Relating the variation of secondary structure of gelatin at fish oil-water interface to adsorption kinetics, dynamic interfacial tension and emulsion stability

Food Chemistry

Volumn 143, Issue , 2014, Pages 484-491

  Liu, Huihua ^a   Wang, Bo ^b   Barrow, Colin J ^b   Adhikari, Benu ^a  

^a UNIVERSITY OF BALLARAT   (Australia)

^b DEAKIN UNIVERSITY   (Australia)

Author keywords

Emulsion stability; Gelatin; Interfacial tension; Protein adsorption kinetics; Zeta potential

Indexed keywords

ADSORPTION; DIFFUSION; FISH; KINETICS; PHASE INTERFACES; PROTEINS; STABILITY; SURFACE TENSION; ZETA POTENTIAL;

ADSORPTION KINETICS; DYNAMIC INTERFACIAL TENSION; EMULSION STABILITY; GELATIN; OIL WATER INTERFACES; PROTEIN ADSORPTION KINETICS; SECONDARY STRUCTURES; SURFACE HYDROPHOBICITY;

EMULSIFICATION;

ACID; FISH OIL; GELATIN; SODIUM HYDROXIDE; WATER;

ADDITION REACTION; ADSORPTION KINETICS; ALPHA HELIX; ARTICLE; BETA TURN; CONTROLLED STUDY; DIFFUSION COEFFICIENT; EMULSION; HYDROPHOBICITY; MOLECULAR DYNAMICS; PH; PROTEIN ANALYSIS; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; SOLUTION AND SOLUBILITY; SURFACE PROPERTY; TENSION; TRIPLE HELIX; VISCOSITY; ZETA POTENTIAL;

EID: 84883170760     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2013.07.130     Document Type: Article

References (52)

