Thermal analysis of β-lactoglobulin complexes with pectins or carrageenan for production of stable biopolymer particles

Food Hydrocolloids

Volumn 24, Issue 2-3, 2010, Pages 239-248

  Jones, Owen ^a   Decker, Eric Andrew ^a   McClements, David Julian ^a  

^a UNIVERSITY OF MASSACHUSETTS   (United States)

Author keywords

Aggregation; Biopolymers; Carrageenan, stability; Nanoparticles; Pectin; Lactoglobulin

Indexed keywords

BIOMOLECULES; DIFFERENTIAL SCANNING CALORIMETRY; ELECTROSTATICS; MOLECULES; PROTEINS; THERMOANALYSIS; TURBIDITY;

BIOPOLYMER PARTICLES; CARRAGEENAN, STABILITY; CARRAGEENANS; ELECTROSTATIC COMPLEXES; HIGH METHOXYL PECTINS; LACTOGLOBULIN; LOW-METHOXYL PECTINS; PECTIN; TURBIDITY MEASUREMENTS; Β-LACTOGLOBULIN;

NANOPARTICLES;

EID: 70450237051     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2009.10.001     Document Type: Article

References (56)

1. Baeza R.I., and Pilosof A.M.R. Calorimetric studies of thermal denaturation of β -lactoglobulin in the presence of polysaccharides. Lebensmittel-Wissenschaft und-Technologie 35 5 (2002) 393-399
2. Benichou A., Aserin A., and Garti N. Protein-polysaccharide interactions for stabilization of food emulsions. Journal of Dispersion Science and Technology 23 (2002) 93-123
3. Brownlow S., Cabral J.H.M., Cooper R., Flower R., Yewdall S.J., Polikarpov I., et al. Bovine β -lactoglobulin at 1.8 A resolution - still an enigmatic lipocalin. Structure 5 (1997) 481-495
4. Chanasattru W., Decker E.A., and McClements D.J. Influence of glycerol and sorbitol on thermally induced droplet aggregation in oil-in-water emulsions stabilized by β-lactoglobulin. Food Hydrocolloids 23 2 (2009) 253-261
5. Chen L., Remondetto G.E., and Subirade M. Food protein-based materials as nutraceutical delivery systems. Trends in Food Science & Technology 17 (2006) 272-283
6. Chanasattru, W, Jones, O.G., Decker, E.A. & McClements, D.J. Impact of Cosolvents on Formation and Properties of Biopolymer Nanoparticles formed by Heat Treatment of -lactoglobulin-Pectin Complexes Food Hydrocolloids 23 (2009) 2450-2457
7. de Kruif C.G., and Tuinier R. Polysaccharide protein interactions. Food Hydrocolloids 15 (2001) 555-563
8. Donato L., Schmitt C., Bovetto L., and Rouvet M. Mechanism of formation of stable heat-induced β-lactoglobulin microgels. International Dairy Journal 19 5 (2009) 295-306
9. Emerich D.F., and Thanos C.G. Target nanoparticle-based drug delivery and diagnosis. Journal of Drug Targeting 15 3 (2007) 163-183
10. Galani D., and Apenten R.K.O. Revised equilibrium thermodynamic parameters for thermal denaturation of β-lactoglobulin at pH 2.6. Thermochimica Acta 363 1-2 (2000) 137-142
11. Gao J.Y., Dubin P.L., and Muhoberac B.B. Measurement of the binding of proteins to polyelectrolytes by frontal analysis continuous capillary electrophoresis. Analytical Chemistry 69 (1997) 2945-2951
12. Girard M., Turgeon S.L., and Gauthier S.F. Interbiopolymer complexing between β-lactoglobulin and low- and high-methoxylated pectin measured by potentiometric titration and ultrafiltration. Food Hydrocolloids 16 6 (2002) 585-591
13. Girard M., Turgeon S.L., and Gauthier S.F. Quantification of the interactions between β-lactoglobulin and pectin through capillary electrophoresis analysis. Journal of Agricultural and Food Chemistry 51 20 (2003) 6043-6049
14. Girard M., Turgeon S.L., and Gauthier S.F. Thermodynamic parameters of β-lactoglobulin-pectin complexes assessed by isothermal titration calorimetry. Journal of Agricultural and Food Chemistry 51 15 (2003) 4450-4455
15. Goldberg M., Langer R., and Jia X.Q. Nanostructured materials for applications in drug delivery and tissue engineering. Journal of Biomaterials Science. Polymer Edition 18 3 (2007) 241-268
16. Hattori T., Hallberg R., and Dubin P.L. Roles of electrostatic interaction and polymer structure in the binding of β-lactoglobulin to anionic polyelectrolytes: measurement of binding constants by frontal analysis continuous capillary electrophoresis. Langmuir 16 (2000) 9738-9743
