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Protein Profiles of Major Korean Rice Cultivars

  • Wei, Chuanha (College of Pharmacy, Chungnam National University) ;
  • Kwon, Oh-Yun (Dept. of Food and Nutrition, Chungnam National University) ;
  • Liu, Xi-Wen (College of Pharmacy, Chungnam National University) ;
  • Kim, Hyoung-Chin (Bio-Evaluation Center, Korea Research Institute of Bioscience and Biotechnology) ;
  • Yoon, Won-Kee (Bio-Evaluation Center, Korea Research Institute of Bioscience and Biotechnology) ;
  • Kim, Hwan-Mook (Bio-Evaluation Center, Korea Research Institute of Bioscience and Biotechnology) ;
  • Kim, Mee-Ree (Dept. of Food and Nutrition, Chungnam National University)
  • Published : 2007.06.30

Abstract

The protein profiles among Korean rice cultivars were assessed by total protein determination, solubility fractionation, SDS-PAGE analysis and scanning densitometry. In the extraction of protein, the SDS/urea system at a neutral pH was more efficient than that at alkaline pH. The determination of total protein showed that the protein content was similar among cultivars, ranging from 87.9 to 92.7 mg/g dry weight. Additionally, the water/NaCl-soluble protein fraction, containing 14${\sim}$16 kDa albumin and 22 kDa globulin ${\alpha}$-globulin, was also similar among cultivars, with a range of 9.94 to 11.98 mg/g dry weight. The SDS-PAGE/densitometry of total protein showed that there was no discernable difference in proteins of higher molecular weights among various cultivars, whereas the amount of lower molecular weight proteins (14${\sim}$16 kDa) is somewhat variable among cultivars. Furthermore, SDS-PAGE analysis of water/NaCl-soluble and propanol-soluble fractions indicates that there is a discernible change in the content of albumin, globulin or prolamin among cultivars. Thus, the PAGE/densitometry method, preceded by solubility fractionation, is useful for examining differences in protein profiles of rice cultivars.

