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dc.contributor.authorCareche, Mercedes-
dc.contributor.authorAlvarez, Cristina-
dc.contributor.authorTejada Yábar, Margarita-
dc.identifierdoi: 10.1021 / jf00052a030-
dc.identifierissn: 0021-8561-
dc.identifier.citationJournal of Agricultural and Food Chemistry 43: 1002- 1010 (1995)-
dc.description.abstractSuwari (set) and kamaboko (set and cooked) gels made with sardine surimi were prepared at normal heat-setting (35 or 40°C) and modori (60°C) temperatures and treated with solutions breaking ionic bonds, hydrogen bonds, hydrophobic interactions, and disulfide bridges. The lower gel strength of the gels obtained at modori temperature corresponded to a higher solubility of these gels in solutions breaking hydrophobic interactions and disulfide bridges. For suwari gels set at 35 and 40°C more protein was solubilized when electrostatic interactions and hydrogen bonds were ruptured. SDS-PAGE showed a higher amount of actin in these two fractions. No myosin heavy chain (MHC) bands were observed in any of the fractions obtained from suwari gels heat-set at 35 and 40°C. However, MHC bands were visible when disulfide bridges were disrupted in gels set at 60°C and in kamaboko gels set at 35°C. This means that the structure of the set gels was altered at cooking temperatures when the kamaboko network was formed. © 1995 American Chemical Society.-
dc.publisherAmerican Chemical Society-
dc.titleSuwari and kamaboko sardine gels: Effect of heat treatment on solubility of networks-
dc.identifier.doi10.1021 / jf00052a030-
dc.description.versionPeer Reviewed-
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