Research Article
Structural Changes in Rice Bran Protein upon Different Extrusion Temperatures: A Raman Spectroscopy Study
Table 2
Tentative assignment of some bands in the Raman spectrum of rice bran protein (RBP).
| | Frequency (cm−1) | Assignment |
| | 514 | νS-S gauche-gauche-gauche conformation | | 530 | νS-S gauche-gauche-trans conformation | | 547 | νS-S trans-gauche-trans conformation | | 620–640 | Phenylalanine (Phe) | | 644 | Tyrosine (Tyr) | | 760 | Tryptophan (Trp) | | 830 | Tyr -ring | | 850 | Tyr -ring | | 940 | νC-C (-helix) | | 1003 | Phe -ring | | 1250 | Amide III bands (-sheet, random coil) | | 1273 | Amide III bands (-helix) | | 1309 | Amide III bands (-helix) | | 1321 | Trp -ring | | 1340 | CH | | 1360 | Trp -ring | | 1450 | CH3, CH2, CH | | 1645–1690 | Amide I bands |
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ν, stretching vibrations; δ, bending vibrations; vs, very strong.
Phe, phenylalanine; Tyr, tyrosine; Trp, tryptophan; α-helix, β-sheet, β-turn, and unordered structure are secondary structure elements of protein.
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