Surimi and Surimi Seafood 2013
DOI: 10.1201/b16009-6
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Historical Review of Surimi Technology and Market Developments

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Cited by 74 publications
(111 citation statements)
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“…In this state, hydrophobic interactions and disulfide bonds are involved (Savadkoohi et al 2013) as the polypeptide chains unfold its helical structure and expose its inner surface to the surrounding aqueous environment in order to reduce the randomness and increase the stability of the system. At relatively higher temperature (>50°C), the extent of protein unfolding increases which in turn enhances such interactions, corresponding to a 3D elastic gel network (Lanier et al 2005).…”
Section: Storage Modulusmentioning
confidence: 99%
“…In this state, hydrophobic interactions and disulfide bonds are involved (Savadkoohi et al 2013) as the polypeptide chains unfold its helical structure and expose its inner surface to the surrounding aqueous environment in order to reduce the randomness and increase the stability of the system. At relatively higher temperature (>50°C), the extent of protein unfolding increases which in turn enhances such interactions, corresponding to a 3D elastic gel network (Lanier et al 2005).…”
Section: Storage Modulusmentioning
confidence: 99%
“…This fact is probably a consequence of the greater interaction among proteins-water-ingredients. In addition, in proteins of cold water species, such as hake, pre-gelation occurs at low temperatures after salt-induced solubilisation due to the endogenous transglutaminase activity present in the muscle (LANIER;CARVAJAL;YONGSAWATDIGUL, 2005). After the setting process, the water is bound in a protein-protein net that constitutes the gel.…”
Section: Colour Measurementmentioning
confidence: 99%
“…And during cooling, the gradual increase suggested that slow continued hydrogen bonds occurred, which was important in stabilization of bound water and increasing gel strength by their great numbers (Lanier et al, 2013;Sun & Arntfield, 2011).…”
Section: Rheological Properties Of Myofibril Solutions During Heatingmentioning
confidence: 99%
“…The heat-induced gelation was associated with the formation of sufficient intermolecular protein bonds such as hydrogen bonds, ionic linkages, hydrophobic interactions and covalent bonds (Lanier, Yongsawatdigul, & CarvajalRondanelli, 2013). The formation of heat-induced gels is a complex thermodynamic process that is related to the muscle sources and types and different cooking conditions such as temperature, pH, protein concentrations and ionic strength (Lanier et al, 2013) and most of the researches focused on the study of myosin heat-induced gelation.…”
Section: Introductionmentioning
confidence: 99%
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