Structural Changes in Rice Bran Protein upon Different Extrusion Temperatures: A Raman Spectroscopy Study

Table 3

Percentages of protein secondary structure: α-helix, β-sheet, β-turn and unordered structure of rice bran protein (RBP) and extruded rice bran protein (ERBP) at different extrusion temperature.

Sample	Percentage of secondary structure elements (%)
	α-helix structure	β-sheet structure	β-turn structure	Unordered structure
RBP	17.43 ± 0.01	41.14 ± 0.04	19.67 ± 0.02	19.76 ± 0.01
ERBP-100	17.83 ± 0.02	38.00 ± 0.03	19.67 ± 0.04	23.50 ± 0.02
ERBP-120	17.08 ± 0.03	34.51 ± 0.02	19.33 ± 0.03	29.08 ± 0.01
ERBP-140	17.01 ± 0.02	31.83 ± 0.04	19.32 ± 0.00	31.83 ± 0.03
ERBP-160	18.31 ± 0.01	36.31 ± 0.02	19.59 ± 0.01	25.78 ± 0.03

RBP: rice bran protein; ERBP-100: extruded rice bran protein at 100°C temperature; ERBP-120: extruded rice bran protein at 120°C temperature; ERBP-140: extruded rice bran protein at 140°C temperature; ERBP-160: extruded rice bran protein at 160°C temperature.
Different superscript letters in the same column indicate significant differences ().
α-helix, β-sheet, β-turn, and unordered structure are secondary structure elements of protein.