Food Science and Biotechnology

Korean Society of Food Science and Technology (한국식품과학회)
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Effect of Gamma Irradiation on the Structural and Physiological Properties of Silk Fibroin

  • Sung, Nak-Yun (Team for Radiation Food Science & Biotechnology, Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute) ;
  • Byun, Eui-Baek (Team for Radiation Food Science & Biotechnology, Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute) ;
  • Kwon, Sun-Kyu (Team for Radiation Food Science & Biotechnology, Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute) ;
  • Kim, Jae-Hun (Team for Radiation Food Science & Biotechnology, Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute) ;
  • Song, Beom-Seok (Team for Radiation Food Science & Biotechnology, Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute) ;
  • Choi, Jong-Il (Team for Radiation Food Science & Biotechnology, Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute) ;
  • Kim, Jin-Kyu (Team for Radiation Food Science & Biotechnology, Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute) ;
  • Yoon, Yo-Han (Team for Radiation Food Science & Biotechnology, Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute) ;
  • Byun, Myung-Woo (Team for Radiation Food Science & Biotechnology, Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute) ;
  • Kim, Mee-Ree (Department of Food and Nutrition, Chungnam National University) ;
  • Yoo, Hong-Sun (Department of Food and Nutrition, Chungnam National University) ;
  • Lee, Ju-Woon (Team for Radiation Food Science & Biotechnology, Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute)
  • Published : 2009.02.28
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Abstract

This study was conducted to examine the changes in the molecular structure and physiological activities of silk fibroin by gamma irradiation. The results of gel permeation chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that the molecular weight of fibroin was increased depending upon the irradiation dose. Secondary structure of fibroin determined by using circular dichroism revealed that the ratio of $\alpha$-helix was increased up to 10 kGy and then decreased depending upon the irradiation dose. Whereas, the ratio of $\beta$-sheet, $\beta$-turn, and random coil were decreased and then increased with an alteration in the $\alpha$-helix secondary conformation. The 2.2-diphenyl-1-picryl-hydrazil (DPPH) radical scavenging activity of fibroin was increased by gamma irradiation at 5 kGy, but was decreased above 10 kGy depending upon the irradiation dose. Also, the inhibition activities of tyrosinase and melanin synthesis of fibroin were increased by gamma irradiation. These results indicated that gamma irradiation could be used as an efficient method to make fibroin more suitable for the development of functional foods and cosmetics.

