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Purification and Characterization of Carboxymethyl Cellulase from Loweporus roseoalbus

Loweporus roseoalbus가 생산하는 Carboxymethyl Cellulase의 정제 및 특성

  • 장형수 (상지대학교 이공과대학 식품영양학과) ;
  • 김준호 (상지대학교 이공과대학 화학과) ;
  • 유관희 (상지대학교 이공과대학 생명과학과)
  • Published : 2005.12.30

Abstract

A carboxymethyl cellulase (CMCase) has been purified from Loweporus roseoalbus. The molecular weight of the purified CMCase was estimated to be 28.5 kDa by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. The maximum activity of the purified CMCase was observed at pH 4.0 and $30^{\circ}C$, and stable for pH 3 to 5 to maintain 60% activity. The CMCase activity was activated by SDS and inhibited by PMSF and 1,10-phenanthroline. The enzyme activity was also decreased by the addition of ethylene diamine tetraacetic acid (EDTA), suggesting that the purified CMCase is metalloenzyme.

섬유소분해능이 우수한 L. roseoalbus로부터 분리 정제한 CMCase의 활용에 대한 기초적인 자료를 제공하고자 실험하여 L. roseoalbus의 배양액으로부터 4단계를 거쳐 분자량이 28.5 kDa인 CMCase를 분리 정제하였다. 이 효소는 pH 4.0에서 최적의 활성을 보여주는 acidic CMCase로 $30^{\circ}C$에서 최대 활성을 나타냈다. EDTA에 의해 활성이 저해되는 것으로 보아 metalloenzyme으로 추정되며, PMSF에 의해 저해되는 것으로 보아 serine 잔기를 갖고 있는 효소로 판단된다. $Al_{2}(SO_{4})_{3}$$FeSO_{4}$에서는 효소활성이 높았으나 $CaCl_{2}$$Na_{2}MoO_{4}$에서는 효소 활성이 낮았다.

Keywords

References

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