2017
DOI: 10.1016/j.lwt.2017.03.026
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Changes in physicochemical properties and protein structure of surimi enhanced with camellia tea oil

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Cited by 127 publications
(103 citation statements)
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“…The relevance of protein secondary structure and gel strength was in accordance with the previous study, in which it was found that the increase of gel strength in surimi was related to the increase of β‐sheet content (Guo et al, ). Moreover, Zhou et al () also reported that the hardness of surimi gels was negatively correlated to the α‐helix content and positively correlated to the β‐sheet content of surimi gels. The reason for this might be that β‐sheet structure has the comparatively larger surface area and the weaker water hydration strength than α‐helices, which is important for protein–protein interactions and gel network formation (Choi & Ma, ; Liu et al, ).…”
Section: Resultsmentioning
confidence: 97%
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“…The relevance of protein secondary structure and gel strength was in accordance with the previous study, in which it was found that the increase of gel strength in surimi was related to the increase of β‐sheet content (Guo et al, ). Moreover, Zhou et al () also reported that the hardness of surimi gels was negatively correlated to the α‐helix content and positively correlated to the β‐sheet content of surimi gels. The reason for this might be that β‐sheet structure has the comparatively larger surface area and the weaker water hydration strength than α‐helices, which is important for protein–protein interactions and gel network formation (Choi & Ma, ; Liu et al, ).…”
Section: Resultsmentioning
confidence: 97%
“…Furthermore, exposed hydrophobic groups aggregated with each other by hydrophobic interactions, which can significantly enhance the formation of three‐dimensional network structure of surimi gels (Liu et al, ). Ionic bonds, are usually formed between two amino acid residues with opposite charges through attractive Coulombic forces, play important roles in the stability of tertiary and quaternary structures in proteins (Zhou et al, ). The index of hydrophobic interactions and ionic bonds decreased when the starches were further added.…”
Section: Resultsmentioning
confidence: 99%
“…The isoelectric point (pI) of myofibrillar protein is approximately 5.5, and the pH of the final products was 7.02 ± 0.02. Therefore, ionic bonds are formed by attractive Coulombic forces between two amino acid residues with opposite charges, and this has a great effect on the stability of protein tertiary and quaternary structures . As can be seen from Fig.…”
Section: Resultsmentioning
confidence: 99%
“…Addition of curdlan, gelatin, or κ ‐carrageenan, at levels of 4 g kg −1 , 1 g kg −1 , or 2 g kg −1 respectively, was able to significantly increase the hydrophobic interaction and further promote the gel strength of surimi ( P < 0.05; Figs and ). Heating can induce protein denaturation and expose myosin hydrophobic groups, which is beneficial to the aggregation and cross‐linking between proteins . Furthermore, the aggregation of the hydrophobic groups of the linked proteins can significantly enhance the formation of the three‐dimensional network structure of surimi gels .…”
Section: Resultsmentioning
confidence: 99%
“…The fat content of squid meat is less than 2%, and the low fat content causes the squid surimi products with good springiness but poor juiciness and smooth feel. To improve the texture and sensory characteristics of squid surimi products, it is necessary to add fat in commercial meat product formulations (Youssef & Barbut, 2009;Zhou et al, 2017).…”
Section: Introductionmentioning
confidence: 99%