined with high-pressure microfluidization treatment on the structure, solubility, and stability of pork myofibrillar proteins

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Cited by 17 publications
(8 citation statements)
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“…Additionally, pressure unfolds and alters the tertiary and quaternary structure of protein during microfluidization which facilitates its adsorption over oil droplets. 13 The partial unfolding and conformational changes of protein caused by microfluidization facilitated the exposure of hydrophobic residues. This could favor the binding ability of protein to the surface of oil droplets.…”
Section: Resultsmentioning
confidence: 99%
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“…Additionally, pressure unfolds and alters the tertiary and quaternary structure of protein during microfluidization which facilitates its adsorption over oil droplets. 13 The partial unfolding and conformational changes of protein caused by microfluidization facilitated the exposure of hydrophobic residues. This could favor the binding ability of protein to the surface of oil droplets.…”
Section: Resultsmentioning
confidence: 99%
“…As a fluid passes through an interaction chamber, the microfluidizer generates strong shear and impact forces that induce the creation of tiny droplet emulsion. 13 On the other hand, ultrasonication creates sound waves that dissipate through liquid media, resulting in cavitation effect and its efficacy depends on the frequency used. The pressure cycle causes small voids in the liquid which eventually collapse during the high-pressure cycle, resulting in high localized turbulence, shear forces, pressures, and temperatures.…”
Section: Introductionmentioning
confidence: 99%
“…As the duration of storage increased from 0 to 60 days, the carbonyl content of traditional bacon protein increased from 2.44 to 5.66 nmol mg À1 and that of alternative salt bacon protein increased from 3.02 to 5.73 nmol mg À1 . During storage, reactive oxygen species (ROSs) can directly attack the side chain groups of amino acids (especially the side chains of lysine, arginine and proline) to form carbonyl groups (Dom ınguez et al, 2022;Zhang et al, 2022aZhang et al, , 2022b. The effect of ROS was less as the bacon was vacuum packaged during storage (Amaral et al, 2018).…”
Section: Carbonyl Contentmentioning
confidence: 99%
“…The circular dichroism of the salt-soluble protein was determined following the method described by Zhang et al (2022aZhang et al ( , 2022b. The secondary structure of the salt-soluble protein was determined at 200-260 nm by a circular dichroism spectrometer (Chirascan V100; Applied Photophysics Ltd., UK).…”
Section: Circular Dichroismmentioning
confidence: 99%
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