해양에서 분리한 Bacillus subtilis SH-1이 분비하는 용균효소의 정제 및 특성

  • 진성현 (부산광역시 보건환경연구원) ;
  • 정영기 (동의대학교 미생물학과) ;
  • 류병호 (경성대학교 식품공학과)
  • Published : 1996.04.01

Abstract

The bacteriolytic enzyme produced from Bacillus subtilis SH-1 was purified and characterized, and its molecular weight was determined. The bacteriolytic enzyme activity was increased about 66.5 times via purification with recovery yield of 18.5%. The optimum pH and temperature of this enzyme were 9.0 and 50$\circ$C. The enzyme was stable within a pH range of 6.0-10.0 and unstable above 60 . The molecular weight of the enzyme was estimated to be 23,000 dalton in a form of monomer with no other subunits. Effect of the enzyme on the lysis of bacteria engaged in food posion was tested. The lysis degree was below 31% against Gram negative bacteria and above 48% in Gram positive bacteria. The values higher than 73% were obtained against Vibrio sp. and Listeria sp. As the turbidity of dissolved peptidoglycan clecreases, the free amino group levels were increased. And, based on hydrolysis of casein, this enzyme was thought to be an endopeptidase.

Keywords

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