Effect of thermal treatment on chemical structure of β-lactoglobulin and basil seed gum mixture at different states by ATR-FTIR spectroscopy

International Journal of Food Properties

Volumn 18, Issue 12, 2015, Pages 2652-2664

  Rafe, Ali ^a   Razavi, Seyed M A ^b  

^a RESEARCH INSTITUTE OF FOOD SCIENCE AND TECHNOLOGY RIFST   (Iran)

^b FERDOWSI UNIVERSITY OF MASHHAD   (Iran)

Author keywords

Basil seed gum; Fourier transform infrared spectroscopy; Gel; Secondary structure; Lactoglobulin

Indexed keywords

AMIDES; CARBOXYLATION; EMULSIFICATION; GELS; HYDROGEN BONDS; MIXTURES; STRUCTURE (COMPOSITION);

ATR FT-IR SPECTROSCOPIES; ATTENUATED TOTAL REFLECTION FOURIER TRANSFORM INFRARED SPECTROSCOPY; BETA-LACTOGLOBULIN; EMULSIFYING PROPERTY; INTERMOLECULAR HYDROGEN BONDING; LACTOGLOBULIN; SECONDARY STRUCTURES; SEED GUM;

FOURIER TRANSFORM INFRARED SPECTROSCOPY;

EID: 84940704698     PISSN: 10942912     EISSN: 15322386     Source Type: Journal    
DOI: 10.1080/10942912.2014.999864     Document Type: Article

References (45)

