Thermal aggregation of patatin studied in situ

Journal of Agricultural and Food Chemistry

Volumn 47, Issue 11, 1999, Pages 4600-4605

  Pots, André M ^a   Ten Grotenhuis, Erik ^b,c   Gruppen, Harry ^d   Voragen, Alphons G J ^d   De Kruif, Kees G ^b,c  

^a TNO   (Netherlands)

^b NIZO FOOD RESEARCH   (Netherlands)

^c TOP INSTITUTE FOOD AND NUTRITION   (Netherlands)

^d WAGENINGEN UNIVERSITY   (Netherlands)

Author keywords

Kinetic; Mechanism; Patatin; Thermal aggregation

Indexed keywords

PATATIN; PROTEIN; UNCLASSIFIED DRUG; VEGETABLE PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; GEL CHROMATOGRAPHY; IONIC STRENGTH; KINETICS; LIGHT SCATTERING; MODEL; NEUTRON SCATTERING; PHYSICAL CHEMISTRY; POLYMERIZATION; POTATO; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; TEMPERATURE; TEMPERATURE SENSITIVITY;

CARBOXYLIC ESTER HYDROLASES; CHROMATOGRAPHY, GEL; KINETICS; MODELS, CHEMICAL; PLANT PROTEINS; PROTEIN CONFORMATION; PROTEIN FOLDING; TEMPERATURE;

EID: 0033231176     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf9901901     Document Type: Article

References (38)

