Controlled formation of protein nanoparticles by enzymatic cross-linking of α-lactalbumin with horseradish peroxidase

Food Hydrocolloids

Volumn 36, Issue , 2014, Pages 53-59

  Dhayal, Surender K ^a   Gruppen, Harry ^a   de Vries, Renko ^a   Wierenga, Peter A ^a  

^a WAGENINGEN UNIVERSITY   (Netherlands)

Author keywords

AF4; Conformation plot; Hierarchical biopolymers; Protein polymers; Shape factor

Indexed keywords

CROSSLINKING; HYDROGEN PEROXIDE; IONIC STRENGTH; OXIDATION; PROTEINS;

AF4; CONFORMATION PLOT; HIERARCHICAL BIOPOLYMER; HORSE-RADISH PEROXIDASE; MESOSCALE STRUCTURE; PROTEIN CONCENTRATIONS; PROTEIN NANOPARTICLES; PROTEIN POLYMERS; RADIUS OF GYRATION; SHAPES FACTORS;

NANOPARTICLES;

ARMORACIA RUSTICANA;

EID: 84884714189     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2013.09.003     Document Type: Article

References (33)

1. Andersson M., Wittgren B., Wahlund K.G. Accuracy in multiangle light scattering measurements for molar mass and radius estimations. Model calculations and experiments. Analytical Chemistry 2003, 75(16):4279-4291.
2. Aymard P., Durand D., Nicolai T., Gimel J.C. Fractality of globular protein aggregates: from the molecular to the microscopic level. Fractals 1997, 05(Suppl.02):23-43.
3. Báez G.D., Moro A., Ballerini G.A., Busti P.A., Delorenzi N.J. Comparison between structural changes of heat-treated and transglutaminase cross-linked beta-lactoglobulin and their effects on foaming properties. Food Hydrocolloids 2011, 25(7):1758-1765.
4. Baynton K.J., Bewtra J.K., Biswas N., Taylor K.E. Inactivation of horseradish peroxidase by phenol and hydrogen peroxide: a kinetic investigation. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1994, 1206(2):272-278.
5. Buchert J., Ercili Cura D., Ma H., Gasparetti C., Monogioudi E., Faccio G., et al. Crosslinking food proteins for improved functionality. Annual Review of Food Science and Technology 2010, 1(1):113-138.
6. Burchard W. Light scattering. Physical techniques for the study of food biopolymers 1994, 343-392. Blackie Academic & Professional, London. S.B. Ross-Murphy (Ed.).
7. Cervantes Martinez A., Rio E., Delon G., Saint-Jalmes A., Langevin D., Binks B.P. On the origin of the remarkable stability of aqueous foams stabilised by nanoparticles: link with microscopic surface properties. Soft Matter 2008, 4(7):1531-1535.
8. Destribats M., Lapeyre V., Wolfs M., Sellier E., Leal-Calderon F., Ravaine V., et al. Soft microgels as Pickering emulsion stabilisers: role of particle deformability. Soft Matter 2011, 7(17):7689-7698.
9. Dickinson E. Food emulsions and foams: Stabilization by particles. Current Opinion in Colloid and Interface Science 2010, 15(1-2):40-49.
10. Ercili-Cura D., Partanen R., Husband F., Ridout M., Macierzanka A., Lille M., et al. Enzymatic cross-linking of β-lactoglobulin in solution and at air-water interface: structural constraints. Food Hydrocolloids 2012, 28(1):1-9.
11. Guevara J.S., Mejia A.F., Shuai M., Chang Y.-W., Mannan M.S., Cheng Z. Stabilization of pickering foams by high-aspect-ratio nano-sheets. Soft Matter 2013, 9(4):1327-1336.
12. Heijnis W.H., Dekker H.L., de Koning L.J., Wierenga P.A., Westphal A.H., de Koster C.G., et al. Identification of the peroxidase-generated intermolecular dityrosine cross-link in bovine α-lactalbumin. Journal of Agricultural and Food Chemistry 2010, 59(1):444-449.
13. Heijnis W.H., Wierenga P.A., van Berkel W.J.H., Gruppen H. Directing the oligomer size distribution of peroxidase-mediated cross-linked bovine α-lactalbumin. Journal of Agricultural and Food Chemistry 2010, 58(9):5692-5697.
14. Hiller B., Lorenzen P.-C. Effect of buffer systems on the extent of enzymatic oligomerisation of milk proteins. LWT - Food Science and Technology 2008, 41(6):1140-1144.
