Study of conformation of vicilin from Dolichos lablab and Phaseolus calcaratus by Fourier-transform infrared spectroscopy and differential scanning calorimetry

Food Research International

Volumn 41, Issue 7, 2008, Pages 720-729

  Law, Ho Ying ^a   Choi, Siu Mei ^a   Ma, Ching Yung ^a  

^a UNIVERSITY OF HONG KONG   (Hong Kong)

Author keywords

Denaturation; Differential scanning calorimetry; Dolichos lablab; FTIR spectroscopy; Phaseolus calcaratus; Protein conformation; Thermal stability; Vicilin

Indexed keywords

AMIDES; CALORIMETERS; CALORIMETRY; DIFFERENTIAL SCANNING CALORIMETRY; FOURIER TRANSFORM INFRARED SPECTROSCOPY; FOURIER TRANSFORMS; LASER INTERFEROMETRY; SCANNING; SPECTROSCOPIC ANALYSIS; THERMODYNAMIC STABILITY;

DIFFERENTIAL SCANNING CALORIMETRY (PHOTO-DSC); ENVIRONMENTAL CONDITIONING; FOURIER; INFRARED (IR); IR SPECTRUM; MONITOR (CO); PHASEOLUS; SCANNING CALORIMETRY; SECONDARY STRUCTURES; THERMAL STABILITY; TRANSFORM INFRA RED SPECTROSCOPY; VICILIN;

INFRARED SPECTROSCOPY;

DOLICHOS; LABLAB PURPUREUS; VIGNA UMBELLATA;

EID: 48149103212     PISSN: 09639969     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodres.2008.05.004     Document Type: Article

References (70)

