2022
DOI: 10.1016/j.lwt.2022.113767
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Study on the mechanism of protein hydrolysate delaying quality deterioration of frozen surimi

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Cited by 22 publications
(8 citation statements)
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“…As shown in Figure 2 , the carbonyl content of surimi MP increased in all groups as the frozen storage time extended, which was consistent with the results of Zhang et al ( 31 ). This suggested that frozen storage enhanced the degree of protein oxidation and increased the protein carbonyl content, which may be related to the release of oxidase and prooxidants from ruptured organelles ( 32 ).…”
Section: Resultssupporting
confidence: 91%
“…As shown in Figure 2 , the carbonyl content of surimi MP increased in all groups as the frozen storage time extended, which was consistent with the results of Zhang et al ( 31 ). This suggested that frozen storage enhanced the degree of protein oxidation and increased the protein carbonyl content, which may be related to the release of oxidase and prooxidants from ruptured organelles ( 32 ).…”
Section: Resultssupporting
confidence: 91%
“…The protein conformational changes could reflect the changes in the gel structure from the microscopic perspective. Using Fourier transform infrared spectroscopy, the proportion of α‐helixes, β‐sheets, β‐turns, and random coils could be obtained through peak differentiation and the imitation of the amide I region (Zhang et al, 2022).…”
Section: Resultsmentioning
confidence: 99%
“…According to the “setting‐freezing‐reheating” procedure and the two‐step heating process of surimi, there are corresponding freezing strategies for the frozen storage of ready‐to‐eat surimi food products, namely, raw‐freezing‐setting‐heating, raw‐setting‐freezing‐heating, and raw‐setting‐heating‐freezing. Under these different freezing methods, the degree of mechanical damage and protein oxidation and degradation caused by ice crystal growth is different (Zhang et al, 2022). During the frozen storage process, the intrusion and mechanical damage of ice crystals to surimi tissues led to substantial thawing losses.…”
Section: Introductionmentioning
confidence: 99%
“…Protein patterns of the surimi were analyzed by SDS-PAGE according to the method of Zhang et al [ 22 ]. In brief, the surimi samples (3.0 g) were mixed with 5% SDS solution (30 mL), homogenized, and held at 85 °C for 1 h. After centrifugation (3500 r/min, 15 min) the supernatant was added to an equal volume of 1× loading buffer, dispersed and then boiled in a water bath for 3 min.…”
Section: Methodsmentioning
confidence: 99%