The characterization of soybean varieties by fluorescence spectroscopy

International Journal of Food Science and Technology

Volumn 40, Issue 5, 2005, Pages 545-555

  Khatib, Khaled A ^a   Herald, Thomas J ^b   Muiño, Pedro L ^c  

^a Mead Johnson Nutritionals ^*  (United States)

^b KANSAS STATE UNIVERSITY   (United States)

^c SAINT FRANCIS UNIVERSITY   (United States)

Author keywords

conglycinin; Glycinin; Soy protein fractions

Indexed keywords

Β-CONGLYCININ; FLUORESCENCE SPECTROSCOPY; GLYCININ; SOY PROTEIN FRACTION; SOYBEAN;

ABSORPTION; AMINO ACIDS; ELECTROMAGNETIC WAVES; FLUORESCENCE; MOLECULAR WEIGHT; PROTEINS; SPECTROSCOPIC ANALYSIS; SYNCHRONOUS MACHINERY;

FOOD PRODUCTS;

GLYCINE MAX;

EID: 18444408384     PISSN: 09505423     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2621.2005.00974.x     Document Type: Article

References (26)

1. Berry, D.G. (1998). Formulating soy foods. Dairy Foods, 99, 29-33.
2. Bopp, J.C., Muiño, P.L. & Callis, P.R. (2003). Nanosecond time-gated fluorescence spectra of NATA and tryptophan: long-lived 450 nm emission from oxidation products. Biophysical Journal, 84, 209A.
3. Campbell, M.F., Kraut, C.W., Yackel, W.C. & Yang, H.S. (1985). Soy protein concentrate, Ch. 9. In: New Protein Foods, Vol. 5, Seed Storage Proteins (edited by A.A. Altschul & H.L. Wilcke). Pp. 301-337. Orlando, FL: Academic Press.
4. Demchenko, A.P. (1986). Ultraviolet Spectroscopy of Proteins, Ch. 7. Pp. 145-172. New York, Springer-Verlag.
5. Deshpande, S.S. & Damodaran, S. (1990). Conformational characteristics of legume 7S globulins as revealed by circular dichroism, derivative UV absorption and fluorescence techniques. International Journal of Peptide and Protein Research, 35, 25-34.
6. Erdmann, J., Johnson, L.A., Liner, I.E. et al. (1999). Soy Protein Products: Characteristics, Nutritional Aspects, and Utilization. Washington, DC: Soy Protein Council. http://www.spcouncil.org.
7. Horton, H., Moran, L., Ochs, R., Rawn, J. & Scrimgeour, L. (2002). Principles of Biochemistry, 3rd edn. Pp. 68-69. Upper Saddle River, NJ: Prentice Hall.
8. Kim, K.S. & Rhee, J.S. (1989). Effects of acetylation on physicochemical properties of 11S-soy protein. Journal of Food Biochemistry, 13, 187-199.
9. Kolar, C.W., Richert, S.H., Decker, C.D., Steinke, F.H. & Vander Zanden, R.J. (1985). Isolated soy protein, Ch. 8. In: New Protein Foods, Vol. 5, Seed Storage Proteins (edited by A.A. Altschul & H.L. Wilcke). Pp. 251-299. New York: Academic Press.
10. Lakemond, C.M.M., Jongh, H.H.J., Hessing, M., Gruppen, H. & Voragen, A.G.J. (2000). Soy glycinin: influence of pH and ionic strength on solubility and molecular structure at ambient temperatures. Journal of Agricultural Food Chemistry, 48, 1985-1990.
11. Maruyama, N., Sato, R., Wada, Y. et al. (1999). Structure-physicochemical function relationships of soybean β-conglycinin constituent subunits. Journal of Agricultural Food Chemistry, 47, 5278-5284.
12. Morales, A. & Kokini, J.L. (1997). Glass transition of soy globulins using differential scanning calorimetry and mechanical spectrometry. Biotechnology Progress, 13, 624-629.
13. Munck, L. (1989). Fluorescence Analysis in Foods, Ch. 1. Pp. 1-29 and Ch. 2. Pp. 33-57. Harlow Essex, UK: Longman Scientific & Technical.
14. Nakhost, Z. & Karel, M. (1983). Changes in bovine myoglobulin due to interaction with methyl linoleate in a model system. Journal of Food Science, 48, 1335-1339.
15. Pederson, E.N., Brooks, D.S. & Muiño, P.L. (2001). Time-resolved fluorescence spectroscopy of tryptophan, indoles, and yohimbine. Biophysical Journal, 80, 365A.
16. Permyakov, E.A. (1998). Introduction to Spectroscopy of Proteins, 2nd edn. Pp. 5-24, 35-48 and 57-77. Boca Raton, FL: CRC Press.
17. Pernollet, J.C. & Mosse, J. (1983). Structures and location of legume and cereal seed storage proteins, Ch. 7. In: Seed Proteins (edited by J. Daussant, J. Mosse & J. Vaughn). Pp. 155-186. Annual Proceedings of the Phytochemical Society of Europe. London: Academic Press.
18. Petruccelli, S. & Añón, M.C. (1995). Partial reduction of soy protein isolates disulfide bonds. Journal of Agricultural Food Chemistry, 43, 2001-2006.
19. Riblett, A., Herald, T.J., Schmidt, K.A. & Tilley, K.A. (2001). Characterization of β-conglycinin and glycinin soy protein fractions from four selected soybean genotypes. Journal of Agricultural Food Chemistry, 49, 4983-4989.
20. Sharma, A. & Schulman, G.S. (1999). Introduction to Florescence Spectroscopy. Pp. 27-68. New York: John Wiley & Sons.
21. Stein, K. (2000). FDA approves health claims labeling for food containing soy protein. Journal of American Dietetic Association, 100, 292.
22. Sudhakar, K., Phillips, C.M., Williams, S.A. & Vanderkooi, J.M. (1993). Excited states of tryptophan in cod parvalbumin. Biophysical Journal, 64, 1503-1511.
23. Utsumi, S., Matsumura, Y. & Mori, T. (1997). Structure-function relationships of soy proteins. In: Food Proteins and their Applications (edited by S. Damodaran & A. Paraf). Pp. 257-291. New York: Dekker.
24. Vivian, J.T. & Callis, P.R. (2001). Mechanisms of tryptophan fluorescence shifts in proteins. Biophysical Journal, 80, 2093-2109.
25. Wagner, R.R., Sorgentini, D.A. & Añón, M.C. (1996). Thermal and electrophoretic behavior, hydrophobicity, and some functional properties of acid treated soy isolates. Journal of Agricultural Food Chemistry, 44, 1881-1889.
26. Yamagishi, T., Ebina, F. & Yamauchi, F. (1982). Analysis of the state of aromatic amino acid residues in heated soybean 7S globulin by absorption derivative spectrophotometry and spectrofluorimetry. Journal of Agricultural Biological Chemistry, 46, 2441-2448.