Effects of thermal denaturation on binding between bixin and whey protein

Journal of Agricultural and Food Chemistry

Volumn 60, Issue 30, 2012, Pages 7526-7531

  Zhang, Yue ^a   Zhong, Qixin ^a  

^a UNIVERSITY OF TENNESSEE   (United States)

Author keywords

binding; bixin; circular dichroism; fluorescence quenching; thermal denaturation; whey protein

Indexed keywords

BINDING; BIXIN; FLUORESCENCE QUENCHING; THERMAL DENATURATIONS; WHEY PROTEINS;

AMINO ACIDS; DAIRY PRODUCTS; DICHROISM; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY; PROTEINS; QUENCHING;

DENATURATION;

BIXIN; BOVINE SERUM ALBUMIN; CAROTENOID; LACTALBUMIN; LACTOGLOBULIN; MILK PROTEIN; WHEY PROTEIN;

ANIMAL; ARTICLE; CATTLE; CHEMISTRY; CIRCULAR DICHROISM; HEAT; INFRARED SPECTROSCOPY; PH; PROTEIN DENATURATION; SPECTROFLUOROMETRY;

ANIMALS; CAROTENOIDS; CATTLE; CIRCULAR DICHROISM; HOT TEMPERATURE; HYDROGEN-ION CONCENTRATION; LACTALBUMIN; LACTOGLOBULINS; MILK PROTEINS; PROTEIN DENATURATION; SERUM ALBUMIN, BOVINE; SPECTROMETRY, FLUORESCENCE; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

BOVINAE;

EID: 84864773121     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf3021656     Document Type: Article

References (34)

