Table 3. Structural changes of myofibrillar protein gels with 1% gelatin by different salt concentration
Area amid I1) | 1,624 cm−1 | 1,650 cm−1 | 1,680 cm−1 |
Control (0.15 M) | 88.53±1.28b | 88.41±2.01b | 92.50±1.88ab |
Control (0.30 M) | 62.50±3.21d | 63.20±3.81d | 76.54±1.12c |
Control (0.45 M) | 56.21±3.04e | 57.52±0.18e | 72.70±1.62d |
Gelatin (0.15 M) | 77.49±2.13c | 78.76±1.72c | 86.37±3.98b |
Gelatin (0.30 M) | 60.03±2.11d | 60.53±0.66d | 75.04±1.52c |
Gelatin (0.45 M) | 56.04±1.82e | 57.30±1.10e | 71.71±1.41d |
Gelatin | 93.73±2.10a | 94.66±1.95a | 96.79±3.84a |
Amid I: quantitative analysis of secondary structures, 1,650 cm−1 (α-helix/ unordered structure), regions around 1,624 cm−1 & 1,680 cm−1 (β-sheets).
Means (n=3) having same superscripts in a same column are not different (p>0.05).