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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| Format: | Article |
| Language: | English |
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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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| author | Linyi Zhou Yong Yang Haibin Ren Yan Zhao Zhongjiang Wang Fei Wu Zhigang Xiao |
| author_facet | Linyi Zhou Yong Yang Haibin Ren Yan Zhao Zhongjiang Wang Fei Wu Zhigang Xiao |
| author_sort | Linyi Zhou |
| collection | DOAJ |
| description | 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. |
| format | Article |
| id | doaj-art-c7fc4ccb713242b8afa899e1af5f5ded |
| institution | Kabale University |
| issn | 2090-9063 2090-9071 |
| language | English |
| publishDate | 2016-01-01 |
| publisher | Wiley |
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| series | Journal of Chemistry |
| spelling | doaj-art-c7fc4ccb713242b8afa899e1af5f5ded2025-02-03T00:59:20ZengWileyJournal of Chemistry2090-90632090-90712016-01-01201610.1155/2016/68987156898715Structural Changes in Rice Bran Protein upon Different Extrusion Temperatures: A Raman Spectroscopy StudyLinyi Zhou0Yong Yang1Haibin Ren2Yan Zhao3Zhongjiang Wang4Fei Wu5Zhigang Xiao6College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, ChinaCollege of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, ChinaCollege of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, ChinaCollege of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, ChinaCollege of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, ChinaCollege of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, ChinaCollege of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, ChinaRaman 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.http://dx.doi.org/10.1155/2016/6898715 |
| spellingShingle | Linyi Zhou Yong Yang Haibin Ren Yan Zhao Zhongjiang Wang Fei Wu Zhigang Xiao Structural Changes in Rice Bran Protein upon Different Extrusion Temperatures: A Raman Spectroscopy Study Journal of Chemistry |
| title | Structural Changes in Rice Bran Protein upon Different Extrusion Temperatures: A Raman Spectroscopy Study |
| title_full | Structural Changes in Rice Bran Protein upon Different Extrusion Temperatures: A Raman Spectroscopy Study |
| title_fullStr | Structural Changes in Rice Bran Protein upon Different Extrusion Temperatures: A Raman Spectroscopy Study |
| title_full_unstemmed | Structural Changes in Rice Bran Protein upon Different Extrusion Temperatures: A Raman Spectroscopy Study |
| title_short | Structural Changes in Rice Bran Protein upon Different Extrusion Temperatures: A Raman Spectroscopy Study |
| title_sort | structural changes in rice bran protein upon different extrusion temperatures a raman spectroscopy study |
| url | http://dx.doi.org/10.1155/2016/6898715 |
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