Loss of structural integrity and hydrophobic ligand binding capacity of acetylated and succinylated bovine β-lactoglobulin |
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| Authors: | Jishnu Chakraborty Niloy Das Kali P Das Umesh C Halder |
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| Affiliation: | 1. Organic Chemistry Section, Department of Chemistry, Jadavpur University, 188, Raja S.C. Mullik Road, Jadavpur, Kolkata 700032, West Bengal, India;2. Protein Chemistry Laboratory, Department of Chemistry, Bose Institute, 93/1 A.P.C. Road, Kolkata 700009, India;1. National Research and Development Center for Egg Processing, College of Food Science and Technology, Huazhong Agricultural University, Wuhan, Hubei 430070, PR China;2. Department of Life Science, Hefei Normal University, Hefei 230061, China;1. Department of Agricultural, Food and Nutritional Science, University of Alberta, Alberta, Canada;2. School of Printing and Packaging, Wuhan University, Hubei, China;1. Top Institute Food and Nutrition, P.O. Box 557, 6700 AN, Wageningen, The Netherlands;2. Laboratory of Physics and Physical Chemistry of Foods, Department of Agrotechnology and Food Sciences, Wageningen University, P.O. Box 17, 6700 AA, Wageningen, The Netherlands;3. ProtIn Consultancy, Nepveulaan 112, 3705LG, Zeist, The Netherlands;1. Advanced Food Systems Research Unit, College of Health and Biomedicine, Victoria University, Melbourne, VIC 8001, Australia;2. Friesland Campina, Amersfoort, The Netherlands;1. College of Science, Gansu Agricultural University, Lanzhou, China;2. College of Food Science and Engineering, Gansu Agricultural University, Lanzhou, China;3. Functional Dairy Product Engineering Lab of Gansu Province, Lanzhou, China;4. Instrumental Research and Analysis Center of Gansu Agricultural University, China |
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| Abstract: | The lysine residues of bovine β-lactoglobulin (β-lg) were acetylated and succinylated to investigate the effect of chemical modification on tertiary and secondary structures. Both derivatives showed higher electrophoretic mobility compared with native β-lg. The molar extinction coefficients of modified proteins were lower than native β-lg. A significant decrease in intrinsic tryptophan fluorescence intensities, and a red shift of emission maxima were observed. The structural stabilities of the derivatives were compared with the native form. Both modified β-lg structures were less stable against guanidine hydrochloride and urea denaturation. Hydrophobicities decreased, as measured by hydrophobic ligand binding of the modified β-lg. Circular dichroism spectra of modified forms were different. The beta structural content of modified β-lactoglobulins decreased substantially with an increase in random coil structure. These modifications changed the tertiary structure, and involved a significant loss of secondary structure of β-lg. |
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