Keywords

References

  1. Kaplan DL, Mello SM, Arcidiacono S, Fossey S, Senecal K, Muller W. Silk. pp. 103-131. In: Protein Based Materials. McGrath K, Kaplan DL (eds). Birkhauser, Boston, MA, USA (1998)
  2. Masahiro S, Hideyuki Y, Norihisa K. Consumption of silk protein, sericin elevates intestinal absorption of zinc, iron, magnesium, and calcium in rats. Nutr. Res. 20: 1505-1511 (2000) https://doi.org/10.1016/S0271-5317(00)80031-7
  3. Minoura N, Tsukada M, Nagura M. Physico-chemical properties of silk fibroin membrane as a biomaterial. Biomaterials 11: 430-434 (1990) https://doi.org/10.1016/0142-9612(90)90100-5
  4. Minoura N, Aiba SI, Higuchi M, Gotoh Y, Tsukada M, Imai Y. Attachment and growth of fibroblast cells on silk fibroin. Biochem. Bioph. Res. Co. 208: 511-516 (1995) https://doi.org/10.1006/bbrc.1995.1368
  5. Qian J, Liu Y, Liu H, Yu T, Deng J. Immobilization of horseradish peroxidase with a regenerated silk fibroin membrane and its application to a tetrathiafulvalene-mediating $H_2O_2$ sensor. Biosens. Bioelectron. 12: 1213-1218 (1997) https://doi.org/10.1016/S0956-5663(97)00056-0
  6. Hanawa T, Watanabe A, Tsuchiya T, Ikoma R, Hidaka M, Sugihara M. New oral dosage form for elderly patients: Preparation and characterization of silk fibroin gel. Chem. Pharm. Bull. 42: 282-288 (1995)
  7. Akai H. New physiological function of silk material. Up-to-date Foodprocess 34: 45-47 (1999)
  8. Gotoh K, Izumi H, Kanamoto T, Tamada Y, Nakashima H. Sulfated fibroin, a novel sulfated peptide derived from silk, inhibits human immunodeficiency virus replication in vitro. Biosci. Biotech. Bioch. 64: 1664-1670 (2000) https://doi.org/10.1271/bbb.64.1664
  9. Kim MK, Lee KH, Lim HJ, Lee SJ, Lee SH, Min KS. Preparation protocols for the functional polypeptide materials from cocoon. Korean patent 98712 (1996)
  10. Byun MW. Application of irradiation techniques to food industry. Radioisotope News 9: 32-37 (1994)
  11. Lee SL, Lee MS, Song KB. Effect of gamma-irradiation on the physicochemical properties of gluten films. Food Chem. 92: 621-625 (2005) https://doi.org/10.1016/j.foodchem.2004.08.023
  12. Hidefumi T, Kazushige I, Youichi K, Fumio Y, Tamikazu K. Production of fine powder from silk by radiation. Macromol. Mater. Eng. 283: 126-131 (2000) https://doi.org/10.1002/1439-2054(20001101)283:1<126::AID-MAME126>3.0.CO;2-#
  13. Masuhiro T, Guiliano F, Norihiko M. Changes in the fine structure of silk fibroin fibers following gamma irradiation. J. Appl. Polym. Sci. 51: 823-829 (2003) https://doi.org/10.1002/app.1994.070510505
  14. Oguz B, Ozge M, Yarkm O, Aysegul B. Silk fibroin as a novel coating material for controlled release of theophylline. Eur. J. Pharm. Biopharm. 60: 373-381 (2005) https://doi.org/10.1016/j.ejpb.2005.02.002
  15. Krieg RC, Van D, Schwamborn K, Knuechel R. Protein quantification and its tolerance for different interfering reagents using the BCA-method with regard to 2D SDS-PAGE. J. Biochem. Bioph. Meth 65: 13-19 (2005) https://doi.org/10.1016/j.jbbm.2005.08.005
  16. Amarowicz R, Pegg RB, Rahimi-Moghaddam P, Barl B, Weil JA. Free-radical scavenging capacity and antioxidant activity of selected plant species from the Canadian prairies. Food Chem. 84: 551-562 (2004) https://doi.org/10.1016/S0308-8146(03)00278-4
  17. Bilodeau ML, Greulich JD, Hullinger RL, Bertolotto C, Ballotti R, Andrisani OM. BMP-2 stimulates tyrosinase gene expression and melanogenesis in differentiated melanocytes. Pigm. Cell Res. 14:328-336 (2001) https://doi.org/10.1034/j.1600-0749.2001.140504.x
  18. Garrison WM. Reaction mechanism in the radiolysis of peptides, polypeptides, and proteins. Chem. Rev. 87: 381-398 (1987) https://doi.org/10.1021/cr00078a006
  19. Stevens CO, Sauberlich HE, Bergstrom GR. Radiation-produced aggregation and inactivation in egg white lysozyme. J. Biochem. 242: 1821-1826 (1967)
  20. Diehl JF. Chemical effects of ionizing radiation, Chap. 3, pp. 42-88. In: Safety of Irradiated Foods. Marcel Decker, New York, NY, USA (1995)
  21. Urbain WM. Food Irradiation. Academic Press, Orlando, FL, USA. pp. 83-123 (1986)
  22. Kume T, Matsuda T. Change in the structural and antigenic properties of proteins by radiation. Radiat. Phys. Chem. 46: 225-231 (1995) https://doi.org/10.1016/0969-806X(95)00017-R
