Food Science and Biotechnology

  • 제18권2호
  • /
  • Pages.488-493
  • /
  • 2009
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  • 1226-7708(pISSN)
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  • 2092-6456(eISSN)
한국식품과학회 (Korean Society of Food Science and Technology)
권호 표지

Characteristics of a Black Soybean (Glycine max L. Merrill) Protein Isolate Partially Hydrolyzed by Alcalase

  • Yoon, Ji-Ho (Department of Bioscience and Biotechnology, Konkuk University) ;
  • Jung, Dong-Chae (Department of Bioscience and Biotechnology, Konkuk University) ;
  • Lee, Eun-Hye (Department of Bioscience and Biotechnology, Konkuk University) ;
  • Kang, Yoon-Seok (Department of Bioscience and Biotechnology, Konkuk University) ;
  • Lee, Sung-Yong (Department of Bioscience and Biotechnology, Konkuk University) ;
  • Park, Sae-Rom (Department of Bioscience and Biotechnology, Konkuk University) ;
  • Yeom, Hye-Jung (Department of Bioscience and Biotechnology, Konkuk University) ;
  • Ha, Mi-Sun (Department of Bioscience and Biotechnology, Konkuk University) ;
  • Park, Sang-Kyu (Department of Bioscience and Biotechnology, Konkuk University) ;
  • Lee, Yu-Si (Department of Food Science & Technology, Chung-Ang University) ;
  • Ha, Sang-Do (Department of Food Science & Technology, Chung-Ang University) ;
  • Kim, Gun-Hee (Plant Resources Research Institute, Duksung Women's University) ;
  • Bae, Dong-Ho (Department of Bioscience and Biotechnology, Konkuk University)
  • 발행 : 2009.04.30
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초록

A protein isolate was prepared from black soybean (Glycine max L. Merrill) that possessed higher antioxidant activity than ordinary white soy protein isolates. The isolate was partially hydrolyzed by alcalase to reduce the allergenicity of black soybean. Alcalase remarkably reduced the molecular mass of the major soybean allergens that have molecular weights of 53, 38, and 24 kDa. Hydrolytic breakdown occurred more effectively in Gly m Bd 30K than in Gly m Bd 60K or Gly m Bd 28K. Alcalase hydrolysis increased the solubility and hydrophobicity of the black soybean protein isolate. The foaming activity and stability of black soybean proteins were highly increased by the partial hydrolysis.