1. Akkermans, C., Venema, P., Van Der Goot, A.J., Gruppen, H., Bakx, E.J., Boom, R.M., Van Der Linden, E. Peptides are Building Blocks of Heat-Induced Fibrillar Protein Aggregates of β-Lactoglobulin Formed at pH 2. Journal of Biomacromolceules 2008, 9 (5), 1474-1479
2. Creusot, N., Gruppen, H. Enzyme-Induced Aggregation and Gelation of Proteins. Journal of Biotechnology Advances 2007, 25 (6), 597-601
3. Allain, A., Paquin, P., Subirade, M. Relationships Between Conformation of β-Lactoglobulin in Solution and Gel States as Revealed by Attenuated Total Reflection Fourier Transform Infrared Spectroscopy. International Journal of Biological Macromolecules 1999, 26 (5), 337-344
4. Boye, J.I., Alli, I. Thermal Denaturation of Mixtures of α-lactalbumin and β-Lactoglobulin: A Differential Scanning Calorimetric Study. Food Research International 2000, 33 (8), 673-682
5. Wada, R., Fujita, Y., Kitabatake, N. Effects of Heating at Neutral and Acid pH on the Structure of β-Lactoglobulin A Revealed by Differential Scanning Calorimetry and Circular Dichroism Spectroscopy. Biochimica et Biophysica Acta (BBA)-General Subjects 2006, 1760 (6), 841-847
6. Dong, A., Matsuura, J., Allison, S.D., Chrisman, E., Manning, M.C., Carpenter, J.F. Infrared and Circular Dichroism Spectroscopic Characterization of Structural Differences Between β-Lactoglobulin A and B. Biochimstry 1996, 35, 1450-1457
7. Aberkane, L., Jasniewski, J., Gaiani, C., Scher, J., Sanchez, C. Thermodynamic Characterization of Acacia Gum-β-Lactoglobulin Complex Coacervation. Langmuir 2010, 26 (15), 12523-12533
8. Boye, J.I., Ismail, A.A., Alli, I. Effects of Physicochemical Factors on the Secondary Structure of β-Lactoglobulin B. Journal of Dairy Research 1996, 63, 97-109
9. Goetz, J., Koehler, P. Study of the Thermal Denaturation of Selected Proteins of Whey and Egg by Low Resolution NMR. LWT-Food Science and Technology 2005, 38 (5), 501-512
10. Ikeda, S., Li-Chan, E.C.Y. Raman Spectroscopy of Heat-Induced Fine-Stranded and Particulate β-Lactoglobulin Gels. Journal of Food Hydrocolloids 2004, 18 (3), 489-498
11. Hosseiniparvar, S.H., Matia-Merino, L., Goh, K.K.T., Razavi, S.M.A., Mortazavi, S.A. Steady Shear Flow Behavior of Gum Extracted from Basil Seed (Ocimum basilicum L.): Effect of Concentration and Temperature. Journal of Food Engineering 2010, 101 (3), 236-243
12. Rafe, A., Razavi, S.M.A. Dynamic Viscoelastic Study on the Gelation of Basil Seed Gum. International Journal of Food Science and Technology 2013, 48 (3), 556-563
13. Mirhosseini, H., Tabatabaee Amid, B., A Review. Study on Chemical Composition and Molecular Structure of Newly Plant Gum Exudates and Seed Gums. Food Research International 2012, 46 (1), 387-397
14. Razavi, S.M.A., Mortazavi, S.A., Matia-Merino, L., Hosseini-Parvar, S.H., Motamedzadegan, A., Khanipour, E. Optimization Study of Gum Extraction from Basil Seeds (Ocimum basilicum L.). International Journal of Food Science and Technology 2009, 44 (9), 1755-1762
15. Rafe, A., Razavi, S.M.A., Farhoosh, R. Rheology and Microstructure of Basil Seed Gum and β-Lactoglobulin Mixed Gels. Food Hydrocolloids 2013, 30 (1), 134-142
16. Rafe, A., Razavi, S.M.A., Khan, S. Rheological. and Structural Properties of β-Lactoglobulin and Basil Seed Gum Mixture: Effect of Heating Rate. Food Research International 2012, 49 (1), 32-38
17. Dickinson, E., McClements, D. J. Protein-Polysaccharides Interactions. In Advances in Food Colloids; Dickinson, E.; Ed.; Blackie Academic & Professional: London, 1995; 81-101
18. Tolstoguzov, V.B. Some Physico-Chemical Aspects of Protein Processing in Foods. Multicomponent Gels. Food Hydrocolloids 1995, 9 (4), 317-332
19. Dickinson, E., James, J.D. Influence of High-Pressure Treatment on β-Lactoglobulin-Pectin Associations in Emulsions and Gels. Food Hydrocolloid 2000, 14 (4), 365-376
20. Gil, E.S., Frankowski, D.J., Bowman, M.K., Gozen, A.O., Hudson, S.M., Spontak, R.J. Mixed Protein Blends Composed of Gelatin and Bombyx Mori Silk Fibroin: Effects of Solvent-Induced Crystallization and Composition. Biomacromolecules 2006, 7 (3), 728-735
21. Gil, E.S., Frankowski, D.J., Hudson, S.M., Spontak, R.J. Silk Fibroin Membranes from Solvent-Crystallized Silk Fibroin/Gelatin Blends: Effects of Blend and Solvent Composition. Materials Science and Engineering 2007, 27 (3), 426-431