1. Amal, R.; Coury, J. R.; Raper, J. A.; Walsh, W. P.; Waite, T. D. Structure and kinetics of aggregating colloidal heamatite. Colloids Surfaces 1990, 46, 1-19.
2. Berne, R. J.; Pecora, R. Dynamic Lightscattering: With Applications to Chemistry, Biology, and Physics; Wiley: New York, 1976.
3. Boye, J. L.; Ma, C.-Y.; Harwalkar, V. R. Thermal denaturation and coagulation of proteins. In Food Proteins and Their Applications; Damodaran, S., Paraf, A., Eds.; Dekker: New York, 1997.
4. Bradford, M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72, 248-254.
5. Damodaran, S. Food proteins: An overview. In Food Proteins and Their Applications; Damodaran, S., Paraf, A., Eds.; Dekker: New York, 1997.
6. Einarson, M. B.; Berg, J. C. Electrosteric stabilization of colloidal latex dispersions J. Colloid Interface Sci. 1993, 155, 165-172.
7. Elofsson, U. A.; Dejmek, P.; Paulsson, M. A. Heat-induced aggregation of β-lactoglobulin studied by dynamic light-scattering. Int. Dairy J. 1996, 6, 343-357.
8. Griffin, W. G.; Griffin, M. C. A.; Martin, S. R.; Price, J. Molecular basis of thermal aggregation of bovine β-lactoglobulin. J. Chem. Soc., Faraday Trans. 1993, 89, 2879-2889.
9. Hedrich, H. C.; Isobe, K.; Stahl, B.; Nokihara, K.; Kordel, M.; Schmid, R. D.; Karas, M.; Hillenkamp, F.; Spener, F. Matrix-assisted ultraviolet laser desorption/ionization mass spectrometry applied to multiple forms of lipases. Anal. Biochem. 1993, 211, 288-292.
10. Hoffmann, M. A. M.; van Mil, P. J. J. M. Heat-induced aggregation of β-lactoglobulin: role of the free thiol group and sidulphide bonds. J. Agric. Food Chem. 1997, 45, 2942-2948.
11. Hoffmann, M. A. M.; Roefs, S. P. F. M.; Verheul, M.; van Mil, P. J. J. M.; De Kruif, K. G. Aggregation β-lactoglobulin studied in situ by light scattering. J. Dairy Res. 1996, 63, 423-440.
12. Hohlberg, A. I.; Stanley, D. W. Kinetics of bean protein thermal denaturation. J. Food Process. Present. 1987, 11, 31-42.
13. Kella, N. K. D. Heat-induced reversible gelation of arachin: kinetics, thermodynamics and protein species involved in the process. Int. J. Biol. Macromol. 1989, 11, 105-112.
14. Koppel, D. E. Analysis of macromolecular polydispersibility in intensity correlation spectroscopy: The method of cumulants. J. Chem. Phys. 1972, 57, 4814-4820.
15. Kyriakidis, A. S.; Yiantsios, S. G.; Karabelas, A. J. A study of colloidal particle brownian aggregation by light scattering techniques. J. Colloid Interface Sci. 1997, 195, 299-306.
16. Lin, M. Y.; Lindsay, H. M.; Weitz, D. A.; Ball, R. C.; Klein, R.; Meakin, P. Universiality in colloid aggregation. Nature 1989, 339, 360-362.
17. Lisinska, G.; Leszcynski, W. Potato Science and Technology; Elsevier Applied Science: London, U.K., 1989.
18. Meakin, P. Models for colloidal aggregation. Annu. Rev. Phys. Chem. 1988, 39, 237-267.
19. Mignery, G. A.; Pikaard, C. S.; Hannapel, D. J.; Park, W. D. Isolation and sequence analysis of cDNA's for the major potato protein patatin. Nucleic Acids Res. 1984, 12, 7987-8000.
20. Overbeek, J. Th. G. Kinetics of flocculation. In Colloid Science; Kruyt, H. R., Ed.; Elsevier: Amsterdam, The Netherlands, 1952; Vol. I.
21. Pedersen, J. S. Analysis of small-angle scattering data from colloids and polymer solutions: modeling and least-squares fitting. Adv. Colloid Interface Sci. 1997, 70, 171-210.
22. Pots, A. M.; Jongh de, H. H. J.; Gruppen, H.; Hamer, R. J.; Voragen, A. G. J. Heat-induced conformational changes of patatin, the major potato protein. Eur. J. Biochem. 1998a, 252, 66-72.
23. Pots, A. M.; de Jongh, H. H. J.; Gruppen, H.; Hessing, M.; Voragen, A. G. J. The pH dependence of the structural stability of patatin. J. Agric. Food Chem. 1998b, 46, 2546-2553.
24. Pots, A. M.; Gruppen, H.; De Jongh, H. H. J.; Van Boekel, M. A. J. S.; Walstra, P.; Voragen, A. G. J. Kinetic modeling of the thermal aggregation of patatin. J. Agric. Food Chem. 1999, 47, 4593-4599.
25. Racusen, D.; Foote, M. A major soluble glycoprotein of potato tubers. J. Food Biochem. 1980, 4, 43-52.
26. Racusen, D.; Weller, D. L. Molecular weight of patatin, a major potato tuber protein. J. Food Biochem. 1984, 8, 103-107.
27. Reerink, H.; Overbeek, J. Th. G. The rate of coagulation as a measure of the stability of silver iodide sols. Faraday Discuss. 1954, 18, 74-84.
28. Renard, D.; Axelos, M. A. V.; Boué, F.; Lefebvre, J. "Ordered" structure in solutions and gels of a globular protein as studied by small angle neutron scattering. Biopolymers 1996, 39, 149-159.
29. Roefs, S. P. F. M.; De Kruif, K. G. A model for the denaturation and aggregation of β-lactoglobulin. Eur. J. Biochem. 1994, 226, 883-889.
30. Rouw, P. W.; De Kruif, C. G. Adhesive hard-sphere colloidal dispersions: Fractal structures and fractal growth in silica dispersions. Phys. Rev. A 1989, 39, 5399-5408.
31. Saito, H.; Shimoda, M. Insecticyanin of Agrius convolvuli: purification and characterization of the biliverdin-binding protein from the larval hemolymph. Zool. Sci. 1997, 14, 777-783.
32. Schurtenberger, P.; Augusteyn, R. C. Structural properties of polydisperse biopolymer solutions: A light scattering study of bovine α-crystallin. Biopolymers 1991, 31, 1229-1240.
33. Stiekema, W. J.; Heidekamp, F.; Dirkse, W. G.; van Beckum, J.; de Haan, P.; ten Bosch, C.; Louwerse, J. D. Molecular cloning and analysis of four potato tuber mRNAs. Plant Mol. Biol. 1988, 11, 255-269.
34. Timmins, P. A.; Zaccai, G. Low resolution structures of biological complexes studied by neutron scattering. Eur. Biophys. J. 1988, 15, 257-268.
35. Verheul, M. Heat-induced aggregation of β-lactoglobulin studied by small-angle neutron scattering. In Aggregation and Gelation of Whey Proteins; Ph.D. Thesis, Universiteit Twente, Enschede, The Netherlands, 1998.
36. Verheul, M.; Roefs, S. P. F. M.; De Kruif, K. G. Kinetics of heat-induced aggregation of β-lactoglobulin. J. Agric. Food Chem. 1998, 46, 896-903.
37. Von Smoluchowski, M. Versuch einer mathematischen theorie der koagulationskinetik kolloider lösungen. Z. Phys. Chem. 1917, 92, 129-168.
38. Ware, B. E. Light scattering. In Optical Techniques in Biological Research; Rousseau, D. L., Ed.; Academic Press: Orlando, FL, 1984.