Nanoscale understanding of thermal aggregation of whey protein pretreated by transglutaminase

Journal of Agricultural and Food Chemistry

Volumn 61, Issue 2, 2013, Pages 435-446

  Wang, Wan ^a   Zhong, Qixin ^a   Hu, Zhixiong ^a  

^a UNIVERSITY OF TENNESSEE   (United States)

Author keywords

enzymatic cross linking; nanostructure; rheology; surface properties; thermal aggregation; whey protein

Indexed keywords

DENATURATION TEMPERATURES; ENZYMATIC CROSS-LINKING; MICROBIAL TRANSGLUTAMINASE (MTGASE); NANO SCALE; NANOSCALE STRUCTURE; PRE-TREATMENT; SURFACE HYDROPHOBICITY; THERMAL AGGREGATION; THERMAL DENATURATIONS; TRANSGLUTAMINASES; WHEY PROTEIN ISOLATE; WHEY PROTEINS;

ATOMIC FORCE MICROSCOPY; DISPERSIONS; HYDROPHOBICITY; NANOSTRUCTURES; NANOTECHNOLOGY; PARTICLE SIZE ANALYSIS; PREHEATING; RHEOLOGY; SODIUM CHLORIDE; SURFACE PROPERTIES; TURBIDITY; ZETA POTENTIAL;

PROTEINS;

BACTERIAL PROTEIN; MILK PROTEIN; NANOPARTICLE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; WHEY PROTEIN;

ARTICLE; BEVERAGE; CHEMISTRY; EMULSION; HEAT; METABOLISM; PARTICLE SIZE; PROTEIN CONFORMATION; PROTEIN STABILITY; SURFACE PROPERTY; SUSPENSION; VISCOSITY;

BACTERIAL PROTEINS; BEVERAGES; EMULSIONS; HOT TEMPERATURE; MILK PROTEINS; NANOPARTICLES; PARTICLE SIZE; PROTEIN CONFORMATION; PROTEIN STABILITY; SURFACE PROPERTIES; SUSPENSIONS; TRANSGLUTAMINASES; VISCOSITY;

EID: 84872592911     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf304506n     Document Type: Article

References (50)