1. Allain A.-F., Paquin P., and 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 26 (1999) 337-344
2. Arakawa T., and Timasheff S.N. Preferential interactions of proteins with salts in concentrated solutions. Biochemistry 21 (1982) 6545-6552
3. Arntfield S.D., and Murray E.D. The influence of processing parameters on food protein functionality. I. Differential scanning calorimetry as an indicator of protein denaturation. Canadian Institute of Food Science and Technology Journal 14 (1981) 289-294
4. Arntfield S.D., Murray E.D., and Ismond M.A.H. Effect of salt on the thermal stability of storage proteins from fababean (Vicia Faba). Journal of Food Science 51 (1986) 371-377
5. Balasubramanian D., and Ramachandran C. Effect of protein denaturants on the structure of water: Electron spin resonance spin probe study. Proceedings of the Indian Academy of Sciences 87B (1978) 53-61
6. Bertazzon A., and Tsong T.Y. Study of effects of pH on the stability of domains in myosin rod by high-resolution differential scanning calorimetry. Biochemistry 29 (1990) 6453-6459
7. Bewley J.D., and Black M. Seeds Germination, structure and composition. Seeds: Physiology of development and germination. 2nd ed. (1994), Plenum Press, New York 1-33
8. Biliaderis C.G. Differential scanning calorimetry in food research - A review. Food Chemistry 10 (1983) 239-265
9. Boulter D., and Croy R.R.D. The structure and biosynthesis of legume seed storage proteins: A biological solution to the storage of nitrogen in seeds. Advances in Botanical Research 27 (1997) 1-84
10. Boye J.I., Alli I., and Ismail A.A. Interactions involved in the gelation of bovine serum albumin. Journal of Agricultural and Food Chemistry 44 (1996) 996-1004
11. Boye J.I., Ma C.-Y., and Harwalkar V.R. Thermal denaturation and coagulation of proteins. In: Damodaran S., and Paraf A. (Eds). Food proteins and their applications (1997), Marcel Dekker, Inc., New York 25-56
12. Boye J.I., Ma C.-Y., and Ismail A. Thermal denaturation and gelation characteristics of β-lactoglobulin genetic variants. In: Whitaker J.R., Shahidi F., Munguia A.L., Yada R.Y., and Fuller G. (Eds). Functional properties of proteins and lipids (ACS symposium series 708) (1998), American Chemical Society, Washington 168-183
13. Boye J.I., Ma C.Y., and Ismail A. Thermal stability of β-lactoglobulins A and B: Effect of SDS, urea, cysteine and N-ethylmaleimide. Journal of Dairy Research 71 (2004) 207-215
14. Byler D.M., and Susi H. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers 25 (1986) 469-487
15. Cai S., and Singh B.R. Identification of β-turn and random coil amide III infrared bands for secondary structure estimation of proteins. Biophysical Chemistry 80 (1999) 7-20
16. Casey R. Distribution and some properties of seed globulins. In: Shewry P.R., and Casey R. (Eds). Seed proteins (1999), Kluwer Academic Publishers, Dordrecht 159-169
17. Chau C.F., and Cheung P.C.K. Functional properties of flours prepared from three Chinese indigenous legume seeds. Food Chemistry 61 (1998) 429-433
18. Chau C.-F., and Cheung P.C.-K. Effects of the physico-chemical properties of three legume fibers on cholesterol absorption in hamsters. Nutrition Research 19 (1999) 257-265
19. Chau C.-F., Cheung P.C.K., and Wong Y.-S. Functional properties of protein concentrates from three Chinese indigenous legume seeds. Journal of Agricultural and Food Chemistry 45 (1997) 2500-2503
20. Chau C.-F., Cheung P.C.K., and Wong Y.-S. Hypocholesterolemic effects of protein concentrates form three Chinese indigenous legume seeds. Journal of Agricultural and Food Chemistry 46 (1998) 3698-3701
21. Cheftel J.C., Cuq J.-L., and Lorient D. Amino acids, peptides and proteins. In: Fennema O.R. (Ed). Food chemistry (1985), Marcel Dekker Inc., New York 356-375
22. Choi S.-M., and Ma C.-Y. Conformational study of globulin from common buckwheat (Fagopyrum esculentum Moench) by fourier transform infrared spectroscopy and differential scanning calorimetry. Journal of Agricultural and Food Chemistry 53 (2005) 8046-8053
23. Clark A.H., Saunderson D.H.P., and Suggett A. Infrared and laser-Raman spectroscopic studies of thermally-induced globular protein gels. International Journal of Peptide and Protein Research 17 (1981) 353-364
24. Damodaran S., and Knisella J.E. Effects of ions on protein conformation and functionality. In: Cherry J.P. (Ed). ACS symposium series 206 (1982), American Chemical Society, Washington 327-357
25. Derbyshire E., Wright D.J., and Boulter D. Legumin and vicilin, storage proteins of legume seeds. Phytochemistry 15 (1976) 3-24
26. Deshpande S.S., and Damodaran S. Conformational characteristics of legume 7S globulins as revealed by circular dichroic, derivative u.v. absorption and fluorescence techniques. International Journal of Peptide and Protein Research 35 (1990) 25-34
27. El Siddig O.O.A., El Tinay A.H., ABD Alla A.W.H., and Elkhalifa A.E.O. Proximate composition, minerals, tannins, in vitro protein digestibility and effect of cooking on protein fractions of hyacinth bean (Dolichos lablab). Journal of Food Science and Technology 39 (2002) 111-115
28. Gerlsma S.Y., and Stuur E.R. The effect of polyhydric and monohydric alcohols on the heat-induced reversible denaturation of lysozyme and ribonuclease. International Journal of Peptide and Protein Research 4 (1972) 377-383
29. Haris P.I., and Severcan F. FTIR spectroscopic characterization of protein structure in aqueous and non-aqueous media. Journal of Molecular Catalysis B Enzymatic 7 (1999) 207-221
30. Harwalkar V.R., and Ma C.-Y. Study of thermal properties of oat globulin by differential scanning calorimetry. Journal of Food Science 52 (1987) 394-398
31. Harwalkar V.R., and Ma C.-Y. Effects of medium composition, preheating, and chemical modification upon thermal behavior of oat globulin and β-lactoglobulin. In: Kinsella J.E., and Soucie W.G. (Eds). Food proteins (1989), The American Oil Chemists' Society, Champaign 210-231
32. Hatefi Y., and Hanstein W.G. Solubilization of particulate proteins and nonelectrolytes by chaotropic agents. Proceedings of the National Academy of Sciences 62 (1969) 1129-1136
33. Kinsella J.E., and Whitehead D.M. Proteins in whey: Chemical, physical and functional properties. Advances in Food Nutrition and Research 33 (1989) 343-438
