Microbiology and Biotechnology Letters (한국미생물·생명공학회지)

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Moce of Action of the Purified Cell Wall Lytic Enzyme from Bacillus sp.

Bacillus sp.로부터 분리 정제한 Cell Wall 분해효소의 반응특성

  • 김태호 (경북대학교 자연과학대학 미생물학과) ;
  • 신우창 (경북대학교 자연과학대학 미생물학과) ;
  • 이동선 (경북대학교 자연과학대학 미생물학과) ;
  • 홍순덕 (경북대학교 자연과학대학 미생물학과)
  • Published : 1995.12.01
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Abstract

An extracellular enzyme showing lytic activity on E. coli peptidoglycan had been isolated from Bacillus sp. BL-29. The lytic enzyme was purified to homogeneity by ion-exchange chromatography and gel filtration, with a recovery of 5%. The enzyme was monomeric and had an estimated molecular weight of 31,000 Da. The mode of action of the purified enzyme was also investigated. When the purified lytic enzyme was incubated with cell wall peptidoglycan, N-terminal amino groups were released without the release of reducing groups. The N-terminal amino acid released was identified as dinitrophenylalanine (DNP-alanine) by analysis of terminal amino acid by dinitrophenylation method. This result suggests that the lytic enzyme should be a kind of N-acetylmura-myl-L-alanine amidase.

Keywords

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