양모-케라틴 유도체 막의 제조 및 그에 대한 메틸오렌지와 그 동족체와의 염색성

Preparation of Wool-Keratin Membrane and Its Dyeability on Methyl Orange and Its Homologs

  • 김공주 (전북대학교 공과대학 섬유공학과) ;
  • 최창남 (전남대학교 공과대학 섬유공학과) ;
  • 진성룡 (전남대학교 공과대학 섬유공학과) ;
  • 이강영 (전남대학교 공과대학 섬유공학과) ;
  • 김영주 (한양여자전문대학 의류과) ;
  • 강영희 (순천대학 가정교육과) ;
  • 김애순 (군산대학 가정학과)
  • 발행 : 1992.10.01

초록

In order to study the dyeability of wool, S-cyano ethylated wool-keratine(SCEK) as a model compound of wool was prepared from the reaction of reduced Merino wool fiber and acrylonitrile. It was found that the cyano etylation modified the $\alpha$-helix structure of microfibril. The binding ability of acid dyes (methyl orange and its homologs) to SCEK and the permeation properties of SCEK membrane were investigated. The first binding constants and the thermodynamic parameters in the course of binding were calculated from the binding experiments with methyl orange in the temperature range of 30-50 ˚C. The free energy change was accompanied by exothermic enthalpy change and entropy gain. These characteristics of thermodynamic parameters suggest that hydrophobic interaction plays a role in the binding of SCEK. The binding ability of ethyl orange and butyl orange showed a cooperative binding phenomena, especially in concentrated solutions. In relation to hydrophobic interaction, the effects of urea were examined. The amounts of bound dye were decreased with the addition of urea in solution. For wool, the bound dye was stacked at concentrated solutions. The permeation coefficients of SCEK membrane were in the order of 10 9 - 10 8 mol/min. in the temperature range of 30~50˚C. The smaller the size of dye molecules, the better the permeability of SCEK membrane was.

키워드

참고문헌

  1. Wool-Nature's Wonder Fiber J.D.Leeder
  2. Wool Science J.A.Maclaren;B.Milligan
  3. Sen-I Gakkaishi v.44 no.3 J.Koga;T.Hikishen;N.Kuroki;K.Joko
  4. J. Korean Soc. Text. Eng. Chem. v.25 no.3 Y.J.Kim;J.Koga;M.Aki;J.W.Kim
  5. 한국섬유공학회지 v.22 no.6 김공주;노중열;가영의;김애순
  6. J. Am. Chem. Soc. v.68 I.M.Klotz;F.M.Walker;R.B.Pivan
  7. A Laboratory Manual of Analytical Methods of Protein Chem. (Including Peptides) v.2 R.M.Rosenberg;I.M.Klotz
  8. J. Chem. Phys. v.13 H.P.Frank;H.E.Evans
  9. J. Am. Chem. Soc. v.79 H.P.Frank;S.Barkin;F.R.Eirich
  10. Advances in Protein Chem. v.14 W.Kauzmann
  11. J. Chem. Phys. v.36 no.12 H.A.Scheraga;G.Nemethy
  12. J. Polym. Sci.: Polym. Chem. Ed. v.11 T.Takagishi;N.Kuroki
  13. J. Polym. Sci.: Polym. Chem. Ed. v.14 T.Takagishi;K.Nakagami;K.Imajo;N.Kuroki
  14. J. Polym. Sci.: Polym. Chem. Ed. v.15 T.Takagishi;K.Imajo;K.Nakagami;N.Kuroki
  15. Biopolymers v.11 T.Takagishi;I.M.Klotz
  16. J. Polym. Sci.: Polym. Chem. Ed. v.20 T.Takagishi;A.Hayashi;N.Kuroki
  17. J. Polym. Sci.: Polym. Chem. Ed. v.21 T.Takagishi;T.Sugimoto;A.Hayashi;N.Kuroki
  18. J. Polym. Sci.: Polym. Chem. Ed. v.20 T.Takagishi;H.Kozuka;G.J.Kim;N.Kuroki
  19. J. Polym. Sci.: Polym. Chem. Ed. v.19 T.Takagishi;H.Kozuka;N.Kuroki
  20. J. Polym. Sci.: Polym. Chem. Ed. v.21 T.Takagishi;H.Kozuka;N.Kuroki
  21. J. Am. Chem. Soc. v.74 I.M.Klotz;R.K.Burkhard;J.M.Urquhart
  22. 한양대 대학원 박사학위논문 양모섬유의 미세구조와 염색성 김영주
  23. Introduction to Spectroscopy D.L.Pavia;G.M.Lampman;G.S.Kriz,Jr.
  24. Text. Res. J. v.37 A.R.Haly;J.W.Snaith
  25. Colloid Polym. Sci. v.261 M.Spei;H.Thomas
  26. J. Polym. Sci.: Polym. Letter Ed. v.22 K.Ishihara;I.Shinohara