Modification of Oxidation Wool Treated with Protease(Part I)-Changes of chemical properties

산화양모의 효소처리에 의한 양모섬유의 개질(제1보)-화학적 성질의 변화-

  • 김영리 (서울대학교 생활과학대학 의류학과) ;
  • 유효선 (서울대학교 생활과학대학 의류학과)
  • Published : 1998.09.01

Abstract

The purpose of this study is the investigation of chemical properties of wool treated with oxidants and protease at low temperature. The chemical degradation of the fibers were investigated by measuring $\alpha$-amimo acid contents and FT-IR analysis. In addition, urea-hydrogensulfite solubility was measured to compare to the oxidation and protease treated wool. The results were as follows. 1) By the oxidation of wool, cystine is oxidised to cysteic acid by way of the intermediate oxides, cystine-S-monooxide and cystine-S-dioxide, in the case hydrolysis catalysed by the protease catalyse. Also, $\alpha$-amimo acid contents is increased, and urea-hydrogensulfite solubility was lower than that of untreated wool. This chemical degradation of wool was occurred due to oxidate hydrolysis in the order of permonosulfate>dichloroisocyanuric acid$\geq$chlorine. 2) The chemical degradation of wool was accelerated by the protease treatment of oxidized wool. Oxidation of wool is considered to make the fiber more susceptibled to enzymatic attact by opening disulphide bond within wool. Enzymatic attact was effectively directed to the wool oxidised by permonosulfate.

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