References

  1. Juliano BO. 1985. Rice Chemistry and Technology. 2nd ed. American Association of Cereal Chemists, St. Paul, MN
  2. Pszczola DE. 2001. Rice: not just for throwing. Food Technol 55: 53-59
  3. Sloan AE. 1997. Grain: all it's cracked up to be. Food Technol 51: 24-29
  4. Villareal RM, Juliano BO. 1978. Properties of glutelin from mature and developing rice grain. Phytochemistry 17: 177-182 https://doi.org/10.1016/S0031-9422(00)94141-4
  5. Lee CY, Kim SK. 1977. Rice protein: its composition, structure, occurrence and biosynthesis. J Korean Agric Chem Soc 20: 156-170
  6. Chrastil J, Zarins Z. 1994. Changes in peptide subunit composition of albumins, globlins, prolamins, and oryzenin in maturing rice grains. J Agric Food Chem 42: 2152-2155 https://doi.org/10.1021/jf00046a015
  7. Tecson EM, Esmama BV, Lontok LP, Julian BO. 1971. Studies on the extraction and composition of rice endosperm glutelin and prolamin. Cereal Chem 48: 169-181
  8. Osbouren JZY, Hettiarachchy NS, Rath N. 2001. Extraction, denaturation and hydrophobic properties of rice flour proteins. J Food Sci 66: 229-232 https://doi.org/10.1111/j.1365-2621.2001.tb11322.x
  9. Padhye VW, Salunkhe DK. 1979. Extraction and characterization of rice proteins. Cereal Chem 56: 389-393
  10. Baldo BA, Wrigley CW. 1984. Allergies to cereals. Adv Cereal Sci Technol 6: 289-356
  11. Limas GG, Salinas M, Moneo I, Fischer S, Wittmann- Liebold B, Mendez E. 1990. Purification and characterization, of ten new rice NaCl-soluble proteins: iden-tification of four, protein-synthesis inhibitors and two immunoglobulin-binding proteins. Planta 181: 1-9 https://doi.org/10.1007/BF00202318
  12. Urisu A, Yamada K, Masuda S, Komada H, Wada E, Kondo Y, Horiba F, Tsuruta M, Yasaki T, Yamada M, Torii S, Nakamua R. 1991. 16-kDa rice protein is one of the major allergens in rice grain extract and responsible for cross-allergenicity between cereal grains in the poaceae family. Int Arch Allergy Appl Immunol 96: 244-252 https://doi.org/10.1159/000235502
  13. Matsuda T, Sugiyama M, Nakamura R, Torii S. 1988. Purification and properties of an allergenic protein in rice grain. Agric Biol Chem 52: 1465-1470 https://doi.org/10.1271/bbb1961.52.1465
  14. Masayuki N, Takahiro A, Atsuo U, Takeya M, Angelina MA, Satoru N, Naohito A, Ryo N, Tsukasa M. 1996. Rice (Oryza sativa L.) ${\alpha}$-Amylase inhibitors of 14-16 kDa are potential allergens and products of a multigene family. J Agric Food Chem 44: 2624-2628 https://doi.org/10.1021/jf9508099
  15. Massimo DV, Giovanni G, Vittorio S. 1997. A small peptide from durum wheat gliadin prevents cell agglutination induced by prolamin-peptides toxic in celiac disease. Toxicology 120: 207-213 https://doi.org/10.1016/S0300-483X(97)00060-7
  16. Silano M, De Vincenzi M. 1999. Bioactive antinutritional peptides derived from cereal prolamins: a review. Nahrung 43: 175-184 https://doi.org/10.1002/(SICI)1521-3803(19990601)43:3<175::AID-FOOD175>3.0.CO;2-Z
  17. Joseph C, Zigrida Z. 1994. Changes in peptide subunit composition of albumins, globulins, prolamins, and oryzenin in maturing rice grains. J Agric Food Chem 42: 2152-2155 https://doi.org/10.1021/jf00046a015
  18. Toshio S, Kunisuke T, Zenzauro K. 1986. Improved extraction of rice prolamin. Agric Biol Chem 50: 2409-2411 https://doi.org/10.1271/bbb1961.50.2409
  19. AOAC. 1990. Protein (crude) in animal feed, CuSO4/TiO2 mixed catalyst Kjeldahl method. In Official Methods of Analysis. Association of Official Analytical Chemists, Arlington, Virginia. p 70
  20. Bradford M. 1976. A rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254 https://doi.org/10.1016/0003-2697(76)90527-3
  21. Lowry OH, Rosenbrough GJ, Farr AL, Randall RJ. 1951. Protein measurement with the Folin-phenol reagent. J Biol Chem 193: 265-275
  22. Laemmli UK. 1970. Cleavage of structural protein during the assembly of the head of bacteriophage T4. Nature 227: 680-685 https://doi.org/10.1038/227680a0
  23. Wei CH, Sok DE, Yang YH, Oh SH, Kim HC, Yoon WK, Kim HM, Kim MR. 2006. Protein composition of domestic and glyphosate-tolerant soybean. J Korean Soc Food Sci Nutr 35: 470-475 https://doi.org/10.3746/jkfn.2006.35.4.470
  24. Tarr GE. 1986. Methods of Protein Microcharacterization. Shively JE, ed. Human Press, Clifton, NJ. p 155-194
  25. Steel RGD, Torrie JH. 1960. Principle and procedures of statistics. McGraw-Hill, New York, USA
  26. Ejeta G, Hassen MM, Mertz ET. 1987. In vitro digestibility and amino acid composition of pearl millet (Pennisetum typhoides) and other cereals. Proc Natl Acad Sci 84: 6016-6019 https://doi.org/10.1073/pnas.84.17.6016
  27. Daniel MB, Stuart JE. 1990. Protein methods. Wiley-Liss Inc., Wilmington DE, USA. p 116
  28. Samson A, Darren N, Dominic M. 2005. Characterization and functional properties of Australian. J Cereal Sci 41: 283-290 https://doi.org/10.1016/j.jcs.2004.10.007

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