Korean Journal of Environmental Agriculture (한국환경농학회지)

The Korean Society of Environmental Agriculture (한국환경농학회)
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Changes of Rice Storage Proteins Affected by Dry and Storage Temperature

건조 및 저장조건에 따른 쌀 저장단백질의 변화양상

  • Shin, Pyung-Gyun (Mushroom Research Division, National Institute of Horticultural & Herval Science) ;
  • Chang, An-Cheol (Soil and Fertilize Management Division, National Academy of Agricultural Science, RDA) ;
  • Hong, Seong-Chang (Soil and Fertilize Management Division, National Academy of Agricultural Science, RDA) ;
  • Lee, Ki-Sang (Soil and Fertilize Management Division, National Academy of Agricultural Science, RDA) ;
  • Lee, Keum-Hee (National Plant Quarantine Service, MAF) ;
  • Lee, Yong-Bok (Soil and Fertilize Management Division, National Academy of Agricultural Science, RDA)
  • 신평균 (농촌진흥청 국립원예특작과학원 버섯과) ;
  • 장안철 (국립농업과학원 토양비료관리과) ;
  • 홍성창 (국립농업과학원 토양비료관리과) ;
  • 이기상 (국립농업과학원 토양비료관리과) ;
  • 이금희 (식물검역원 중부격리재배연구소) ;
  • 이용복 (국립농업과학원 토양비료관리과)
  • Published : 2008.12.31
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Abstract

Quality of rice grain changes during dry storage with internal physiological changes and external injury by organism. Storage rice changes by condition with respiration via variable temperature, hydrolysis enzyme reaction, lipid peroxidation occurs with change of palatability. During dry storage, physiological change with protein variation pattern was examined by image analysis on proteomic technology. Analysis revealed that protein activity had no change store at room temperature and store at $40^{\circ}C$, but decreased store at $60^{\circ}C$. Analysis of variable hydrophobic protein pattern revealed that protein activity of beta-tubulin, protein disulfide isomerase, vacuolar ATPase b subunit, globulin was not significantly decreased all dry and store condition. However, heat shock protein 70, and glutathione transferase was significantly decreased when rice dried at $60^{\circ}C$ compared with room temperature and $40^{\circ}C$ dry condition.

Keywords

References

  1. Chae, J.C. (2002) Present status prospect of crop production technology to improve the crop quality and functionality, Korean J. Crop Sci. 47(S), 1-14
  2. Choi, H.C. (2002) Current status and perspectives in varietal improvement of rice cultivars for high-quality and value-added products, Korean J. Crop Sci. 47(S), 15-32
  3. Ju, Z.Y., Hettiarachchy, N.S., and Rath, N. (2001) Extraction, Denaturation and hydrophobic properties of rice flour proteins, J. Food Science 66(2), 229-232 https://doi.org/10.1111/j.1365-2621.2001.tb11322.x
  4. Juliano, B.O. (1994) Polysaccharides, proteins, and lipids of rice, In: Rice: Chemistry and Technology, St. Paul, Minn., Amer Assoc of Cereal Chemists, p. 98-141
  5. Komatsu, S., Kajiwara, H., and Hirano, H. (1993) A rice protein library: a data-file of rice proteins separated by two-dementional electrophoresis, Theor. Appl. Genet. 86, 935-942
  6. Komatsu, S., Konish, H., Shen, S., and Yang, G. (2003) Rice proteomics. A step toward functional analysis of the rice genome, Mole Cell Proteomics 2.1, 2-10 https://doi.org/10.1074/mcp.R200008-MCP200
  7. Komatsu, S., Kojima, K., Suzuki, K., Ozaki, K., and Higo, K. (2004) Rice proteome database based on two-dementional poltacrylamide gel electrophoresis: its ststus in 2003, Nucleic Acids Research 32, D389-D392
  8. Tanaka, N., Mitsui, S., Hiroya, H., Yanagi, K., and Komatsu, S. (2005) Expression and function of proteins during development of the basal region in rice seedling, Mole Cell Proteomics 4.6, 796-808 https://doi.org/10.1074/mcp.M400211-MCP200
  9. Bradford, M.M. (1976) A rapid and sensitive method for the quantitation 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
  10. Anderson, N.L., Esquer-Blasco, R., Hofmann, J.P., and Anderson, N.G., (1991) A two-dimensional gel database of rat liver proteins useful in gene regulation and drug effects studies, Electrophoresis 12(11), 907-30 https://doi.org/10.1002/elps.1150121110
  11. Shevchenko, A., Wilm, M., Vorm, O., and Mann. M. (1996) Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels, Anal. Chem. 68, 850-858 https://doi.org/10.1021/ac950914h
  12. Wang, D.X., Kalb S.R., and Cotter, R.J. (2004) Improved procedures for N-terminal sulfonation of peptides for matrix-assisted laser desorption/ ionization post-source decay peptide sequencing, Rapid Commun. Mass Spectrom. 18, 96-102 https://doi.org/10.1002/rcm.1289
  13. http://prowl.rockefeller.edu/prowl/-pepfrag.html
  14. Yamada, C., Izumi, H., Hirano, J., Mizukuchi, A., Kise, M., Matsuda T., and Kato. Y. (2005) Degradation of soluble proteins including some allergens in brown rice grains by endogenous proteolytic activity during germination and heat-processing, Biosci. Biotechnol. Biochem. 69, 1877-1883 https://doi.org/10.1271/bbb.69.1877

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