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• W2092279877 abstract "The effect of CaCl2 on aggregation and conformational changes of tropical tilapia (Oreochromis niloticus) actomyosin incubated at 4 and 40 °C was investigated. Aggregation of tilapia actomyosin incubated at 40 °C for 30 min increased with addition of 10–100 mM CaCl2. Formation of higher molecular weight protein (HMP) at 40 °C was enhanced by addition of >10 mM Ca2+ ion, but suppressed by 2 mM N-ethylmaleimide (NEM) and 1 mM phenylmethnesulfonyl fluoride (PMSF), suggesting the involvement of endogenous transglutaminase (TGase). Moreover, addition of 10–100 mM CaCl2 destabilized actomyosin as evident by an increase in aniline naphthalenesulfonate surface hydrophobicity (S0-ANS) and loss of α-helical structure at 40 °C. However, CaCl2 only increased S0-ANS of actomyosin incubated at 4 °C without disturbing its secondary structure. Both ε-(γ-glutamyl)lysine isopeptide bonds and hydrophobic interactions appeared to be involved in HMP aggregates formed at 40 °C. Breaking force and deformation of actomyosin gels incubated at 40 °C for 30 min increased with added CaCl2 level and reached the maximum at 100 mM CaCl2, corresponding to an increased intensity of HMP observed on 5% SDS-PAGE. Ca2+ improved gelation during setting at 40 °C by not only activating endogenous TGase but also promoting hydrophobic interactions among unfolded actomyosin. Setting was also induced to a lesser extent at 4 °C in the presence of >10 mM CaCl2." @default.
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• W2092279877 date "2007-05-01" @default.
• W2092279877 modified "2023-10-14" @default.
• W2092279877 title "Aggregation and conformational changes of tilapia actomyosin as affected by calcium ion during setting" @default.
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• W2092279877 doi "https://doi.org/10.1016/j.foodhyd.2006.04.006" @default.
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