2008
DOI: 10.1016/j.foodchem.2007.05.067
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Protein and water structural changes in fish surimi during gelation as revealed by isotopic H/D exchange and Raman spectroscopy

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Cited by 126 publications
(73 citation statements)
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“…As the fish protein and water H‐bound, ionic bond and hydrophobic interaction in the gel, creating crosslinking gaps, so the moisture will be locked in certain areas, improving the water retention of the gel system. The entire network structure is thus more closely knit, thereby, improving the gel characteristics (Sánchez‐González et al., 2008). High‐temperature treatments may undermine the gel properties and change the three‐dimensional network structure, thus decreasing the gel's WHC.…”
Section: Resultsmentioning
confidence: 99%
“…As the fish protein and water H‐bound, ionic bond and hydrophobic interaction in the gel, creating crosslinking gaps, so the moisture will be locked in certain areas, improving the water retention of the gel system. The entire network structure is thus more closely knit, thereby, improving the gel characteristics (Sánchez‐González et al., 2008). High‐temperature treatments may undermine the gel properties and change the three‐dimensional network structure, thus decreasing the gel's WHC.…”
Section: Resultsmentioning
confidence: 99%
“…Both IR and NIR spectroscopy have been applied to study untreated wood (Altaner et al 2006;Chow 1972;Fackler and Schwanninger 2011;Fernandes et al 2011;Suchy et al 2010a, b;Taniguchi et al 1966;Tsuchikawa and Siesler 2003a, b), while no published data on modified wood are available. Similarly, no known study uses Raman spectroscopy to probe the wood-water interactions by deuteration, whereas a few have been published on deuteration of proteins (Bolton and Scherer 1989;Sánchez-González et al 2008) and lactose (Whiteside et al 2008). Even more information about hydroxyls can be gained from 2D correlation infrared spectroscopy (Noda 1990(Noda , 2006Noda et al 1993).…”
Section: Vibrational Spectroscopymentioning
confidence: 99%
“…It has been used to study the structure of isolated meat proteins such as myosin (Carew, Asher, & Stanley, 1975;Barret, Peticolas, & Robson, 1978). Structural studies of thermal gelation of meat and fish products have also been performed using this technique (Bouraoui, Nakai, & Li-Chan, 1997;Sánchez-González et al, 2008;Herrero, Carmona, López-López, & Jiménez-Colmenero, 2008b). Recently, Raman spectroscopic studies have also been conducted to examine the structural changes that occur in meat proteins upon addition of cold-set binding agents to meat systems (Herrero, Cambero, Ordóñez, de la Hoz, & Carmona, 2008a).…”
Section: Introductionmentioning
confidence: 99%