2020
DOI: 10.1007/s11947-020-02416-x
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Myofibrillar Protein Structure and Gel Properties of Trichiurus Haumela Surimi Subjected to High Pressure or High Pressure Synergistic Heat

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Cited by 51 publications
(19 citation statements)
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“…Our results of secondary structure were in agreement with the results reported by Chen et al. (2020), who found that the secondary structure of the protein changed significantly with the extension of high‐pressure treatment time. Through the analysis of the amide I band, the secondary structure composition of collagen was quantified.…”
Section: Resultssupporting
confidence: 93%
See 1 more Smart Citation
“…Our results of secondary structure were in agreement with the results reported by Chen et al. (2020), who found that the secondary structure of the protein changed significantly with the extension of high‐pressure treatment time. Through the analysis of the amide I band, the secondary structure composition of collagen was quantified.…”
Section: Resultssupporting
confidence: 93%
“…The positions of amide I, II, and III of above two gelatinized collagens were relatively close, but the corresponding absorption peak of high-pressure treatment is not as sharp as that of the control, indicating that the collagen structural integrity of high-pressure group is poor. Our results of secondary structure were in agreement with the results reported by Chen et al (2020), who found that the secondary structure of the protein changed significantly with the extension of highpressure treatment time. Through the analysis of the amide I band, the secondary structure composition of collagen was quantified.…”
Section: Infrared Spectra Of Gelatinized Collagensupporting
confidence: 93%
“…Similarly, Debusca, Tahergorabi, Beamer, Matak, and Jaczynski (2014) reported that hardness and chewiness increased incrementally with the addition of dietary fiber. Chen et al (2020) found that α‐helix content of myofibrillar protein in the hairtail surimi was positively correlated with the gel strength. Our previous reports showed that the addition of laver powder could increase the content of α‐helix in surimi gels (Xu et al, 2020), this might explain why laver improved gel properties of surimi gels.…”
Section: Resultsmentioning
confidence: 99%
“…HHP could disrupt the intermolecular β-sheet structure in abalone proteins, which was compensated for by forming new intramolecular β-sheet interactions [28]. Chen et al found that the β-turn was reduced with the treatment of pressure [37]. In general, highly ordered structures (α-helix, β-sheet and β-turn) unfold under HHP, resulting in an increase in random coil structure [26].…”
Section: Secondary Structurementioning
confidence: 99%
“…At 500 atmospheres, myosin unfolds; at 1000 atmospheres, they cling together, while at pressures higher than 1500 atmospheres, myosin forms aggregates and gels [65]. Chen et al investigated the relationship between the gel properties of surimi and the structure of MP under high pressure (300~450MPa) [37]. The results showed that the secondary structure of MP in the surimi gels was significantly correlated with the whiteness, strength and structural characteristics of the gels.…”
Section: Effect Of Hhp On Myofibrillar Protein Gelmentioning
confidence: 99%