2021
DOI: 10.1016/j.lwt.2020.110786
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Robustness of protein: Using pH shifting and low speed shearing to partially recover conformation and dispersibility of myosin from pale, soft, exudative (PSE)-like chicken breast

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Cited by 10 publications
(8 citation statements)
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“…There are many physical and chemical methods that can be applied to improve the functional properties of WBMP and subsequently enhance the texture and water-holding capacity (WHC) of the resulting WBMP gel. These strategies include high-intensity ultrasound (HIU) [10] , pulsed electric fields [11] , pH shifting and low-speed shearing [12] , glycosylation [13] , and isoelectric solubilization/precipitation [14] . Among these, HIU is convenient for use in actual production.…”
Section: Introductionmentioning
confidence: 99%
“…There are many physical and chemical methods that can be applied to improve the functional properties of WBMP and subsequently enhance the texture and water-holding capacity (WHC) of the resulting WBMP gel. These strategies include high-intensity ultrasound (HIU) [10] , pulsed electric fields [11] , pH shifting and low-speed shearing [12] , glycosylation [13] , and isoelectric solubilization/precipitation [14] . Among these, HIU is convenient for use in actual production.…”
Section: Introductionmentioning
confidence: 99%
“…The isoelectric point (p I ) of myosin is 5.4. When the pH is close to p I , myosin tends to assemble and its solubility becomes low (Yang et al., 2021). Myosin aggregation, which made group B gelation more effective.…”
Section: Resultsmentioning
confidence: 99%
“…Turbidity is usually determined to indicate the aggregation degree of myosin molecules [ 31 ]. As shown in Figure 1 B, as the NaCl concentration increased, the turbidity of myosin treated solely by NaCl (control) significantly decreased ( p < 0.05), suggesting a reduction in the aggregation degree of myosin.…”
Section: Resultsmentioning
confidence: 99%