22. Aberkane, L., Jasniewski, J., Gaiani, C., Hussain, R., Scher, J., Sanchez, C. Structuration Mechanism of β-lactoglobulin-Acacia Gum Assemblies in Presence of Quercetin. Food Hydrocolloids 2012, 29 (1), 9-20
23. De Kruif, C.G., Tuinier, R. Polysaccharide Protein Interactions. Food Hydrocolloids 2001, 15 (4-6), 555-563
24. Vetri, V., Militello, V. Thermal Induced Conformational Changes Involved in the Aggregation Pathways of β-Lactoglobulin. Biophysical Chemistry 2005, 113 (1), 83-91
25. Pelton, J.T., McLean, L.R. Spectroscopic Methods for Analysis of Protein Secondary Structure. Analytical Biochemistry 2000, 277 (2), 167-176
26. Ngarize, S., Herman, H., Adams, A., Nazlin, H. Comparison of Changes in the Secondary Structure of Unheated, Heated, and High-Pressure-Treated β-Lactoglobulin and Ovalbumin Proteins Using Fourier Transform Raman Spectroscopy and Self-Deconvolution. Journal of Agriculture and Food Chemistry 2004, 52 (21), 6470-6477
27. Long, G., Ji, Y., Pan, H., Sun, Z., Li, Y., Qin, G. Characterization of Thermal Denaturation Structure and Morphology of Soy Glycinin by FTIR and SEM. International Journal of Food Properties 2015,. 18 (4), 763-774
28. Hu, X., Kaplan, D., Cebe, P. Determining Beta-Sheet Crystallinity in Fibrous Proteins by Thermal Analysis and Infrared Spectroscopy. Macromolceules 2006, 39 (18), 6161-6170
29. Renkema, J.M.S., Knabben, J.H.M., Vliet, T.V. Gel Formation by β-Conglycinin and Glycinin and Their Mixtures. Food Hydrocolloids 2001, 15 (4-6), 407-414
30. Militello, V., Casarino, C., Emanuele, A., Giostra, A., Pullara, F., Leone, M. Aggregation Kinetics of Bovine Serum Albumin Studied by FTIR Spectroscopy and Light Scattering. Journal of Biophysical Chemistry 2004, 107 (2), 175-187
31. Sakai, K., Sakurai, K., Sakai, M., Hoshino, M., Goto, Y. Conformation and Stability of Thiol-Modified Bovine β-Lactoglobulin. Protein Science 2000, 9, 1719-1729
32. Boye, J.I., Ismail, A.A., Alli, I. Effects of Physicochemical Factors on the Secondary Structure of β-Lactoglobulin. Journal of Dairy Research 1996, 63 (1), 97-109
33. Lefevre, T., Subirade, M. Structural and Interaction Properties of β-Lactoglobulin as Studied by FTIR Spectroscopy. International Journal of Food Science and Technology 1999, 34 (5-6), 419-428
34. Eissa, A., Puhl, C., Saad, K. Enzymatic Crosslinking of β-Lactoglobulin: Conformational Properties using FTIR Spectroscopy. Biomacromolecules 2006, 7 (6), 1707-1713
35. Nikonenko, N.A., Buslov, D.K., Sushko, R.G.Z., Bankov, B. Analysis of the Structure of Carbohydrates with Use of the Regularized Deconvolution Method of Vibrational Spectra. BAÜ Fen Bil. Enst. Dergisi 2002, 4, 2
36. Ma, X., Pawlik, M. Intrinsic Viscosities and Huggins Constants of Guar Gum in Alkali Metal Chloride Solutions. Carbohydrate Polymers 2007, 70 (1), 15-24
37. Kelly Ross, K., Siow, Y., Brown, D., Isaak, C., Fukumoto, L., Godfrey, D. Characterization of Water Extractable Crude Polysaccharides from Cherry, Raspberry, and Ginseng Berry Fruits: Chemical Composition and Bioactivity. International Journal of Food Properties 2015, 18 (3), 670-689
38. Kong, J., Yu, S. Fourier Transform Infrared Spectroscopic Analysis of Protein Secondary Structures. Acta Biochimica et Biophysica Sinica 2007, 39 (8), 549-559
39. Wang, Q., Ellis, P.R., Ross-Murphy, S.B. Dissolution Kinetics of Guar Gum Powders-II. Effects of Concentration and Molecular Weight. Carbohydrate Polymers 2003, 53 (1), 75-83
40. Synytsya, A., Copikova, J., Matejka, P., Machovic, V. Fourier Transform Raman and Infrared Spectroscopy of Pectins. Carbohydrate Polymers 2003, 54 (1), 97-106
41. Gullekson, C., Lucas, L., Hewitt, K., Kreplak, L. Surface-Sensitive Raman Spectroscopy of Collagen I Fibrils. Biophysical Journal 2011, 100 (7), 1837-1845
42. Gnanasambandam, R., Proctor, A. Preparation of Soy Hull Pectin. Food Chemistry 1999, 65, 461-467
43. Jung, C. Insight into Protein Structure and Protein-Ligand Recognition by Fourier Transform Infrared Spectroscopy. Journal of Molceular Recognition 2000, 13 (6), 325-351
44. Durrani, C.M., Pryrtupa, D.A., Donald, A.M., Clark, A.H. Phase Diagram of Mixtures of Polymers in Aqueous Solution Using Fourier Transform Infrared Spectroscopy. Macromolecules 1993, 26, 981-987
45. Gounga, M.E., Xu, S., Wang, Z. Whey Protein Isolate-Based Edible Films as Affected by Protein Concentration, Glycerol Ratio, and Pullulan Addition in Film Formation. Journal of Food Engineering 2007, 83 (4), 521-530