1. Lee, S. J.; Choi, S. J.; Li, Y.; Decker, E. A.; McClements, D. J. Protein-stabilized nanoemulsions and emulsions: comparison of physicochemical stability, lipid oxidation, and lipase digestibility J. Agric. Food Chem. 2011, 59, 415-427
2. Loveday, S. M.; Su, J.; Rao, M. A.; Anema, S. G.; Singh, H. Effect of calcium on the morphology and functionality of whey protein nanofibrils Biomacromolecules 2011, 12, 3780-3788
3. Betz, M.; Hörmansperger, J.; Fuchs, T.; Ulrich Kulozik, U. Swelling behaviour, charge and mesh size of thermal protein hydrogels as influenced by pH during gelation Soft Matter 2012, 8, 2477-2485
4. Chen, L.; Subirade, M. Alginate-whey protein granular microspheres as oral delivery vehicles for bioactive compounds Biomaterials 2006, 27, 4646-4654
5. Chen, L.; Subirade, M. Chitosan/β-lactoglobulin core-shell nanoparticles as nutraceutical carriers Biomaterials 2005, 26, 6041-6053
6. Foegeding, E. A.; Davis, J. P.; Doucet, D.; McGuffey, M. K. Advances in modifying and understanding whey protein functionality Trends Food Sci. Technol. 2002, 13, 151-159
7. 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, 143-151
8. Kulmyrzaev, A.; Bryant, C.; McClements, D. J. Influence of sucrose on the thermal denaturation, gelation, and emulsion stabilization of whey proteins J. Agric. Food Chem. 2000, 48, 1593-1597
9. Baier, S.; McClements, D. J. Impact of preferential interactions on thermal stability and gelation of bovine serum albumin in aqueous sucrose solutions J. Agric. Food Chem. 2001, 49, 2600-2608
10. Chantrapornchai, W.; McClements, D. J. Influence of glycerol on optical properties and large-strain rheology of heat-induced whey protein isolate gels Food Hydrocolloids 2002, 16, 461-466
11. Chanasattru, W.; Decker, E. A.; McClements, D. J. Modulation of thermal stability and heat-induced gelation of β-lactoglobulin by high glycerol and sorbitol levels Food Chem. 2007, 103, 512-520
12. Yong, Y. H.; Foegeding, E. A. Effects of caseins on thermal stability of bovine β-lactoglobulin J. Agric. Food Chem. 2008, 56, 10352-10358
13. Zhang, W.; Zhong, Q. Microemulsions as Nanoreactors to produce whey protein nanoparticles with enhanced heat stability by sequential enzymatic cross-linking and thermal pretreatments J. Agric. Food Chem. 2009, 57, 9181-9189
14. Zhang, W.; Zhong, Q. Microemulsions as nanoreactors to produce whey protein nanoparticles with enhanced heat stability by thermal pretreatment Food Chem. 2010, 119, 1318-1325
15. Jaros, D.; Partschefeld, C.; Henle, T.; Rohm, H. Transglutaminase in dairy products: chemistry, physics, applications J. Texture Stud. 2006, 37, 113-155
16. Rodriguez-Nogales, J. Enhancement of transglutaminase-induced protein cross-linking by preheat treatment of cows' milk: a statistical approach Int. Dairy J. 2006, 16 (1) 26-32
17. Agyare, K. K.; Damodaran, S. pH-stability and thermal properties of microbial transglutaminase-treated whey protein isolate J. Agric. Food Chem. 2010, 58, 1946-1953
18. Agyare, K. K.; Damodaran, S. pH-stability and thermal properties of microbial transglutaminase-treated whey protein isolate J. Agric. Food Chem. 2010, 58 (3) 1946-1953
19. Tanimoto, S. Y.; Kinsella, J. E. Enzymatic modification of proteins: effects of transglutaminase cross-linking on some physical properties of β-lactoglobulin J. Agric. Food Chem. 1988, 36, 281-285
20. Truong, V. D.; Clare, D. A.; Catignani, G. L.; Swaisgood, H. E. Cross-linking and rheological changes of whey proteins treated with microbial transglutaminase J. Agric. Food Chem. 2004, 52, 1170-1176
21. Tang, C. H.; Ma, C. Y. Modulation of the thermal stability of β-lactoglobulin by transglutaminase treatment Eur. Food Res. Technol. 2007, 225, 649-652
22. Rodriguez-Nogales, J. M. Effect of preheat treatment on the transglutaminase-catalyzed cross-linking of goat milk proteins Process Biochem. 2006, 41, 430-437
23. Rodriguez-Nogales, J. M. Enhancement of transglutaminase-induced protein cross-linking by preheat treatment of cows' milk: a statistical approach Int. Dairy J. 2006, 16, 26-32
24. Folk, J. E.; Cole, P. W. Transglutaminase: mechanistic features of the active site as determined by kinetic and inhibitor studies Biochim. Biophys. Acta 1966, 122, 244-264
25. Alizadeh-Pasdar, N.; Li-Chan, E. C. Y. Comparison of protein surface hydrophobicity measured at various pH values using three different fluorescent probes J. Agric. Food Chem. 2000, 48, 328-334
