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Abstract
Volume 6, Issue 4, August Issue - 2018, Pages:677-683 |
| Authors: Kamal Alhammad, Nazlin Howell |
| Abstract: FT-Raman spectroscopy revealed comparative intensity changes of many bands and wave number shifts, when comparing bovine serum albumin (BSA) separately, BSA mixed with 500 ppm cinnamaldehyde and BSA mixed with 500 ppm cinnamon. It is clear that there are small shifts in wave numbers. The intensity of tryptophan band at 760 ± 2 cm-1 was 0.42 ± 0.02; there was no significant difference between the value for BSA alone and BSA + cinnamon sample (0.433 ± 0.081). In contrast, in sample BSA + cinnamaldehyde the tryptophan band intensity (0.296 ± 0.066) significantly decreased (p<0.05). The decrease was ascribed to Trp vibrational modes and C-H bending due to the enhancement of hydrophobic residues open to the outer surface of proteins. This result can be used to monitor denaturation in protein aliphatic and aromatic side chains. The decrease in the tyrosine ratio 855/830 cm-1 of the BSA mixture with cinnamon and cinnamaldehyde separately, compared to BSA alone, was attributed to strong hydrogen bonding interactions in the mixture involving tyrosine residues. |
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