Table 2.
Secondary structure band assignments in the RuBisCO-rich protein fractions obtained via ultrasound-assisted extraction from pumpkin leaves.
| Secondary Structure | Band Assignment in the RuBisCO-Rich Protein Fraction (%) | ||||||
|---|---|---|---|---|---|---|---|
| Without Ultrasound * | UAE-20% | UAE-30% | UAE-40% | UAE-50% | UAE-60% | UAE-70% | |
| β-sheet (intermolecular) | 34.55 ± 1.09 a | 19.58 ± 1.12 b | 20.02 ± 1.00 b | 15.08 ± 2.04 c | 16.51 ± 1.55 c | 16.33 ± 1.25 c | 18.22 ± 1.30 b |
| β-sheet (extended) | 15.09 ± 1.06 c | 23.57 ± 1.15 a | 18.95 ± 0.95 b | 17.61 ± 1.24 b | 20.14 ± 1.80 ba | 22.19 ± 1.20 a | 23.28 ± 1.45 a |
| Random coil | n.d. | 13.60 ± 0.85 b | 10.48 ± 1.45 b | 20.39 ± 2.54 a | 11.16 ± 2.02 b | 5.21 ± 1.54 c | n.d. |
| α-helix | 36.71 ± 1.14 b | 12.29 ± 1.65 e | 18.59 ± 1.42 d | 20.44 ± 1.72 c | 25.32 ± 2.00 c | 37.67 ± 1.40 b | 57.24 ± 1.20 a |
| β-turn | 13.64 ± 1.24 d | 30.97 ± 1.42 a | 31.98 ± 2.01 a | 26.49 ± 2.00 b | 26.87 ± 1.72 b | 18.61 ± 2.64 c | 1.26 ± 0.25 e |
* Maceration process performed under the same reaction conditions, but without ultrasonication. n.d.—not determined. The data are presented as the mean ± SD (n = 3). Means with different letters for the same secondary structure of proteins (row) are significantly different (p < 0.05). Legend: UAE-20%, UAE-30%, UAE-40%, UAE-50%, UAE-60%, and UAE-70% mean ultrasound-assisted extraction process at 20, 30, 40, 50, 60, and 70% amplitudes, respectively.