Structural changes induced in bovine serum albumin by covalent attachment of chlorogenic acid |
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| Affiliation: | 1. Department of Engineering, Aarhus University, Gustav Wieds vej 10, Aarhus 8000, Denmark;2. Department of Dairy Science, Faculty of Agriculture, Cairo University, Giza 12613, Egypt;3. Department of Biochemistry, Faculty of Agriculture, Cairo University, Giza 12613, Egypt;4. Department of Chemistry, Aarhus University, Gustav Wieds vej 14, Aarhus 8000, Denmark;5. Department of Biomedicine, Aarhus University, Wilhelm Meyers Allé 4, Aarhus 8000, Denmark;1. College of Food Science, Northeast Agricultural University, Harbin 150030, China;2. College of Food Engineering, Harbin University of Commerce, Harbin, Heilongjiang 150028, China;3. Heilongjiang Green Food Science Research Institute, Harbin 150028, China;4. National Research Center of Soybean Engineering and Technology, Harbin 150028, China;1. Beijing Advanced Innovation Center for Food Nutrition and Human Health, Beijing Laboratory for Food Quality and Safety, Beijing Key Laboratory of Functional Food from Plant Resources, College of Food Science & Nutritional Engineering, China Agricultural University, Beijing, 100083, China;2. Department of Food Science, University of Massachusetts Amherst, Amherst, MA 01003, USA;3. Department of Biochemistry, Faculty of Science and Production of Bioproducts for Industrial Applications Research Group, P.O. Box 80203, Jeddah, 21589, Saudi Arabia |
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| Abstract: | Bovine serum albumin (BSA) was modified by covalent attachment of chlorogenic acid using different concentrations at pH 9. The derivatization was accompanied by a reduction of lysine, cysteine and tryptophan residues. The isoelectric points were shifted to lower pH values and formation of high molecular weight fractions was noted. The structural changes were studied using circular dichroism, differential scanning calorimetry (DSC), intrinsic fluorescence, and binding of anilinonaphthalenesulfonic acid. The results showed that the content of α-helix decreased with a parallel increase in unordered structures with higher degrees of derivatization. DSC revealed a decrease in both denaturation temperature and enthalpy. Surface hydrophobicity declined, indicating that hydrophilic regions were exposed on the molecular surface. Proteolytic digestion showed that, at a lower degree of derivatization, the tryptic degradation was most adversely effected, whereas the peptic digestion declined with increasing modification. A trypsin inhibitory effect of the breakdown products released from derivatized BSA was also observed. |
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