Purification and Evaluation of Rice Bran Hydrolysates with Antimutagenicity

  • Heo, Seok (Department of Applied Biology and Chemistry, Konkuk University) ;
  • Hettiarachy, Navam (Department of Food Science, University of Arkansas) ;
  • Park, Jong-Seok (Department of Food Science and Technology, Dongguk University) ;
  • Kim, Hyung-Il (Department of Food Science and Technology, Dongguk University) ;
  • Paik, Hyun-Dong (Department of Food Science and Biotechnoogy of Animal Resources, Konkuk University) ;
  • Yun, Mi-Suk (Department of Applied Biology and Chemistry, Konkuk University) ;
  • Lee, Si-Kyung (Department of Applied Biology and Chemistry, Konkuk University)
  • 발행 : 2007.04.30

초록

A 3% suspension of heat-stabilized defatted rice bran was treated with papain, followed by inactivating the enzyme by heat, and centrifuged. The supernatant was subjected to ultrafiltration, and fractions with various molecular sizes, F1 (>30 kDa), F2 (10-30 kDa), F3 (5-10 kDa), F4 (3-5 kDa), and F5 (3 kDa<), were freeze-dried, and evaluated for antimutagenicity by Ames test using Salmonella typhimurium TA 100 against phenazine methosulfate. The F3 fraction containing highest antimutagenicity from ultrafiltration was separated into 6 fractions by DEAE-Sephadex A-25 ion-exchange column chromatography (F3-1-F3-6). Each fractions having protein contents were pooled, dialyzed, freeze dried, and evaluated for antimutagenicity. Among the six fractions, the F3-1, F3-2, and F3-6 fractions showed antimutagenicity, which were 80.2, 53.4, and 58.6% at concentration of $100\;{\mu}g/plate$, respectively. These F3-1, F3-2, and F3-6 fractions were subjected to Sephadex G-50 gel filtration column chromatography for further purification. Among the purified fractions, the F3-1-1, F3-2-2, and F3-6-1 fractions showed antimutagenicity of 84.5, 58.6, and 69.8% at concentration of $100\;{\mu}g/plate$, respectively. It is thought that these peptides can find application for nutraceutical and pharmaceutical products.

