2012
DOI: 10.1007/s00217-012-1750-7
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Rheological behavior of heat-induced actomyosin gels from yellowcheek carp and grass carp

Abstract: Dynamic rheological behavior of actomyosin from yellowcheek carp (YAM) and grass carp (GAM) during gelling was investigated at different protein concentrations. The viscoelastic properties of YAM and GAM solutions and gels were also studied. Before heating, YAM and GAM solutions exhibited the weak gel-like behavior. After heating and cooling, G 0 of YAM was much higher than the corresponding value of GAM. During heating and cooling, the G 0 values of actomyosin showed a strong relationship with protein concent… Show more

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Cited by 23 publications
(9 citation statements)
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“…During gelation, changes in the G′ value indicated the transformation into an elastic gel network and reflected the changes in stiffness or rigidity of the protein gel (Ding et al 2012). A high G′ usually indicates that the product is more rigid (Xiong and Blanchard 1994).…”
Section: Dynamic Rheological Measurementsmentioning
confidence: 99%
“…During gelation, changes in the G′ value indicated the transformation into an elastic gel network and reflected the changes in stiffness or rigidity of the protein gel (Ding et al 2012). A high G′ usually indicates that the product is more rigid (Xiong and Blanchard 1994).…”
Section: Dynamic Rheological Measurementsmentioning
confidence: 99%
“…Grass carp is one of the most important freshwater fish species in the world [ 30 ]. Nowadays grass carp is mainly dependent on aquaculture [ 31 ]. The threonine requirement of juvenile grass carp was estimated to 13.7 g/kg diet, corresponding to 36.0 g/kg of dietary protein [ 10 ].…”
Section: Introductionmentioning
confidence: 99%
“…Then a significant increase of surface hydrophobicity occurred for both normal and PSE-like actomyosin as temperature rose from 40°C to 60°C (p<0.05). This result indicated the changes in conformation of actomyosin including exposing hydrophobic aromatic amino acid residues to protein surface, which induced the formation of hydrophobic interaction to participate in the gelation process [43,44]. There was no significant difference between the surface hydrophobicity of normal and PSE-like actomyosin at 50°C and 60°C (p>0.05), suggesting PSE-like actomyosin exhibited a rapid unfolding rate and exposed the buried hydrophobic aromatic amino acid residues to its surface during heating from 20°C to 60°C [45].…”
Section: Resultsmentioning
confidence: 99%