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참고문헌

  1. Koide T, Hashimoto Y, Kamei H, Kojima T, Hasegawa M, Terabe K. Antitumor effect of anthocyanin fractions extracted from red soybean and red beans in vitro and in vivo. Cancer Biother. Radio. 12: 277-280 (1997)
  2. Wang H, Cao G, Prior RL. Oxygen radical absorbing capacity of anthocyanins. J. Agr. Food Chem. 45: 304-309 (1997) https://doi.org/10.1021/jf960421t
  3. Holt S. Soya: The health food of the next millennium. Korea Soybean Digest 14: 77-90 (1997)
  4. Lee JH, Baek IY, Kang NS, Ko JM, Han WY, Kim HT, Oh KW, Suh DY, Ha TJ, Park KH. Isolation and characterization of phytochemical constituents from soybean (Glycine max L. Merr.). Food Sci. Biotechnol. 15: 392-398 (2006)
  5. Kim JH, Yoshiki Y, Okubo K. Relationships among various types in saponins content of soybean seeds. Korea Soybean Digest 11: 55-61 (1994)
  6. Oakenfull D. Saponins in food. Food Chem. 7: 19-40 (1981) https://doi.org/10.1016/0308-8146(81)90019-4
  7. Kim YH. Biological activities of soyasaponins and their genetic and environmental variations in soybean. Korean J. Crop Sci. 48: 49-57 (2003)
  8. Pool-Zobel BL, Bub A, Schroder N, Rechrmmer G. Anthocyanins are potent antioxidants in model systems but do not reduce endogenous oxidative DNA damage in human colon cells. Eur. J. Nutr. 38: 227-234 (1999) https://doi.org/10.1007/s003940050065
  9. Kim SL, Kim HB, Chi HY, Park NK, Son JR, Yun, HT, Kim SJ. Variation of anthocyanins and isoflavones between yellowcotyledon and green-cotyledon seeds of black soybean. Food Sci. Biotechnol. 14: 778-782 (2005)
  10. Goldbohm AR, Hertog MGL, Brants HAM, van Poppel G, van den Brandt PA. Intake of flavonoids and cancer risk: A prospective cohort study. p. 166. In: Polyphenols in Food. COST 916 Bioactive Plant Cell Wall Components in Nutrition and Health. Official Publications of the European Communities, Rue Mercier, Luxembourg (1998)
  11. Penas E, Prestamo G, Polo F, Gomez R. Enzymatic proteolysis, under high pressure of soybean whey: Analysis of peptides and the allergen Gly m 1 in the hydrolysates. Food Chem. 99: 569-573 (2006) https://doi.org/10.1016/j.foodchem.2005.08.028
  12. Ogawa T, Bando N, Tsuji H, Nishikawa K, Kitamura K. $\alpha$-Subunit of $\beta$-conglycinin, an allergenic protein recognized by IgE antibodies of soybean-sensitive patients with atopic dermatitis. Biosci. Biotech. Bioch. 59: 831-833 (1995) https://doi.org/10.1271/bbb.59.831
  13. Samoto M, Fukuda Y, Takahashi K, Tabuchi K, Hiemori M, Tsuji H, Ogawa T, Kawamura Y. Substantially complete removal of three major allergenic soybean proteins (Gly m Bd 30K, Gly m Bd 28K, and the α-subunit of conglycinin) from soy protein by using mutant soybean, tohoku 124. Biosci. Biotech. Bioch. 61: 2148-2150 (1997) https://doi.org/10.1271/bbb.61.2148
  14. AOAC. Official Method of Analysis of AOAC Intl. 17th ed. Method 979.09. Association of official Analytical Communities, Gaithersburg, MA, USA (2000)
  15. Yamashita M, Arai S, Matsuyama J, Gonda M, Kato H, Fujimaki M. Enzyme modification of proteins in foodstuffs. Part 2. Phenomenal survey on $\alpha$-chymotryptic plastein synthesis from peptic hydrolyzate of soy protein. Agr. Biol. Chem. 34: 1484-1491 (1970) https://doi.org/10.1271/bbb1961.34.1484
  16. Kim SY, Peter SW, Rhee K. Functional properties of proteolytic enzyme modified soy protein isolate. J. Agr. Food Chem. 38: 651-656 (1990) https://doi.org/10.1021/jf00093a014
  17. Lee IH, Hung YH, Chou CC. Total phenolic and anthocyanin contents, as well as antioxidant activity, of black bean koji fermented by Aspergillus awamori under different culture condition. Food Chem. 104: 936-942 (2007) https://doi.org/10.1016/j.foodchem.2006.12.049
  18. Achouri A, Wang Z. Effect of succinylation on the physicochemical properties of soy protein hydrolysate. Food Res. Int. 34: 507-714 (2001) https://doi.org/10.1016/S0963-9969(01)00063-1
  19. Bera MB, Mukherjee RK. Solubility, emulsifying, and foaming properties of rice bran protein concentrates. J. Food Sci. 54: 142-145 (1989) https://doi.org/10.1111/j.1365-2621.1989.tb08587.x
  20. Kato A, Takahashi A, Matsudomi N, Kobayashi K. Determination of foaming properties of proteins by conductivity measurement. J. Food Sci. 48: 62-65 (1983) https://doi.org/10.1111/j.1365-2621.1983.tb14788.x
  21. Pearce KN, Kinsella JE. Emulsifying properties of proteins:Evaluation of a turbidimetric technique. J. Agr. Food Chem. 26:716-723 (1979)
  22. Ogawa T, Samoto M, Takahashi K. Soybean allergens and hypoallergenic soybean products. J. Nutr. Sci. Vitaminol. 46: 271-279 (2000) https://doi.org/10.3177/jnsv.46.271
  23. Damodaran S, Paraf A. Food Proteins and Their Applications. Marcel Dekker, New York, NY, USA. p. 413 (1997)
  24. Richardson T, Hyslop DB. Enzymes. pp. 371-476. In: Food Chem. Fennema OR (ed). Marcel Dekker, New York, NY, USA (1985)
  25. Lee JO, Lee SI, Cho SH, Oh CK, Ryu CH. A new technique to produce hypoallergenic soybean proteins using three different fermenting microorganism. J. Allergy Clin. Immunol. 113: S239 (2004)
  26. Kato A, Komatsu K, Fujimoto K, Kobayashi K. Relationship between surface functional properties and flexibility of proteins detected by the protease susceptibility. J. Agr. Food Chem. 33: 931-934 (1985) https://doi.org/10.1021/jf00065a039
  27. Kitabatake N, Doi E. Surface tension and foamability of protein and surfactant solutions. J. Food Sci. 53: 1542-1569 (1998) https://doi.org/10.1111/j.1365-2621.1988.tb09319.x
  28. Manev ED, Sazdanova SV, Wasan DT. Emulsion and foam stability:The effect of film size and film drainage. J. Colloid Interf. Sci. 97:591-594 (1984) https://doi.org/10.1016/0021-9797(84)90334-5
  29. Marmur A. The effect of gravity on thin fluid films. J. Colloid Interf. Sci. 100: 407-413 (1984) https://doi.org/10.1016/0021-9797(84)90446-6