Physicochemical and functional characterization of cocosin, the coconut 11S globulin

Food Science and Technology Research

Volumn 16, Issue 3, 2010, Pages 225-232

  Angelia, Mark Rickard N ^a   Garcia, Roberta N ^a   Caldo, Kristian Mark P ^a   Prak, Krisna ^b   Utsumi, Shigeru ^b   Tecson Mendoza, Evelyn Mae ^a  

^a UNIVERSITY OF THE PHILIPPINES LOS BAÑOS   (Philippines)

^b KYOTO UNIVERSITY   (Japan)

Author keywords

Coconut; Cocosin; Emulsifying ability; Globulins; Solubility; Storage proteins; Thermal denaturation

Indexed keywords

INSECTIVORA;

EID: 77954303952     PISSN: 13446606     EISSN: None     Source Type: Journal    
DOI: 10.3136/fstr.16.225     Document Type: Article

References (35)

1. Balasundaresan, D., Sugadev, R. and Ponnuswamy, M.N. (2002). Purification and crystallization of coconut globulin cocosin from Cocos nucifera. Biochim. Biophys. Acta., 1601, 121-122. (Pubitemid 38234538)
2. Bradford, M.M. (1976). A rapid and sensitive method for the quantitation of microgram quantities for proteins utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254.
3. Carr, H.J., Plumb, G.W., Parker, M.L. and Lambert, N. (1990). Characterization and crystallization of an 11S seed storage globulin from coconut (Cocos nucifera). Food Chem., 38, 11-20.
4. rd Edition," ed. by Fennema, O.R., Marcel Dekker, New York, pp. 322-430.
5. DeMason, D.A. and Sekhar, K.N.C. (1990). Electrophoretic characterization and immunological localization of coconut (Cocos nucifera L.) endosperm storage proteins. Bot. Gaz., 151, 302-313.
6. Ellman, G.L. (1959). Tissue sulfhydryl groups. Arch. Biochem. Biophys., 82, 70-77.
7. Garcia, R.N., Arocena, R.V., Laurena, A.C. and Tecson-Mendoza, E.M. (2005). The 11S and 7S globulins of Coconut (Cocos nucifera L.): Purification and characterization. J. Agric. Food Chem., 53, 1734-1739.
8. Gueguen, J., Chevalier, M., Barbot, J. and Schaeffer, F. (1988). Dissociation and aggregation of pea legumin induced by pH and ionic strength. J. Sci. Food Agric., 44, 167-182.
9. Habeeb, A.F.S.A. (1975). Reaction of protein sulfhydryl groups with Ellman's reagent. Methods Enzymol., 25, 457-464.
10. Hidalgo, J. and Gamper, E. (1977). Solubility and heat stability of whey protein concentrates. J. Dairy Sci., 60, 1515-1518.
11. Hortsmann, C. (1983). Specific subunit pairs of legumin from Vicia faba. Phytochemistry, 22, 1861-1866.
12. Hoshi, Y. and Yamauchi, F. (1983). Determination of sulfhydryl and disulfide contents of soybean HS globulin and their change by lyophilization. Agric. Biol. Chem., 47, 2435-2440.
13. Krawczyk, G., Gisher, G., and Sewall, C. 2005. Stabilizing UHT Soy Beverages. Dairy Foods, January 10, 2005. http://www.dairy-foods.com/Articles/ Ingredient-Technology/7add47062e0a7010VgnVCM100000f932a8c0 (Accessed June 2009).
14. Kwon, K., Bae, D., Park, K.H. and Rhee, K.C. (1996a) Aqueous extraction and membrane techniques improve coconut protein concentrate functionality. J. Food Science, 61, 753-756. (Pubitemid 26310647)
15. Kwon, K., Park, K.H. and Rhee, K.C. (1996b). Fractionation and characterization of proteins from coconut (Cocos nucifera L.). J. Agric. Food Chem., 44, 1741-1745. (Pubitemid 126646192)
16. Kwon, K. and Rhee, K.C. (1996). Emulsifying coconut proteins as a function of salt, phosphate, and temperature. JAOCS, 73, 1669-1673. (Pubitemid 126547264)
17. Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head bacteriophage T4. Nature, 227, 680-685.
