International Journal of Industrial Entomology and Biomaterials

Korean Society of Sericultural Science (한국잠사학회)
권호 표지

Effect of Low Molecular Weight Silk Fibroin on the Inhibition of Tyrosinase Activity

  • Kang, Gyung Don (School of Biological Resources and Materials Engineering, Seoul National University) ;
  • Lee, Ki Hoon (School of Biological Resources and Materials Engineering, Seoul National University) ;
  • Shin, Bong Seob (Department of Textile Engineerings, Sangju National University) ;
  • Nahm, Joong Hee (School of Biological Resources and Materials Engineering, Seoul National University) ;
  • Park, Young Hwan (School of Biological Resources and Materials Engineering, Seoul National University)
  • Published : 2004.09.01
Download PDF
⟨ Previous Next ⟩

Abstract

Low molecular weight silk fibroin (LMSF), which was prepared by hydrolysis of silk fibroin using high-temperature and high-pressure method, was found to inhibit the oxidation of L-3,4,-dihydroxyphenylalanine (L-DOPA) catalyzed by mushroom tyrosinase (EC 1.14.18.1). LMSF contained mostly free amino acids such as L-glycine, L-alanine, and L-serine and oligopeptides, mainly glycine-alanine dimer. As a result of analyzing the inhibition kinetics from Lineweaver-Burk plots, L-glycine and glycine-alanine dimer showed noncompetitive behavior while uncompetitive behavior was observed in L-alanine, and L-serine. When weight percent concentration of ${ID_50}$ was compared, L-glycine was most effective on the inhibition and LMSF was also good enough for the inhibition effect of tyrosinase activity. LMSF showed a mixed-type inhibition and the inhibitory mechanism of LMSF might be caused by free amino acids and oligopeptides. As a result of spectroscopic observation with time, initial rate of increase of DOPAchrome decreased remarkably and the time to reach maximum absorbance increased as an increase of the concentration of L-glycine, meaning that L-glycine made itself mainly responsible for the formation of chelate with ${Cu^2+}$ in tyrosinase. However, in case of L-alanine, L-serine, and especially glycine-alanine dimmer, the production of DOPAchrome after an arrival at maximum absorbance decreased, indicating the production of adducts through the reaction with DOPAquinone.

