Abstract
ABSTRACTThe effect of a salt substitute (SS) containing L-lysine (Lys) and L-histidine (His) on secondary structure and gel properties of myosin from grass carp was examined. The results indicated that the α-helix content of myosin treated with SS was 29.00%, 29.03% and 35.93% more than that with NaCl at 0.4, 0.6 and 0.8 mol/L (P < 0.05), respectively, suggesting that some fractions of the β-sheet, β-turn and random coil were transformed into α-helix. A similar pattern of storage modulus (G’) was found between NaCl and SS treatments, and the G’ of SS treatments at the end of gelation completion was higher than that of NaCl treatments. The salt substitute improved the gel strength and hardness of myosin at 0.4, 0.6 and 0.8 mol/L. The results indicated that the changes in secondary structure and gel properties of myosin may be mainly due to the L-lys and/or L-his in salt substitute.
Highlights
As a principal component of myofibrillar proteins, myosin was an asymmetrical protein with two globular heads attached to long α-helical rod-like tail (Privalov, 1982)
In the course of developing a novel salt substitute, it was found that L-histidine and L-lysine had a significant effect on the saltiness of cuttlefish bone extract (Zhang et al, 2014)
The combined action of L-histidine and L-lysine in salt substitute caused a transformation of β-sheet, β-turn and random coil to α-helix
Summary
As a principal component of myofibrillar proteins, myosin was an asymmetrical protein with two globular heads attached to long α-helical rod-like tail (Privalov, 1982). Divalent metal ions such as calcium and magnesium have been shown to alter the structure and functionality of the protein (Nayak, Kenney, Slider, Head, & Killefer, 1998a, 1998b). These cations were used as components of a salt substitute (Aliño, Grau, Fuentes, & Barat, 2010; Gou, Guerrero, Gelabert, & Arnau, 1996; Guàrdia, Guerrero, Gelabert, Gou, & Arnau, 2008). The cuttlefish bone extract was found to contain high levels of L-lysine and L-histidine and proved to have 27% less sodium content than that in NaCl at the same degree of saltiness. There is little research about the influence of a salt substitute containing L-histidine and L-lysine on structural properties and gel properties of warm-
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