17. Hoffmann M.A.M., and van Mil P. Heat-induced aggregation of β-lactoglobulin: role of the free thiol group and disulfide bonds. Journal of Agricultural and Food Chemistry 45 8 (1997) 2942-2948
18. Hoffmann M.A.M., and van Mil P. Heat-induced aggregation of β-lactoglobulin as a function of pH. Journal of Agricultural and Food Chemistry 47 5 (1999) 1898-1905
19. Hoffmann M.A.M., van Miltenburg J.C., van der Eerden J.P., van Mil P., and deKruif C.G. Isothermal and scanning calorimetry measurements on β-lactoglobulin. Journal of Physical Chemistry B 101 35 (1997) 6988-6994
20. Hong Y.-H., and McClements D.J. Formation of hydrogel particles by thermal treatment of β-lactoglobulin-chitosan complexes. Journal of Agricultural and Food Chemistry 55 14 (2007) 5653-5660
21. Iametti S., DeGregori B., Vecchio G., and Bonomi F. Modifications occur at different structural levels during the heat denaturation of β-lactoglobulin. European Journal of Biochemistry 237 1 (1996) 106-112
22. Ibanoglu E. Effect of hydrocolloids on the thermal denaturation of proteins. Food Chemistry 90 4 (2005) 621-626
23. Janhoj T., and Ipsen R. Effect of pre-heat treatment on the functionality of microparticulated whey protein in acid milk gels. Milchwissenschaft 61 2 (2006) 131-134
24. Janhoj T., Peterson C.B., Frost M.B., and Ipsen R. Sensory and rheological characterization of low-fat stirred yogurt. Journal of Texture Studies 37 3 (2006) 276-299
25. Jones O.G., Decker E.A., and McClements D.J. Formation of biopolymer particles by thermal treatment of β-lactoglobulin-pectin complexes. Food Hydrocolloids 23 (2009) 1312-1321
26. Jones, O.G., Lesmes, U., Dubin, P.L.McClements, D.J. Effect of polysaccharide charge on formation and properties of biopolymer nanoparticles created by heat treatment of β-lactoglobulin-pectin complexes. Food Hydrocolloids, in press.
27. Jones O.G., and McClements D.J. Stability of biopolymer particles formed by heat treatment of β-lactoglobulin/beet pectin electrostatic complexes. Food Biophysics 3 (2008) 191-197
28. Le Bon C., Nicolai T., and Durand D. Kinetics of aggregation and gelation of globular proteins after heat-induced denaturation. Macromolecules 32 19 (1999) 6120-6127
29. Lobato-Calleros C., Martinez-Torrijos O., Sandoval-Castilla O., Perez-Orozco J.P., and Vernon-Carter E.J. Flow and creep compliance properties of reduced-fat yoghurts containing protein-based fat replacers. International Dairy Journal 14 9 (2004) 777-782
30. Ma C.Y., and Harwalkar V.R. Effects of medium and chemical modification on thermal characteristics of β-lactoglobulin. Journal of Thermal Analysis and Calorimetry 47 5 (1996) 1513-1525
31. McClements D.J. Non-covalent interactions between proteins and polysaccharides. Biotechnology Advances 24 6 (2006) 621-625
32. Norton I.T., and Frith W.J. Microstructure design in mixed biopolymer composites. Food Hydrocolloids 15 (2001) 543-553
33. Plashchina I.G., Mrachkovskaya T.A., Danilenko A.N., Kozhevnikov G.O., Starodubrovskaya N.Y., Braudo E.E., et al. Complex formation of faba bean legumin with chitosan: surface activity and emulsion properties of complexes. Food colloids: Fundamentals of formulation conference (pp. 293-303). Potsdam, Germany (2000)
34. Qi X.L., Holt C., McNulty D., Clarke D.T., Brownlow S., and Jones G.R. Effect of temperature on the secondary structure of β-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: a test of the molten globule hypothesis. The Biochemical Journal 324 (1997) 341-346
35. Ridley B.L., O'Neill M.A., and Mohnen D. Pectins: structure, biosynthesis, and oligogalacturonide-related signaling. Phytochemistry 57 (2001) 929-967
36. Rinaudo M. Polyelectrolyte properties of a plant and animal polysaccharide. International meeting on structural aspects of the intercellular matrices of plants and animals (2008), Springer/Plenum Publishers, St Tropez, FRANCE 277-289
