Structural Stability of Globulins

Journal of Agricultural and Food Chemistry

Volumn 44, Issue 1, 1996, Pages 100-105

  Gorinstein, Shela ^a,b   Zemser, Marina ^a   Paredes López, Octavio ^c  

^a HEBREW UNIVERSITY OF JERUSALEM   (Israel)

^b David R Bloom Center for Pharmacy

^c DEPARTAMENTO DE FÍSICA   (Mexico)

Author keywords

Amaranth; Calorimetry; Denaturation; Quinoa; Spectroscopy

Indexed keywords

AMARANTHUS CAUDATUS; BOVINAE; CHENOPODIUM QUINOA;

EID: 0002980769     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf9500849     Document Type: Article

References (33)

1. Arntfield, S. D.; Murray, E. D. The influence of processing parameters on food protein functionality; I: differential scanning calorimetry as an indicator of protein denaturation. Can. Inst. Food Sci. Technol. J. 1981, 14, 289-294.
2. Arntfield, S. D.; Ismond, M. A. H.; Murray, E. D. Use of intrinsic fluorescence to follow the denaturation of vicilin, a storage protein from Vicia, faba. Int. J. Pept. Protein Res. 1987, 29, 9-20.
3. Barba de la Rosa, A. P.; Paredes-López, O.; Gueguen, J. Characterization of amaranth globulins by ultracentrifugation and chromatographic techniques. J. Agric. Food Chem. 1992, 40, 937-940.
4. Biliaderis, C. G. Differential scanning ealorimetry in food research. A review. Food Chem. 1983, 10, 239-265.
5. Bora, P. S.; Brekke, C. J.; Powers, J. R. Heat induced gelation of pea (Pisum Sativum) mixed globulins, vicilin and legumin. J. Food Sci. 1994, 59, 594-596.
6. Brinegar, C.; Goundan, S. Isolation and characterization of chenopodin, the 11S seed storage protein of quinoa (Chenopodium quinoa). J. Agric. Food Chem. 1993, 41, 182-185.
7. Coulter, L.; Lorenz, K. Quinoa composition, nutritional value, food applications. Lebensm. Wiss. Technol. 1990, 23, 203-207.
8. Gorinstein, S.; Moshe, R.; Greene, L. J.; Arruda, P. Evaluation of four Amaranthus species through protein electrophoretic patterns and their amino acid composition. J. Agric. Food Chem. 1991, 39, 851-854.
9. Gorinstein, S.; Zemser, M.; Friedman, M.; Chang, Sh. M. Simultaneous differential scanning calorimetry, X-ray diffraction and FT-IR spectrometry in studies of ovalbumin denaturation. Int. J. Pept. Protein Res. 1995, 45, 248-256.
10. Gorinstein, S.; Zemser, M.; Friedman, M.; Vasco-Méndez, N. L.; Paredes-López, O. Denaturant-induced conformations of globulins. J. Agric. Food Chem. 1996, 44, 93-99.
11. Hizukuri, S. In Starch Science Handbook (Japanese); Nakamura, M., Suzuki, S., Eds.; Asakura Shoten: Tokyo, Japan. 1978; pp 209-209.
12. Kaiden, K.; Matsui, T.; Tanaka, S. A study of the amide III band by FT-IR spectrometry of the secondary structure of albumin, myoglobin, and α-globulin. Appl. Spectrosc. 1987, 42, 180-184.
13. Kato, K.; Matsui, T.; Tanaka, S. Quantitative estimation of α-helix coil content in bovine serum albumin by Fourier transform-infrared spectroscopy. Appl. Spectrosc. 1987, 41, 861-865.
14. Kato, A.; Ibrahim, H. R.; Watanabe, H.; Honma, K.; Kobayashi, K. Structural and gelling properties of dry-heating egg white proteins. J. Agric. Food Chem. 1990, 38, 32-37.
