Microbiology and Biotechnology Letters (한국미생물·생명공학회지)

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Purification and Characterization of a Pectate Lyase from Bacillus sp. HSA-925

Bacillus sp. HSA-925 Pectate Lyase의 정체 및 특성

  • 박성희 (경북대학교 자연과학대학 미생물학과) ;
  • 김태호 (경북대학교 자연과학대학 미생물학과) ;
  • 김종국 (경북대학교 자연과학대학 미생물학과) ;
  • 홍순덕 (경북대학교 자연과학대학 미생물학과)
  • Published : 1994.02.01
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Abstract

Purification and characterization of pectate lyase from Bacillus sp HSA-925. Bacillus sp. HSA-925 isolated from soil produced constitutively an extracellular pectate lyase when cultivated in LB broth. The pectate lyase(EC 4.2.2.2) was purified from the cuylture broth by preciptation with ammonium sulfate, followed by column chromatography on CM-cellulose C-50 and repeated gel filtration on Sephadex G-75G. The enzyme had a molecular weight of 32-33 kDa. The activity was mazimum at pH 9.5 AND 45$\CIRC $C. The enzume activity was stable at 55$\circ $C for 15 min and between pH7-12. The activation energy, Km and V$_{max}$ for the pectate lyase were 5.8779 kcal/mol, 6.33$\times $10$^{-2}$ mol/ml and 2.09$\times $10$^{2}$ $\mu $mol/min respectively. The enzyme was activated by Ca$^{2+}$, Cu$^{2+}$ and inhibited by Li$^{+}$, Hg$^{2+}$, EDTA.

Keywords

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