Chemical Interactions and Protein Conformation Changes During Silver Carp (Hypophthalmichthys Molitrix) Surimi Gel Formation

Figures & data

Figure 1  PAGE of extracted native myosin.

Table 1  Effect of setting time on surimi gel properties

Heating time (min)		Surimi gel properties
40°C	90°C	Breaking force (g)	Deformation (mm)	Gel strength (g × mm)
30	30	364.33 ± 47.00	10.73 ± 0.88	3936.02 ± 745.97
60	30	470.50 ± 33.87	11.32 ± 0.40	5331.53 ± 522.78
90	30	468.00 ± 38.16	11.24 ± 0.71	5275.46 ± 670.39
120	30	441.00 ± 38.88	11.15 ± 0.87	4937.40 ± 745.24

Figure 2  Variations of chemical interactions during the formation of suwari gels and surimi gels. In horizontal axis, the numbers 1, 2, 3, 4, 5, 6, 7, 8, and 9 represent surimi, suwari gel setting at 40°C for 30 min, suwari gel setting at 40°C for 60 min, suwari gel setting at 40°C for 90 min, suwari gel setting at 40°C for 120 min, surimi gel setting at 40°C for 30 min, surimi gel setting at 40°C for 60 min, surimi gel setting at 40°C for 90 min, and surimi gel setting at 40°C for 120 min, respectively.

Figure 3  Laser Raman spectroscopy. A: surimi; B: suwari gel setting for 60 min at 40°C; C: surimi gel setting for 60 min at 40°C and cooking for 30 min at 90°C.

Table 2 Percent of secondary structure units of myosin

	Percent of secondary structure units of myosin (%)
Treating methods^a	α-Helix	β-Sheet	β-Turn	Random coil
1	94.11	0.00	0.00	5.89
2	27.00	0.00	10.40	62.60
3	33.70	0.00	12.40	53.90

^a1: native myosin (pH 7.5); 2: myosin heating for 60 min at 40°C; 3:myosin heating for 60 min at 40°C, then heating for 30 min at 90°C.

Figure 4  CD spectra of myosin during heating. The numbers 1, 2, and 3 represent native myosin (pH 7.5), myosin heating for 60 min at 40°C, myosin heating for 60 min at 40°C, and then heating for 30 min at 90°C, respectively.