18. Lakemond, C.M.M., De Jongh, H.H.J., Hessing, M., Gruppen, H. and Voragen, A.G.J. (2000). Soy glycinin: Influence of pH and ionic strength on solubility and molecular structure at ambient temperatures. J. Agric. Food Chem., 48, 1985-1990. (Pubitemid 30431176)
19. Maruyama, N., Prak, K., Motoyama, S., Choi, S., Yagasaki, K., Ishimoto, M. and Utsumi, S. (2004). Structure-physicochemical function relationships of soybean glycinin at subunits levels assessed by using mutant lines. J. Agric. Food Chem., 52, 8197-8201. (Pubitemid 40053714)
20. Mepba, H.D. and Achinewhu, S.C. (2003). Effects of processing on protein nutritive quality of coconut Cocos nucifera products. Plant Foods Hum. Nutr., 58, 15-25.
21. Mills, E.N.C., Jenkins, J., Marigheto, N., Belton, P.S., Gunning, A.P. and Morris, V.J. (2002). Allergens of the cupin superfamily. Biochem. Soc. Trans., 30, 925-929.
22. Mohamad Ramlan, B.M.S., Maruyama, N., Adachi, M., Hontani, N., Saka, S., Kato, N., Ohkawa, Y. and Utsumi, S. (2002). Comparison of protein chemical and physicochemical properties of rapeseed cruciferin with those of soybean glycinin. J. Agric. Food Chem., 50, 7380-7385. (Pubitemid 35424906)
23. Mori, T., Maruyama, N., Nishizawa, K., Higasa, T., Yagasaki, K., Ishimoto, M. and Utsumi, S. (2004). The composition of newly synthesized proteins in the endoplasmic reticulum determines the transport pathways of soybean seed storage proteins. Plant J., 40, 238-249. (Pubitemid 39404073)
24. Reiner, C.K., Kada, G. and Gruber, H.J. (2002). Quick measurement of protein sulfhydryls with Ellman's reagent and with 4,4'-dithiodipyridine. Anal. Bioanal. Chem., 373, 266-276. (Pubitemid 34756941)
25. Rickert, D.A., Johnson, L.A. and Murphy, P.A. (2004). Functional properties of improved glycinin and β-conglycinin fractions. J. Food Sci., 69, 303-311.
26. Samson A.S. S.J., Khaund, R.N., Cater, C.M., and Mattil, K.F. 1971. Extractability of coconut proteins. J. Food Sci., 36, 72-728.
27. Shen, C. (2007). Process for making stable protein based acid beverage. United States Patent 7229659. http://www.freepatentsonline.com/7229659.html.
28. Shewry, P.R., Napier, J.A. and Tatham, A.S. (1995). Seed storage proteins: Structures and biosynthesis. Plant Cell, 7, 945-956.
29. Sjögren, B. and Spychalski, R. (1930). The molecular weight of cocosin. J. Am. Chem. Soc., 52, 4400-4404.
30. Soares, L.H.DB., Albuquerque, F., Assmann and Ayub, M.A.Z. (2004). Physicochemical properties of three food proteins treated with transglutaminase. Ciência Rural, 34, 1219-1223.
31. Staswick, P.E., Hermodson, M.A. and Nielsen, N.C. (1984). Idenfication of the cystines which link the acidic and basic components of the glycinin subunits. J. Biol. Chem., 259, 13431-13435.
32. Tandang, M.R.G., Adachi, M., Inui, N., Maruyama, N. and Utsumi, S. (2004). Effects of protein engineering of canola procruciferin on its physicochemical and functional properties. J. Agric. Food Chem., 52, 6810-6817.
33. Utsumi, S., Matsumura, Y. and Mori, T. (1997). Structure-function relationships of soy protein. In "Food Proteins and Their Applications," ed. by Damodaran, S. and Paraf, A., Marcel Dekker Inc., New York, pp. 257-291.
34. Venktesh, V. and Prakash, V. (1993). Functional properties of the total proteins of sunflower (Helianthus annuus L.) seed-effect of physical and chemical treatments. J. Agric. Food Chem., 41, 18-23.
35. Wolf, W.J. (1993). Sulfhydryl content of glycinin: Effect of reducing agents. J. Agric. Food. Chem., 41, 168-176.