37. Santipanichwong R., Suphantharika M., Weiss J., and McClements D.J. Core-shell biopolymer nanoparticles produced by electrostatic deposition of beet pectin onto heat-denatured β-lactoglobulin aggregates. Journal of Food Science 73 6 (2008) 23-30
38. Sawyer L. β-lactoglobulin. In: Fox P.F., and McSweeney P.L.H. (Eds). Advanced dairy chemistry. Proteins, part A Vol. 1 (2003), Kluwer Academic/Pluwer, New York, NY 319-386
39. Schmitt C., Bovay C., Rouvet M., Shojaei-Rami S., and Kolodziejczyk E. Whey protein soluble aggregates from heating with NaCl: physicochemical, interfacial, and foaming properties. Langmuir 23 (2007) 4155-4166
40. Schmitt C., Sanchez C., Desobry-Banon S., and Hardy J. Structure and technofunctional properties of protein-polysaccharide complexes: a review. Critical Reviews in Food Science and Nutrition 38 8 (1998) 689-753
41. Seyrek E., Dubin P.L., Tribet C., and Gamble E.A. Ionic strength dependence of protein-polyelectrolyte interactions. Biomacromolecules 4 (2003) 273-283
42. Sperber B., Schols H.A., Stuart M.A.C., Norde W., and Voragen A.G.J. Influence of the overall charge and local charge density of pectin on the complex formation between pectin and β-lactoglobulin. Food Hydrocolloids 23 3 (2009) 765-772
43. Tamime A.Y., Kalab M., Muir D.D., and Barrantes E. The microstructure of set-style, natural yogurt made by substituting microparticulate whey protein for milk fat. Journal of the Society of Dairy Technology 48 4 (1995) 107-111
44. Tolstoguzov V.B. Thermodynamic aspects of biopolymer functionality in biological systems, foods, and beverages. Critical Reviews in Biotechnology 22 2 (2002) 89-174
45. Tolstoguzov V.B. Some thermodynamic considerations in food formulation. Food Hydrocolloids 17 1 (2003) 1-23
46. Tolstoguzov V.B. Ingredient interactions: aggregation and phase separation. In: McClements D.J. (Ed). Understanding and controlling the microstructure of complex foods, part I: Microstructural elements and their interactions (2006), Woodhead, Cambridge, UK
47. Turgeon S.L., Beaulieu M., Schmitt C., and Sanchez C. Protein-polysaccharide interactions: phase-ordering kinetics, thermodynamic and structural aspects. Current Opinion in Colloid & Interface Science 8 4-5 (2003) 401-414
48. Turgeon S.L., Schmitt C., and Sanchez C. Protein-polysaccharide complexes and coacervates. Current Opinion in Colloid & Interface Science 12 4-5 (2007) 166-178
49. Ubbink J., and Krueger J. Physical approaches for the delivery of active ingredients in foods. Trends in Food Science & Technology 17 (2006) 244-254
50. Vardhanabhuti B., Yucel U., Coupland J.N., and Foegeding E.A. Interactions between β-lactoglobulin and dextran sulfate at near neutral pH and their effect on thermal stability. Food Hydrocolloids 23 6 (2009) 1511-1520
51. Verheul M., Roefs S., and de Kruif K.G. Kinetics of heat-induced aggregation of β-lactoglobulin. Journal of Agricultural and Food Chemistry 46 3 (1998) 896-903
52. Walter R.H. Polysaccharide dispersions: Chemistry and technology in food (1998), Academic Press, San Diego, CA
53. Wang X., Lee J., Wang Y.-W., and Huang Q. Composition and rheological properties of β-lactoglobulin/pectin coacervates: effects of salt concentration and initial protein/polysaccharide ratio. Biomacromolecules 8 (2007) 992-997
54. Weinbreck F., Nieuwenhuijse H., Robijn G.W., and de Kruif C.G. Complexation of whey proteins with carrageenan. Journal of Agricultural and Food Chemistry 52 11 (2004) 3550-3555
55. Williams P.A. Gelling agents. In: Williams P.A. (Ed). Handbook of industrial water soluble polymers (2007), Blackwell Publ., Oxford, UK 73-97
56. Yu S., Hu J., Pan X., Yao P., and Jiang M. Stable and pH-sensitive nanogels prepared by self-assembly of chitosan and ovalbumin. Langmuir 22 (2006) 2734-2759