15. Kinsella, J. E.; Phillips, L. G. Structure: functional relationship in food proteins, film and foaming behaviour. In Food Proteins; Kinsella, J. E., Soucie, W. G., Eds.; American Oil Chemists' Society: Champaign, IL, 1989, Chapter 4, pp 125-158.
16. Konishi, Y.; Fumita, Y.; Ikeda K; Okuno, K.; Fuwa H. Isolation and characterization of globulin from seeds of Amaranthus hypochondriacus. Agric. Biol. Chem. 1985, 49, 1453-1459.
17. Konishi, Y.; Yoshimoto, H. Amaranth globulin as a heat-stable emulsifying agent. Agric. Biol. Chem. 1989, 53, 3327-3328.
18. Ma, C. Y.; Harwalkar, V. R. Studies of thermal denaturation of oat globulin by differential scanning calorimetry. J. Food Sci. 1988, 53, 531-534.
19. Mansour, E. H.; Dworschak, E.; Peredi, J.; Lugasi, A. Evaluation of pumpkin seed (Cucurbita pepo, Kakai 35) as a new source of protein. Acta Aliment. 1993, 22, 3-13.
20. Marcone, M. F.; Yada, R. Y. Isolation, purification, and characterization of the oligomeric seed globulin from Amaranthus hypochondriacus. Agric. Biol. Chem. 1991, 55, 2281-2289.
21. Marcone, M. F.; Yada, R. Y. Study of the charge profile and covalent subunit-association of the oligomeric seed globulin from Amaranthus hypochondriacus. J. Agric. Food Chem. 1992, 40, 385-389.
22. Nagano, T.; Mori, H.; Nishinari, K. Effect of heating and cooling on the gelation kinetics of 7S globulin from soybeans. J. Agric. Food Chem. 1994, 42, 1415-1419.
23. Nara, Sh.; Mori, A.; Komiya, T. Study of relative crystallinity of moist potato starch. Starch / Staerke 1978, 30, 111-114.
24. Paredes-López, O.; Guzmán-Maldonado, H.; Ordorica-Falomir, C. Food proteins from emerging seed sources. In New and Developing Sources of Food Proteins; Hudson, B. J. F., Ed.; Chapman and Hall: London, 1994; pp 240-279.
25. Pharmacia LKB. Separation Technique File No. 100/5001255 P100, Pharmacia LKB, S-75-182 Uppsala, Sweden, 1985.
26. Saio, K.; Watanabe, T. Differences in functional properties of 7S and 11S soybean proteins. J. Texture Stud. 1978, 9, 135-157.
27. Segura-Nieto, M.; Barba de la Rosa, A. P.; Paredes-López, O. Biochemistry of amaranth proteins. In Amaranth-Biology, Chemistry and Technology; Paredes-López, O., Ed.; CRC: Boca Raton, FL, 1994; Chapter 8, pp 76-95.
28. Utsumi, S.; Damodaran, S.; Kinsella, J. E. Heat induced proteins: preferential association of 11S basic subunits and of 7S. J. Agric. Food Chem. 1984, 32, 1406-1412.
29. Van-Seuningen, I.; Davril, M. A rapid periodic acid-Schiff staining procedure for the detection of glycoproteins using the Phast system. Electrophoresis 1992, 13, 97-99.
30. Voutsina, L. P.; Cheung, E.; Nakai, S. Relationships of hydrophilicity to emulsifying properties of heat denatured proteins. J. Food Sci. 1983, 48, 26-32.
31. Wagner, J. R.; Añon, M. C. Denaturation kinetics of myofibrillar proteins in bovine muscle. J. Food Sci. 1985, 50, 1547-1550.
32. Wang, D.-H.; Damodaran, S. Thermal gelation of globular proteins: influence of protein conformation on gel strength. J. Agric. Food Chem. 1991, 39, 433-438.
33. Zemser, M.; Friedman, M.; Katzhendler, J.; Greene, L. J.; Minsky, A.; Gorinstein, S. Relationship between functional properties and structure of ovalbumin. J. Prot. Chem. 1994, 13, 261-274.