Keywords

References

  1. Ben-Shalom, N., V. Kahn, E. Harel and A. M. Mayer (1977) Catechol oxidase from green olives: properties and partial purification. Phytochemistry 16, 1153-1158 https://doi.org/10.1016/S0031-9422(00)94350-4
  2. Cilliers, J. J. L. and V. L. Singleton (1990) Caffeic acid autox-idation and the effect of thiol. J. Agric. Food Chern. 33, 1789-1796
  3. Duckworth, H. W. and J. E. Coleman (1970) Physicochemical and kinetic properties of mushroom tyrosinase. J. Biol. Chern. 245, 1613-1625
  4. Eichhorn, G. L. (1973) Inorganic chemistry. Elservier-Scien-tific Publishiing Co., New York
  5. Embs, R. J. and Na P. Markakis (1965) The mechanism of sulfite inhibition of browning caused by polyphenol oxidase. J. Food Sci. 30, 753-758 https://doi.org/10.1111/j.1365-2621.1965.tb01836.x
  6. Golan-Goldhirsh, A. and J. R. Whitaker (1984) Effect of ascor-bic acid, sodium bisulfite, and thiol compounds on mush-room polyphenyl oxidase. J. Agric. Food Chern. 32, 1003-1009 https://doi.org/10.1021/jf00125a013
  7. Healey, D. F and K. G. Strothkamp (1981) Inhibition of the catecholase and cresolase activity of mushroom tyrosinase by azide. Arch. Biochem. Biophys. 211, 1573-1575
  8. Hsu, A. E, J. J. Shieh, D. D. Bills and K. White (1988) Inhibi-tion of mushroom polyphenoloxidase by ascorbic acid deriv-atives. J. Food Sci. 53, 765-771 https://doi.org/10.1111/j.1365-2621.1988.tb08951.x
  9. Janovitz-Klapp, A. H. F. C. Richard, P. M. Goupy and J. J. Nicolas (1990) Inhibition studies on apple polyphenol oxi-dase. J. Agric. Food Chern. 38, 926-931 https://doi.org/10.1021/jf00094a002
  10. Jimenez, M., S. Cazarra, J. Escribano, J. Cabanes and E Gar-cia-Carmona (2001) Competitive inhibition of mushroom tyrosinase by 4-substituted benzaldehydes. J Agric. Food Chern. 49, 4060-4063 https://doi.org/10.1021/jf010194h
  11. Kahn, V. (1985) Effect of proteins, protein hydrolyzates and amino acids on -dihydroxyphenolase activity of polyphenol oxidase of mushroom, avocado, and banana. J. Food Sci. 50, 111-115 https://doi.org/10.1111/j.1365-2621.1985.tb13288.x
  12. Kang, G. D., K H. Lee, B. S. Shin and J. H. Nahm (2002) Preparation and characterization of low molecular weight silk fibroin by high-temperature and high-pressure method. J. Appl. Polym. Sci. 85, 2890-2895 https://doi.org/10.1002/app.10796
  13. Maeda, K. and M. Fukuda (1996) Arbutin: mechanism of its depigmenting action in human melanocyte culture. J. Phar-macol. Exp. Ther. 276, 765-769
  14. Mayer, A. M. and E. Harel (1979) Polyphenol oxidases in plants. Phytochemistry 18, 193-215 https://doi.org/10.1016/0031-9422(79)80057-6
  15. Nahm, J. H. and B. S. Shin (1998): The structure and physic-ochemical properies of silk; in Silk science. Sunwoo, J. H. (ed.), pp. 84-99, SNU Press
  16. Nerya, O., J. Vaya, R. Musa, S. Izrael, R. Ben-Arie and S. Tamir (2003) Glabrene and isoliquiritigenin as tyrosinase inhibitors from licorice roots. J. Agric. Food Chern. 51, 1201-1207 https://doi.org/10.1021/jf020935u
  17. Richard-Forget, F. C., P. M. Goupy and J. J. Nicolas (1992) Cysteine as a inhibitor of enzymatic browning. 2. kinetic studies. J. Agric. Food Chern. 40, 2108-2113 https://doi.org/10.1021/jf00023a014
  18. Robert, C, C. Rouch and F. Cadet (1997) Inhibition of palmito (Acanthophoenix rubra) polyphenol oxidase by carboxylic acids. Food Chern. 59, 355-360 https://doi.org/10.1016/S0308-8146(96)00179-3
  19. Sapers, G. M. and M. A. Ziolkowski (1987) Comparison of erythobic acid and ascorbic acids as inhibitors of enzymatic browning in apple. J. Food Sci. 52, 1732-1733 https://doi.org/10.1111/j.1365-2621.1987.tb05917.x
  20. Sayavedra-Soto, L. A. and M. W. Montgomery (1986) Inhibi-tion of polyphenoloxidase by sulfite. J. Food Sci. 51, 1531-1536 https://doi.org/10.1111/j.1365-2621.1986.tb13852.x
  21. Shuler, M. L. and F. Kargi (1992) Enzymes; in Bioprocess engineering basic concepts. E Kargi (ed.), pp. 58-102, Prentice Hall PTR, New Gersey
  22. Sugimoto, K, T. Nishimura, K. Nomura, K. Sugimoto and T. Kuriki (2003) Syntheses of arbutin-glycosides and a com-parison of their inhibitory effects with those of -arbutin and arbutin on human tyrosinase. Chern. Pharm. Bull. 51, 798-801 https://doi.org/10.1248/cpb.51.798
  23. Synge, R. L. M (1975) Interaction of polyphenols with proteins in plants and plant products. Plant Foods Hum. Nutr. 24, 337-340 https://doi.org/10.1007/BF01092220
  24. Taylor, S. L. and R. K Bush (1986) Sulfites as food ingredi-ents. Food Technol. 40, 47-52
  25. Viola, R. E., C. R. Hartzell and J. J. Villafranca (1979) Cop-per(II) complexes of carnosine, glycylglycine, and glycylg-lycine-imidazole mixtures. J. Inorg. Biochem. 10, 293-307 https://doi.org/10.1016/S0162-0134(00)80196-8