15. Hunter T.N., Pugh R.J., Franks G.V., Jameson G.J. The role of particles in stabilising foams and emulsions. Advances in Colloid and Interface Science 2008, 137(2):57-81.
16. Kim D.A., Cornec M., Narsimhan G. Effect of thermal treatment on interfacial properties of β-lactoglobulin. Journal of Colloid and Interface Science 2005, 285(1):100-109.
17. Kirkland J.J., Dilks C.H., Rementer S.W., Yau W.W. Asymmetric-channel flow field-flow fractionation with exponential force-field programming. Journal of Chromatography A 1992, 593(1-2):339-355.
18. Lantto R., Puolanne E., Kalkkinen N., Buchert J., Autio K. Enzyme-aided modification of chicken-breast myofibril proteins: effect of laccase and transglutaminase on gelation and thermal stability. Journal of Agricultural and Food Chemistry 2005, 53(23):9231-9237.
19. Leeman M., Wahlund K.-G., Wittgren B. Programmed cross flow asymmetrical flow field-flow fractionation for the size separation of pullulans and hydroxypropyl cellulose. Journal of Chromatography A 2006, 1134(1-2):236-245.
20. Mahmoudi N., Axelos M.A.V., Riaublanc A. Interfacial properties of fractal and spherical whey protein aggregates. Soft Matter 2011, 7(17):7643-7654.
21. Mahmoudi N., Gaillard C., Boué F., Axelos M.A.V., Riaublanc A. Self-similar assemblies of globular whey proteins at the air-water interface: effect of the structure. Journal of Colloid and Interface Science 2010, 345(1):54-63.
22. Moro A., Báez G.D., Ballerini G.A., Busti P.A., Delorenzi N.J. Emulsifying and foaming properties of β-lactoglobulin modified by heat treatment. Food Research International 2013, 51(1):1-7.
23. Moro A., Báez G.D., Busti P.A., Ballerini G.A., Delorenzi N.J. Effects of heat-treated β-lactoglobulin and its aggregates on foaming properties. Food Hydrocolloids 2011, 25(5):1009-1015.
24. Nicolai T., Urban C., Schurtenberger P. Light scattering study of turbid heat-set globular protein gels using cross-correlation dynamic light scattering. Journal of Colloid and Interface Science 2001, 240(2):419-424.
25. Nilsson L. Separation and characterization of food macromolecules using field-flow fractionation: a review. Food Hydrocolloids 2013, 30(1):1-11.
26. Pichorner H., Metodiewa D., Winterbourn C.C. Generation of superoxide and tyrosine peroxide as a result of tyrosyl radical scavenging by glutathione. Archives of Biochemistry and Biophysics 1995, 323(2):429-437.
27. Pickering S.U. CXCVI.-Emulsions. Journal of the Chemical Society, Transactions 1907, 91(0):2001-2021.
28. Podzimek S. Size exclusion chromatography. Light scattering, size exclusion chromatography and asymmetric flow field flow fractionation 2011, John Wiley & Sons, Inc., Hoboken, New Jersey.
29. Ramsden W. Separation of solids in the surface-layers of solutions and 'suspensions' (observations on surface-membranes, bubbles, emulsions, and mechanical coagulation). Preliminary account. Proceedings of the Royal Society of London 1903, 72(477-486):156-164.
30. Rullier B., Novales B., Axelos M.A.V. Effect of protein aggregates on foaming properties of β-lactoglobulin. Colloids and Surfaces A: Physicochemical and Engineering Aspects 2008, 330(2-3):96-102.
31. Saricay Y., Dhayal S.K., Wierenga P.A., de Vries R. Protein cluster formation during enzymatic cross-linking of globular proteins. Faraday Discussions 2012, 158(1):51-63.
32. Saricay Y., Wierenga P., de Vries R. Nanostructure development during peroxidase catalysed cross-linking of α-lactalbumin. Food Hydrocolloids 2013, 33(2):280-288.
33. Schmitt C., Bovay C., Rouvet M., Shojaei-Rami S., Kolodziejczyk E. Whey protein soluble aggregates from heating with NaCl: Physicochemical, interfacial, and foaming properties. Langmuir 2007, 23(8):4155-4166.