26. Han, X. Q.; Damodaran, S. Thermodynamic compatibility of substrate proteins affects their cross-linking by transglutaminase J. Agric. Food Chem. 1996, 44, 1211-1217
27. Ercili-Cura, D.; Partanen, R.; Husband, F.; Ridout, M.; Macierzanka, A.; Lille, M.; Boer, H.; Lantto, R.; Buchert, J.; Mackie, A. R. Enzymatic cross-linking of β-lactoglobulin in solution and at air-water interface: structural constraints Food Hydrocolloids 2012, 28, 1-9
28. Reddy, I. M.; Kella, N. K. D.; Kinsella, J. E. Structural and conformational basis of the resistance of β-lactoglobulin to peptic and chymotryptic digestion J. Agric. Food Chem. 1988, 36, 737-741
29. Cozzolino, A.; Di Pierro, P.; Mariniello, L.; Sorrentino, A.; Masi, P.; Porta, R. Incorporation of whey proteins into cheese curd by using transglutaminase Biotechnol. Appl. Biochem. 2003, 38, 289-295
30. Sharma, R.; Zakora, M.; Qvist, K. B. Susceptibility of an industrial α-lactalbumin concentrate to cross-linking by microbial transglutaminase Int. Dairy J. 2002, 12, 1005-1012
31. Eissa, A. S.; Puhl, C.; Kadla, J. F.; Khan, S. A. Enzymatic cross-linking of β-lactoglobulin: conformational properties using FTIR spectroscopy Biomacromolecules 2006, 7, 1707-1713
32. Parker, R.; Noel, T. R.; Brownsey, G. J.; Laos, K.; Ring, S. G. The nonequilibrium phase and glass transition behavior of β-lactoglobulin Biophys. J. 2005, 89, 1227-1236
33. Molek, J. R.; Zydney, A. L. Separation of PEGylated-lactalbumin from unreacted precursors and byproducts using ultrafiltration Biotechnol. Prog. 2007, 23, 1417-1424
34. Brownsey, G. J.; Noel, T. R.; Parker, R.; Ring, S. G. The glass transition behavior of the globular protein bovine serum albumin Biophys. J. 2003, 85, 3943-3950
35. Elofsson, C.; Dejmek, P.; Paulsson, M.; Burling, H. Atomic force microscopy studies on whey proteins Int. Dairy J. 1997, 7, 813-819
36. Aymard, P.; Nicolai, T.; Durand, D.; Clark, A. Static and dynamic scattering of β-lactoglobulin aggregates formed after heat-induced denaturation at pH 2 Macromolecules 1999, 32, 2542-2552
37. Ikeda, S.; Foegeding, E. Effects of lecithin on thermally induced whey protein isolate gels Food Hydrocolloids 1999, 13, 239-244
38. Ikeda, S.; Morris, V. J. Fine-stranded and particulate aggregates of heat-denatured whey proteins visualized by atomic force microscopy Biomacromolecules 2002, 3, 382-389
39. Rabiey, L.; Britten, M. Effect of protein composition on the rheological properties of acid-induced whey protein gels Food Hydrocolloids 2009, 23 (3) 973-979
40. Ryan, K.; Vardhanabhuti, B.; Jaramillo, D.; van Zanten, J.; Coupland, J.; Foegeding, E. Stability and mechanism of whey protein soluble aggregates thermally treated with salts Food Hydrocolloids 2012, 27, 411-420
41. Israelachvili, J. N. Intermolecular and Surface Forces, 2 nd ed.; Academic Press: San Diego, CA, 1992.
42. Zhu, H. M.; Damodaran, S. Heat-induced conformational-changes in whey-protein isolate and its relation to foaming properties J. Agric. Food Chem. 1994, 42, 846-855
43. Nicorescu, I.; Loisel, C.; Vial, C.; Riaublanc, A.; Djelveh, G.; Cuvelier, G.; Legrand, J. Combined effect of dynamic heat treatment and ionic strength on denaturation and aggregation of whey proteins-part I Food Res. Int. 2008, 41, 707-713
44. Fitzsimons, S. M.; Mulvihill, D. M.; Morris, E. R. Denaturation and aggregation processes in thermal gelation of whey proteins resolved by differential scanning calorimetry Food Hydrocolloids 2007, 21, 638-644
45. Unterhaslberger, G.; Schmitt, C.; Sanchez, C.; Appolonia-Nouzille, C.; Raemy, A. Heat denaturation and aggregation of β-lactoglobulin enriched WPI in the presence of arginine HCl, NaCl and guanidinium HCl at pH 4.0 and 7.0 Food Hydrocolloids 2006, 20, 1006-1019
46. Haug, I.; Skar, H.; Vegarud, G.; Langsrud, T.; Draget, K. Electrostatic effects on β-lactoglobulin transitions during heat denaturation as studied by differential scanning calorimetry Food Hydrocolloids 2009, 23 (8) 2287-2293
47. Vardhanabhuti, B.; Foegeding, E. A. Rheological properties and characterization of polymerized whey protein isolates J. Agric. Food Chem. 1999, 47, 3649-3655
48. 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
49. McClements, D. J. Food Emulsions: Principles, Practice, and Techniques, 2 nd ed.; CRC Press: Boca Raton, FL, 2005.
50. Russel, W. B.; Saville, D. A.; Schowalter, W. R. Colloidal Dispersions; Cambridge University Press: Cambridge, UK, 1989.