  23. Masuda T, Koseki SY, Yasumoto K, Kitabatake N. Characterization of anti-irradiation-denatured ovalbumin monoclonal antibodies. Immunochemical and structural analysis of irradiation-denatured ovalbumin. J. Agr. Food Chem. 48: 2670-2674 (2000) https://doi.org/10.1021/jf990999d
  24. Lee JW, Kim JH, Yook HS, Kang GO, Lee SY, Hwang HJ, Byun MW. Effects of gamma radiation on the allergenic and antigenic properties of milk proteins. J. Food Protect. 64: 272-276 (2001) https://doi.org/10.4315/0362-028X-64.2.272
  25. Davies KJ. Protein damage and degradation by oxygen radicals: I. General aspects. J. BioI. Chem. 262: 9895-9901 (1987)
  26. Chang CT, Wu SC, Venaminov SY, Yang JT. Circular dichroism analysis of protein conformation: Inclusion of $\beta$-turn. Anal. Biochem. 91: 13-31 (1978) https://doi.org/10.1016/0003-2697(78)90812-6
  27. Mayer L. Current concepts in mucosal immunity. I. Antigen presentation in the intestine: New rules and regulations. J. Phycol. 274: 77-92 (1998)
  28. Cho Y, Song KB. Effect of chaotropic salt on the secondary structure of pig skin gelatin. Biosci. Biotech. Bioch. 61: 1194-1195 (1997) https://doi.org/10.1271/bbb.61.1194
  29. Moon S, Song KB. Effect of $\gamma$-irradiation on the molecular properties of ovalbumin and ovomucoid and protection by ascorbic acid. Food Chem. 74: 479-483 (2001) https://doi.org/10.1016/S0308-8146(01)00166-2
  30. Gaber MH. Effect of gamma irradiation on the molecular properties of bovine serum albumin. J. Biosci. Bioeng. 100: 203-206 (2005) https://doi.org/10.1263/jbb.100.203
  31. Lee S, Lee S, Song KB. Effect of gamma-irradiation on the physicochemical properties of porcine and bovine blood plasma proteins. Food Chem. 82: 521-526 (2003) https://doi.org/10.1016/S0308-8146(02)00592-7
  32. Choi JH, Kim DI, Park SH, kim JM, Lee JS, Lee KG, Yeo JH, Lee YW. Effects of silk fibroin on oxidative stress and membrane fluidity in brain of SD rats. Korean J. Life Sci. 10: 511-518 (2000)
  33. Yeo JH, Lee KG, Kweon HY, Woo SO, Han SM, Kim SS, Demura M. Fractionation of a silk fibroin hydrolysate and its protective function of hydrogen peroxide toxicity. J. Appl. Polym. Sci. 102:772-776 (2006) https://doi.org/10.1002/app.23740
  34. Jo C, Son JH, Lee HJ, Byun MW. Irradiation application of color removal and purification of green tea leave extract. Radiat. Phys. Chem. 66: 179-184 (2003) https://doi.org/10.1016/S0969-806X(02)00273-6
  35. Ahn HJ, Kim JH, Yook HS, Byun MW. Irradiation effects on free radical-scavenging and antioxidant activity of phytic acid. J. Food Sci. 68: 2221-2224 (2003) https://doi.org/10.1111/j.1365-2621.2003.tb05750.x
  36. Variyar PS, Limaye A, Sharma A. Radiation-induced enhancement of antioxidant contents of soybean (Glycine max Merrill). J. Agr. Food Chem. 52: 3385-3388 (2004) https://doi.org/10.1021/jf030793j
  37. Dooley TP. Topical skin depigmentation agents: Current products and discovery of novel inhibitors of melanogenesis. J. Dermatol. Treat. 8: 275-279 (1997) https://doi.org/10.3109/09546639709160535
  38. Huang KF, Chen YW, Chang CT, Chou ST. Studies on the inhibitory effect of Graptopetalum paraguayense E. Walther extracts on mushroom tyrosinase. Food Chem. 89: 583-587 (2005) https://doi.org/10.1016/j.foodchem.2004.03.022
  39. Synge RLM. Interaction of polyphenols with proteins in plants and plant products. Plant Food Hum. Nutr. 24: 337-340 (1975) https://doi.org/10.1007/BF01092220
  40. Katz LL. Inorganic Biochemistry. Elservier-Scientific Publishing Co., Amsterdam, Netherland. pp. 1210-1243 (1973)
  41. Viola RE, Hartzell CR, Villafranca JJ. Copper (II) complexes of carnosine, glycylglycine, and glycylglycine-imidazole mixture. J. Inorg. Biochem. 10: 293-307 (1979) https://doi.org/10.1016/S0162-0134(00)80196-8
  42. Kang GD, Lee KH, Shin BS, Nahm JH. Preparation and characterization of low molecular weight silk fibroin by hightemperature and high-pressure method. J. Appl. Polym. Sci. 85:233 2890-2895 (2002) https://doi.org/10.1002/app.10796
  43. Kato F, Wada I, Jimbow K. Interaction of calnexin and calreticulin is required for acid-resistant structure and correct processing of tyrosinase-related protein from ER to melanosomes. J. Dermatol. Sci. 16: S96 (1998) https://doi.org/10.1016/S0923-1811(98)83573-1