Structural Changes in Rice Bran Protein upon Different Extrusion Temperatures: A Raman Spectroscopy Study
Raman spectroscopy is critically evaluated to establish the limits to which it may be used to detect changes in protein conformation upon extrusion. Rice bran protein (RBP) extruded with different temperatures (100, 120, 140, and 160°C, labeled as ERBP-) was considered. DSC showed that extrusion at...
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| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Wiley
2016-01-01
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| Series: | Journal of Chemistry |
| Online Access: | http://dx.doi.org/10.1155/2016/6898715 |
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| Summary: | Raman spectroscopy is critically evaluated to establish the limits to which it may be used to detect changes in protein conformation upon extrusion. Rice bran protein (RBP) extruded with different temperatures (100, 120, 140, and 160°C, labeled as ERBP-) was considered. DSC showed that extrusion at 100°C increased TD of RBP but decreased its ΔH, while, after extrusion treatment at 120°C, RBP completely denatured. A progressive increase in unordered structure and a general decrease in α-helix structure and β-sheet structure of extruded RBP were observed from Raman study. Meanwhile the content of unordered structure increased up to 140°C and then decreased at 160°C, while the trend of α-helix and β-sheet content was opposite, which was contributed to the composite effect of formation of some more protein aggregation and protein denaturation. Extrusion generally induced a significant decrease in Trp band near 760 cm−1 but an increase at 160°C. No significant difference was observed in Tyr doublet ratios between controlled RBP samples and extruded RBP below 160°C, whereas Tyr doublet ratios of extruded RBP decreased at 160°C. Intensity of the band assigned to CHn bending decreased progressively and then increased as extrusion temperature increased, indicating changes in microenvironment and polarity. |
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| ISSN: | 2090-9063 2090-9071 |