34. Ko T.-P., Ng J.D., and McPherson A. The three-dimensional structure of canavalin from jack bean (Canavalia ensiformis). Plant Physiology 101 (1993) 729-744
35. Ko T.-P., Ng J.D., and McPherson A. The refined structure of canavalin from jack bean in two crystal forms at 2.1 and 2.0 Å resolution. Acta Crystallographica D56 (2000) 411-420
36. Koshiyama I., Hamano M., and Fukushima D. A heat denaturation study of the 11S globulin in soybean seeds. Food Chemistry 6 (1981) 309-322
37. Krimm S., and Bandekar J. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Advances in Protein Chemistry 38 (1986) 181-364
38. Kumosinski T.F., and Unruh J.J. Quantitation of the global secondary structure of globular proteins by FTIR spectroscopy: comparison with X-ray crystallographic structure. Talanta 43 (1996) 199-219
39. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
40. Lawrence M.C., Izard T., Beuchat M., Blagrove R.J., and Colman P.M. Structure of phaseolin at 2.2 Å resolution: Implications for a common vicilin/legumin structure and the genetic engineering of seed storage proteins. Journal of Molecular Biology 238 (1994) 748-776
41. Lawrence M.C., Suzuki E., Varghese J.N., Davis P.C., Van Donkelaar A., Tulloch P.A., and Colman P.M. The three-dimensional structure of the seed storage protein phaseolin at 3 Å resolution. The EMBO Journal 9 (1990) 9-15
42. Li, S. C. (1973). Chinese medicinal herbs. (Trans. F. P. Smith, G. A. Stuart), (Vol. 155, p. 316). San Francisco: Georgetown Press.
43. Li-Chan E.C.Y. The applications of Raman spectroscopy in food science. Trends in Food Science and Technology 7 (1996) 361-370
44. Lowry O.H., Rosenbrough N.J., Farr A.L., and Randall R.J. Protein measurement with Folin-phenol reagent. Journal of Biological Chemistry 193 (1951) 265-275
45. Ma C.-Y., and Harwalkar V.R. Studies of thermal denaturation of oat globulin by differential scanning calorimetry. Journal of Food Science 53 (1988) 531-534
46. Ma C.-Y., Rout M.K., and Mock W.-Y. Study of oat globulin conformation by Fourier transform infrared spectroscopy. Journal of Agricultural and Food Chemistry 49 (2001) 3328-3334
47. Marcone M.F., Kakuda Y., and Yada R.Y. Salt-soluble seed globulins of various dicotyledonous and monocotyledonous plants-I. Isolation/purification and characterization. Food Chemistry 62 (1998) 27-47
48. Matsudomi N., Rector D., and Kinsella J.E. Gelation of bovine serum albumin and β-lactoglobulin; Effects of pH, salts and thiol reagents. Food Chemistry 40 (1991) 55-69
49. Melander W., and Horváth C. Salt effects on hydrophobic interactions in precipitation and chromatography of proteins: An interpretation of the lyotropic series. Archives of Biochemistry and Biophysics 183 (1977) 200-215
50. Meng G.-T., and Ma C.-Y. Fourier-transform infrared spectroscopic study of globulin from Phaseolus angularis (red bean). International Journal of Biological Macromolecules 29 (2001) 287-294
51. Meng G.-T., and Ma C.-Y. Thermal properties of Phaseolus angularis (red bean) globulin. Food Chemistry 73 (2001) 453-460
52. Meng G., and Ma C.-Y. Characterization of globulin from Phaseolus angularis (red bean). International Journal of Food Science and Technology 37 (2002) 687-695
53. Nagano T., Akasaka T., and Nishinari K. Study on the heat-induced conformational changes of β-conglycinin by FTIR and CD analysis. Food Hydrocolloids 9 (1995) 83-89
54. Nagano T., Mori H., and Nishinari K. Rheological properties and conformational states of β-conglycinin gels at acidic pH. Biopolymers 34 (1994) 293-298
55. Pernollet J.-C., and Mossé J. Structure and location of legume and cereal seed storage proteins. In: Daussant J., Mossé J., and Vaughan J. (Eds). Seed proteins (1983), Academic Press Inc. (London) Ltd., London 155-191
56. Petruccelli S., and Añón M.C. pH-Induced modifications in the thermal stability of soybean protein isolates. Journal of Agricultural and Food Chemistry 44 (1996) 3005-3009
57. Potekhin S.A., and Privalov P.L. Co-operative blocks in tropomyosin. Journal of Molecular Biology 159 (1982) 519-535
58. Privalov P.L. Stability of proteins: Proteins which do not present a single cooperative system. Advances in Protein Chemistry 35 (1982) 1-104
59. Privalov P.L., and Khechinashvilli N.N. A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetry study. Journal of Molecular Biology 86 (1974) 665-684
60. Smith D.M. Protein interactions in gels: Protein-protein interactions. In: Hettiarachchy N.S., and Ziegler G.R. (Eds). Protein functionality in food systems (1994), Marcel Dekker Inc., New York 209-224
61. Steinhardt, J. (1975). The nature of specific and non-specific interactions of detergents with proteins: Complexing and unfolding. In H. Sund, G. Blauer (Eds.), Protein-ligand interactions: Proceedings of a symposium held at the University of Konstanz, West Germany, September 2-6, 1974 (pp. 412-426). Berlin: Walter de Gruyter & Co.
62. Surewicz W.K., and Mantsch H.H. New insight into protein secondary structure from resolution-enhanced infrared spectra. Biochimica et Biophysica Acta 952 (1988) 115-130
63. Susi H., and Byler D.M. Protein structure by Fourier transform infrared spectroscopy: Second derivative spectra. Biochemical and Biophysical Research Communications 115 (1983) 391-397
64. Utsumi S. Plant food protein engineering. Advances in Food and Nutrition Research 36 (1992) 89-208
65. Wang C.-H., and Damodaran S. Thermal gelation of globular proteins: Influence of protein conformation on gel strength. Journal of Agricultural and Food Chemistry 39 (1991) 433-438
66. Wong K.H., and Cheung P.C.K. Nutritional assessment of three Chinese indigenous legumes in growing rats. Nutrition Research 18 (1998) 1573-1580
67. Wright D.J. Thermoanalytical methods in food research. Critical Reports on Applied Chemistry 5 (1984) 1-36
68. Wright D.J. The seed globulins. In: Hudson B.J.F. (Ed). Developments in food proteins-5 (1987), Elsevier Applied Science Publishers Ltd., Essex 81-156
69. Xiong Y.L., and Kinsella J.E. Mechanism of urea-induced whey protein gelation. Journal of Agricultural and Food Chemistry 38 (1990) 1887-1891
70. Zirwer D., Gast K., Welfle H., Schlesier B., and Schwenke K.D. Secondary structure of globulins from plant seeds: A re-evaluation from circular dichroism measurements. International Journal of Biological Macromolecules 7 (1985) 105-108