키워드

참고문헌

  1. Agricultural Statistics Board. Crop production 2005 Summary. Available from: http://usda.mannlib.comell.edu/reports/nassr/field/ pcp-bban/cropan06.pdf. Accessed Apr. 10, 2006
  2. Saunders RM. The properties of rice bran as a food stuff. Cereal Food World 35: 632-662 (1990)
  3. Choi EM, Kim AJ, Hwang JK. Enhanced immune cell functions and cytokine production after in vitro stimulation with arabinoxylans fraction from rice bran. Food Sci. Biotechnol. 14: 479-486 (2005)
  4. Lee SK, Jang IS, Kim KM, Park SK, Lee WY, Youn KS, Bae DH. Changes in functional properties of rice bran and sesame meal proteins through chemical modifications. Food Sci. Biotechnol. 13: 555-560 (2004)
  5. Yokoyama WH. Nutritional properties of rice and rice bran. pp. 595-609. In: Rice Chemistry and Technology. Champagne ET (ed). American Association of Cereal Chemists, St. Paul, MN, USA (2004)
  6. Prakash J. Rice bran proteins: properties and food uses. Crit. Rev. Food Sci. 36: 537-552 (1996) https://doi.org/10.1080/10408399609527738
  7. Helm RM, Burks AW. Hypoallergenicity of rice bran protein. Cereal Food World 41: 839-843 (1996)
  8. Waldron KW, Johnson IT, Fenwick GR. Food and Cancer Prevention: Chemical and Biological Aspects. Royal Society of Chemistry, Cambridge, UK. pp. 331-401 (1993)
  9. Tang S. Optimization of protein extraction system and protein functionalities for heat-stabilized defatted rice bran. PhD thesis, University of Arkansas, Fayetteville, AR, USA (2002)
  10. Vis EH, Plinck AF, Alink GM, van Boekel MS. Antimutagenicity of heat-denatured ovalbumin, before and after digestion, as compared to caseinate, BSA, and soy protein. J. Agr. Food Chem. 46: 3713-3718 (1998) https://doi.org/10.1021/jf980140g
  11. Karakaya S, Kavas A. Antimutagenic activities of some foods. J. Sci. Food Agr. 79: 237-242 (1999) https://doi.org/10.1002/(SICI)1097-0010(199902)79:2<237::AID-JSFA178>3.0.CO;2-K
  12. Lee EJ, Lee HJ, Kim JK. Antimutagenic effects on aflatoxin B1 of soybean pastes fermented by Bacillus strains. Food Sci. Biotechnol. 14: 878-880 (2005)
  13. Shin HS, Lee Y. Influence of commercial marinades on heterocyclic aromatic amine formation and overall mutagenicity in fried beef steak. Food Sci. Biotechnol. 14: 323-327 (2005)
  14. Rhee C, Park H. Three glycoproteins with antimutagenic activity identified in Lactobacillus plantarum KLAB21. Appl. Environ. Microb. 67: 3445-3449 (2001) https://doi.org/10.1128/AEM.67.8.3445-3449.2001
  15. Kurech T, Kikugawa K, Fukuda S, Hasunuma M. Inhibition of Nnitrosamine formation by soya products. Food Cosmet. Toxicol. 19: 425-428 (1981) https://doi.org/10.1016/0015-6264(81)90445-4
  16. Bogdanov IG, Dalev PG, Gurevich LA, Kolosov MN, Malkove VP, Plemyannikova LA, Sorokina IB. Anti-tumor glycopeptides from Lactobacillus bulgaricus cell wall. FEBS Lett. 57: 259-261 (1975) https://doi.org/10.1016/0014-5793(75)80312-7
  17. Abdelali H, Cassand P, Soussotte V, Koch-Bocabeille B, Narbonne F. Antimutagenicity of components of dairy products. Mutat. Res. 331: 133-141 (1995) https://doi.org/10.1016/0027-5107(95)00059-R
  18. Romero F, Espliego F, Perez BJ, de Quesada TG, Gravalos D, de la Calle F, Femadea-Puentes JL. Thiocoraline, a new depsipeptide with antitumor activity produced by a marine Micromonospora. I. Taxonomy, fermentation, isolation, and biological activities. J. Antibiot. 50: 734-737 (1997) https://doi.org/10.7164/antibiotics.50.734
  19. Kim SE, Kim HH, Kim JY, Kang YI, Woo HJ, Lee HJ. Anticancer activity of hydrophobic peptides from soy proteins. Biofactors 12: 151-155 (2000) https://doi.org/10.1002/biof.5520120124
  20. Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of proteindye binding. Anal. Biochem. 72: 248-254 (1976) https://doi.org/10.1016/0003-2697(76)90527-3
  21. Ames BN, McCann J, Yamasaki E. Methods for detecting carcinogens and mutagens with the Salmonella/mammalian-microsome mutagenicity test. Mutat. Res. 31: 347-364 (1975) https://doi.org/10.1016/0165-1161(75)90046-1
  22. SAS Institute, Inc. SAS/STAT Software. Release 8.2. Statistical Analysis Systems Institute, Cary, NC, USA (2001)
  23. Hosono A, Wardojo R, Otani H. Inhibitory effects of lactic acid bacteria from fermented milk on the mutagenicities of volatile nitrosamines. Agr. Biol. Chem. Tokyo 54: 1639-1643 (1990) https://doi.org/10.1271/bbb1961.54.1639
  24. Nishioka K, Miyamoto T, Kataoka K, Nakae T. Preliminary studies on antimutagenic activities of lactic acid bacteria. Jpn, J. Zootech. Sci. 60: 491-494 (1989)
  25. van Boekel MS, Weerens CM, Holstra A, Scheidtweiler CE, Alink GM. Antimutagenic effects of casein and its digestion products. Food Chem. Toxicol. 31: 731-737 (1993) https://doi.org/10.1016/0278-6915(93)90144-N
  26. Matar C, Nadathur SS, Bakalinsky AT, Goulet J. Antimutagenic effects of milk fermented by Lactobacillus helveticus L89 and a protease-deficient derivative. J. Dairy Sci. 80: 1965-1970 (1997) https://doi.org/10.3168/jds.S0022-0302(97)76139-3
  27. Berg HE, van Boekel MS, Jongen WF. Heating milk: a study on mutagenicity. J. Food Sci. 55: 1000-1003 (1990) https://doi.org/10.1111/j.1365-2621.1990.tb01583.x