1. Aider, M., Djenane, D., & Ounis, W. B. (2012). Amino acid composition, foaming, emulsifying properties and surface hydrophobicity of mustard protein isolate as affected by pH and NaCl. International Journal of Food Science and Technology, 47, 1028-1036.
2. Akbulut, M., and Reddy., N. K., Bechtloff, B., Koltzenburg, S., Vermant, J., & Prud'homme, R. K. (2008). Flow-induced conformational changes in gelatin structure and colloidal stabilization. Langmuir, 24, 9636-9641.
3. Barth, A., & Zscherp, C. (2002). What vibrations tell us about proteins. Quarterly Reviews of Biophysics, 35, 369-430. (Pubitemid 36207229)
4. Berthomieu, C., & Hienerwadel, R. (2009). Fourier transform infrared (FTIR) spectroscopy. Photosynthesis Research, 101, 157-170.
5. Byler, D. M., & Susi, H. (1986). Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers, 25, 469-487.
6. Chaudhuri, T. K., and Das., K. P., & Sinha, N. K. (1993). Surface hydrophobicity of a low molecular weight basic trypsin subtilisin inhibitor from marine turtle eggwhite. Journal of Biochemistry, 113, 729-733. (Pubitemid 23201370)
7. Dagorn-Scaviner, C., Gueguen, J., & Lefebvre, J. (1987). Emulsifying properties of pea globulins as related to their adsorption behaviors. Journal of Food Science, 52, 335-341.
8. Dalgleish, D. G. (2006). Food emulsions - their structures and structure-forming properties. Food Hydrocolloids, 20, 415-422. (Pubitemid 43213122)
9. Dauphas, S. p., and Beaumal., V. r., Gunning, P., Mackie, A., Wilde, P., Vié, V., et al. (2007). Structures and rheological properties of hen egg yolk low density lipoprotein layers spread at the air-water interface at pH 3 and 7. Colloids and Surfaces, B: Biointerfaces, 57(1), 124.
10. de Jongh, H. H. J., & Wierenga, P. A. (2006). Assessing the extent of protein intermolecular interactions at air-water interfaces using spectroscopic techniques. Biopolymers, 82, 384-389. (Pubitemid 44000909)
11. de Kruif, C. G., Weinbreck, F., & de Vries, R. (2004). Complex coacervation of proteins and anionic polysaccharides. Current Opinion in Colloid and Interface Science, 9, 340-349. (Pubitemid 39592818)
12. Dicharry, C., Arla, D., Sinquin, A., Graciaa, A., & Bouriat, P. (2006). Stability of water/ crude oil emulsions based on interfacial dilatational rheology. Journal of Colloid and Interface Science, 297, 785-791.
13. Dong, A., Huang, P., & Caughey, W. S. (1990). Protein secondary structures in water from second-derivative amide I infrared spectra. Biochemistry, 29, 3303-3308. (Pubitemid 20131472)
14. Dong, A., Huang, P., & Caughey, W. S. (1992). Redox-dependent changes in b-extended chain and turn structures of cytochrome c in water solution determined by second derivative amide I infrared spectra. Biochemistry, 31, 182-189.
15. Drenth, J., & Mesters, J. (2007). Principles of protein X-ray crystallography (3rd ed.). New York: Springer.
16. Eisenberg, A., & Bailey, F. E. (1986). Coulombic interactions in macromolecular systems. The Society.
17. Fainerman, V., Lucassen-Reynders, E., & Miller, R. (2003). Description of the adsorption behaviour of proteins at water/fluid interfaces in the framework of a two-dimensional solution model. Advances in Colloid and Interface Science, 106, 237-259.
18. Joshi, M., Adhikari, B., Aldred, P., Panozzo, J. F., Kasapis, S., & Barrow, C. J. (2013). Interfacial and emulsifying properties of lentil protein isolate. Food Chemistry, 134(3), 1343-1353.
19. Jung, J. M., and Gunes., D. Z., & Mezzenga, R. (2010). Interfacial activity and interfacial shear rheology of native β-lactoglobulin monomers and their heat-induced fibers. Langmuir, 26(19), 15366-15375.
20. Kalnin, N., Baikalov, I., & Venyaminov, S. Y. (1990). Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. III: Estimation of the protein secondary structure. Biopolymers, 30, 1273-1280.
21. Kato, A., & Nakai, S. (1980). Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins. Biochimica et Biophysica Acta (BBA)-Protein Structure, 624, 13-20.
22. Kauppinen, J. K., and Moffatt., D. J., Mantsch, H. H., & Cameron, D. G. (1981). Fourier self-deconvolution: A method for resolving intrinsically overlapped bands. Applied Spectroscopy, 35, 271-276.
23. Kim, H. J., Decker, E., & McClements, D. (2002). Role of post adsorption conformation changes of β-lactoglobulin on its ability to stabilize oil droplets against flocculation during heating at neutral pH. Langmuir, 18, 7577-7583. (Pubitemid 35383178)
24. Kirby, B. J., & Hasselbrink, E. F. (2004). Zeta potential of microfluidic substrates. 1: Theory, experimental techniques, and effects on separations. Electrophoresis, 25, 187-202.
25. Kolanowski, W., & Laufenberg, G. (2006). Enrichment of food products with polyunsaturated fatty acids by fish oil addition. European Food Research and Technology, 222, 472-477. (Pubitemid 43214145)
26. Kong, J., & Yu, S. (2007). Fourier transform infrared spectroscopic analysis of protein secondary structures. Acta Biochimica et Biophysica Sinica, 39, 549-559. (Pubitemid 47293710)
27. Kotsmar, C., Grigoriev, D., Xu, F., Aksenenko, E., Fainerman, V., Leser, M., et al. (2008). Equilibrium of adsorption of mixed milk protein/surfactant solutions at the water/air interface. Langmuir, 24, 13977-13984.