1. Bu, G.; Luo, Y.; Zheng, Z.; Zheng, H. Effect of heat treatment on the antigenicity of bovine α-lactalbumin and β-lactoglobulin in whey protein isolate Food Agric. Immunol. 2009, 20 (3) 195-206
2. Oldfield, D. J.; Singh, H.; Taylor, M. W. Kinetics of heat-induced whey protein denaturation and aggregation in skim milks with adjusted whey protein concentration J. Dairy Res. 2005, 72 (3) 369-378
3. Mutilangi, W. A. M.; Panyam, D.; Kilara, A. Functional properties of hydrolysates from proteolysis of heat-denatured whey protein isolate J. Food Sci. 1996, 61 (2) 270-275
4. Bhattacharjee, C.; Das, K. P. Thermal unfolding and refolding of β-lactoglobulin - an intrinsic and extrinsic fluorescence study Eur. J. Biochem. 2000, 267 (13) 3957-3964
5. Viseu, M. I.; Melo, E. P.; Carvalho, T. I.; Correia, R. F.; Costa, S. M. B. Unfolding kinetics of β-lactoglobulin induced by surfactant and denaturant: a stopped-flow/fluorescence study Biophys. J. 2007, 93 (10) 3601-3612
6. Sulkowska, A.; Bojko, B.; Rownicka, J.; Pentak, D.; Sulkowski, W. Effect of urea on serum albumin complex with antithyroid drugs: fluorescence study J. Mol. Struct. 2003, 651, 237-243
7. Preston, H. D.; Rickard, M. D. Extraction and chemistry of annatto Food Chem. 1980, 5 (1) 47-56
8. Zhang, Y.; Zhong, Q. X. Binding between bixin and whey protein at pH 7.4 studied by spectroscopy and isothermal titration calorimetry J. Agric. Food Chem. 2012, 60 (7) 1880-1886
9. Monahan, F. J.; German, J. B.; Kinsella, J. E. Effect of pH and temperature on protein unfolding and thiol-disulfide interchange reactions during heat-induced gelation of whey proteins J. Agric. Food Chem. 1995, 43 (1) 46-52
10. Hinrichs, J. Incorporation of whey proteins in cheese Int. Dairy J. 2001, 11 (4-7) 495-503
11. Bryant, C. M.; McClements, D. J. Molecular basis of protein functionality with special consideration of cold-set gels derived from heat-denatured whey Trends Food Sci. Technol. 1998, 9 (4) 143-151
12. Palatasa, H.; Harjinder, S.; Creamer, L. K. Characterization of heat-induced aggregates of β-lactoglobulin, α-lactalbumin and bovine serum albumin in a whey protein concentrate environment J. Dairy Res. 2001, 68 (3) 483-497
13. Damodaran, S. Zinc-induced precipitation of milk fat globule membranes: a simple method for the preparation of fat-free whey protein isolate J. Agric. Food Chem. 2010, 58 (20) 11052-11057
14. Qi, Z. D.; Zhou, B.; Xiao, Q.; Shi, C.; Liu, Y.; Dai, J. Interaction of rofecoxib with human serum albumin: determination of binding constants and the binding site by spectroscopic methods J. Photochem. Photobiol. A-Chem. 2008, 193 (2-3) 81-88
15. Zhou, B.; Qi, Z. D.; Xiao, Q.; Dong, J. X.; Zhang, Y. Z.; Liu, Y. Interaction of loratadine with serum albumins studied by fluorescence quenching method. J. Biochem. Biophys. Methods 2007, 70, 743-747.
16. Burgos, I.; Dassie, S. A.; Villarreal, M. A.; Fidelio, G. D. Thermodynamic and structural analysis of homodimeric proteins: model of β-lactoglobulin Biochim. Biophys. Acta-Proteins Proteomics 2012, 1824 (2) 383-391
17. McClements, D. J.; Keogh, M. K. Physical-properties of cold-setting gels formed from heat-denatured whey-protein isolate J. Sci. Food Agric. 1995, 69 (1) 7-14
18. Zhang, Y.; Qi, Z. D.; Zheng, D.; Li, C. H.; Liu, Y. Interactions of chromium(III) and chromium(VI) with bovine serum albumin studied by UV spectroscopy, circular dichroism, and fluorimetry Biol. Trace Elem. Res. 2009, 130 (2) 172-184
19. Lakowicz, J. R. Principles of Fluorescence Spectroscopy, 2 nd ed.; Plenum Press: New York, 1999.
20. Lange, D. C.; Kothari, R.; Patel, R. C.; Patel, S. C. Retinol and retinoic acid bind to a surface cleft in bovine β-lactoglobulin: a method of binding site determination using fluorescence resonance energy transfer Biophys. Chem. 1998, 74 (1) 45-51
21. Weiss, S. Fluorescence spectroscopy of single biomolecules Science 1999, 283 (5408) 1676-1683
22. Harvey, B. J.; Bell, E.; Brancaleon, L. A tryptophan rotamer located in a polar environment probes pH-dependent conformational changes in bovine β-lactoglobulin A J. Phys. Chem. B 2007, 111 (10) 2610-2620
23. Kelkar, D. A.; Chaudhuri, A.; Haldar, S.; Chattopadhyay, A. Exploring tryptophan dynamics in acid-induced molten globule state of bovine α-lactalbumin: a wavelength-selective fluorescence approach Eur. Biophys. J. Biophys. Lett. 2010, 39 (10) 1453-1463
24. Kandagal, P. B.; Ashoka, S.; Seetharamappa, J.; Shaikh, S. M. T.; Jadegoud, Y.; Ijare, O. B. Study of the interaction of an anticancer drug with human and bovine serum albumin: spectroscopic approach J. Pharm. Biomed. Anal. 2006, 41 (2) 393-399
25. Kong, H.; Wang, H.; Zhang, S. C.; Zhang, X. R. A thermochemiluminescence array for recognition of protein subtypes and their denatured shapes Analyst 2011, 136 (18) 3643-3648
26. Whitmore, L.; Wallace, B. A. DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data Nucleic Acids Res. 2004, 32, W668-W673
27. Sreerama, N.; Woody, R. W. A self-consistent method for the analysis of protein secondary structure from circular-dichroism Anal. Biochem. 1993, 209 (1) 32-44
28. Pelton, J. T.; McLean, L. R. Spectroscopic methods for analysis of protein secondary structure Anal. Biochem. 2000, 277 (2) 167-176
29. Xu, D. X.; Yuan, F.; Jiang, J. P.; Wang, X. Y.; Hou, Z. Q.; Gao, Y. X. Structural and conformational modification of whey proteins induced by supercritical carbon dioxide Innovative Food Sci. Emerging Technol. 2011, 12 (1) 32-37
30. Bhattacharjee, C.; Saha, S.; Biswas, A.; Kundu, M.; Ghosh, L.; Das, K. P. Structural changes of β-lactoglobulin during thermal unfolding and refolding - an FT-IR and circular dichroism study Protein J. 2005, 24 (1) 27-35
31. Hu, X.; Zhao, M. M.; Sun, W. Z.; Zhao, G. L.; Ren, J. Y. Effects of microfluidization treatment and transglutaminase cross-linking on physicochemical, functional, and conformational properties of peanut protein isolate J. Agric. Food Chem. 2011, 59 (16) 8886-8894
32. Li, H.; Hardin, C. C.; Foegeding, E. A. NMR studies of thermal denaturation and cation-mediated aggregation of β-lactoglobulin J. Agric. Food Chem. 1994, 42 (11) 2411-2420
33. Davis, P. J.; Williams, S. C. Protein modification by thermal processing Allergy 1998, 53, 102-105
34. Palazolo, G.; Rodriguez, F.; Farruggia, B.; Pico, G.; Delorenzi, N. Heat treatment of β-lactoglobulin: structural changes studied by partitioning and fluorescence J. Agric. Food Chem. 2000, 48 (9) 3817-3822