28. Lee, D. C., and Haris., P. I., Chapman, D., & Mitchell, R. C. (1990). Determination of protein secondary structure using factor analysis of infrared spectra. Biochemistry, 29, 9185-9193. (Pubitemid 20320883)
29. Mackie, A. R., and Ridout., M. J., Moates, G., Husband, F. A., & Wilde, P. J. (2007). Effect of the interfacial layer composition on the properties of emulsion creams. Journal of Agricultural and Food Chemistry, 55, 5611-5619. (Pubitemid 47092935)
30. Mackie, A. R., and Gunning., A. P., Ridout, M. J., & Morris, V. J. (1998). Gelation of gelatin observation in the bulk and at the air-water interface. Biopolymers, 46(4), 245-252.
31. Michaeli, I. (1978). Ions in macromolecular and biological systems: Proceedings of the 29th symposium of the Colston Research Society. London: Scientechnica.
32. Miller, R., Fainerman, V., Aksenenko, E., Leser, M., & Michel, M. (2004). Dynamic surface tension and adsorption kinetics of β-casein at the solution/air interface. Langmuir, 20, 771-777.
33. Murray, B. S. (2002). Interfacial rheology of food emulsifiers and proteins. Current Opinion in Colloid and Interface Science, 7, 426-431. (Pubitemid 36007989)
34. Oberg, K. A., and Ruysschaert., J. M., & Goormaghtigh, E. (2004). The optimization of protein secondary structure determination with infrared and circular dichroism spectra. European Journal of Biochemistry, 271, 2937-2948. (Pubitemid 38980278)
35. Pearce, K. N., & Kinsella, J. E. (1978). Emulsifying properties of proteins: evaluation of a turbidimetric technique. Journal of Agricultural and Food Chemistry, 26, 716-723.
36. Pereira, L. G. C., Johansson, C., Radke, C. J., & Blanch, H. W. (2003). Surface forces and drainage kinetics of protein-stabilized aqueous films. Langmuir, 19, 7503-7513.
37. Petrescu, A. J., and Milac., A. L., Petrescu, S. M., Dwek, R. A., & Wormald, M. R. (2004). Statistical analysis of the protein environment of N-glycosylation sites: implications for occupancy, structure, and folding. Glycobiology, 14, 103-114. (Pubitemid 38263095)
38. Reis, P., Miller, R., Kragel, J., Leser, M., Fainerman, V., Watzke, H., et al. (2008). Lipases at interfaces: Unique interfacial properties as globular proteins. Langmuir, 24, 6812-6819.
39. Roberts, S. A., and Kellaway., I. W., Taylor, K. M. G., Warburton, B., & Peters, K. (2005). Combined surface pressure-interfacial shear rheology study of the effect of pH on the adsorption of proteins at the air-water interface. Langmuir, 21, 7342-7348. (Pubitemid 41156751)
40. Rotenberg, Y., Boruvka, L., & Neumann, A. (1983). Determination of surface tension and contact angle from the shapes of axisymmetric fluid interfaces. Journal of Colloid and Interface Science, 93, 169-183.
41. Sarver, R. W., & Krueger, W. C. (1991). Protein secondary structure from Fourier transform infrared spectroscopy: A data base analysis. Analytical Biochemistry, 194, 89-100.
42. Savitzky, A., & Golay, M. J. E. (1964). Smoothing and differentiation of data by simplified least squares procedures. Analytical Chemistry, 36, 1627-1639.
43. Singh, T., Boral, S., Bohidar, H., & Kumar, A. (2010). Interaction of gelatin with room temperature ionic liquids: A detailed physicochemical study. The Journal of Physical Chemistry B, 114, 8441-8448.
44. Smith, B. C. (2009). Fundamentals of Fourier transform infrared spectroscopy. CRC.
45. Sreerama, N., and Venyaminov., S. Y., & Woody, R. W. (2000). Estimation of protein secondary structure from circular dichroism spectra: Inclusion of denatured proteins with native proteins in the analysis. Analytical Biochemistry, 287(2), 243-251. (Pubitemid 32006233)
46. Surh, J., and Ward., L. S., & McClements, D. J. (2006). Ability of conventional and nutritionally-modified whey protein concentrates to stabilize oil-in-water emulsions. Food Research International, 39, 761-771. (Pubitemid 43766425)
47. Thies, C. (2007). Microencapsulation of flavors by complex coacervation. In J. M. Lakkis (Ed.), Encapsulation and Controlled Release Technologies in Food Systems (pp. 149-170). Iowa, USA: Blackwell Publishing, Ames.
48. Wang, B., Li, D., Wang, L. J., Adhikari, B., & Shi, J. (2010). Ability of flaxseed and soybean protein concentrates to stabilize oil-in-water emulsions. Journal of Food Engineering, 100, 417-426.
49. Ward, A., & Tordai, L. (1946). Time-dependence of boundary tensions of solutions. I. The role of diffusion in time-effects. The Journal of Chemical Physics, 14, 453.
50. Wishart, D., Sykes, B., & Richards, F. (1991). Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. Journal of Molecular Biology, 222(2), 311-333. (Pubitemid 121004009)
51. Xiong, Y. L. (2004). Muscle proteins. In R. Y. Yadda (Ed.), Proteins in food processing (pp. 106-120). Cambridge, England: Woodhead Publishing Limited.
52. Zhai, J., and Wooster., T. J., Hoffmann, S. V., Lee, T. H., Augustin, M. A., & Aguilar, M. I. (2011). Structural rearrangement of β-lactoglobulin at different oil-water interfaces and its effect on emulsion stability. Langmuir, 27, 9227-9236.