Journal of Applied Biological Chemistry

The Korean Society for Applied Biological Chemistry (한국응용생명화학회)
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Characterization of extracellular protease from Pseudoxanthomonas sp. WD12 and WD32

Pseudoxanthomonas sp. WD12와 WD32의 세포외 단백질분해효소 특성

  • Cho, Woon-Dong (Department of Microbiology, Chungbuk National University) ;
  • Oh, Ji-Sung (Department of Microbiology, Chungbuk National University) ;
  • Roh, Dong-Hyun (Department of Microbiology, Chungbuk National University)
  • Received : 2016.05.23
  • Accepted : 2016.07.05
  • Published : 2016.12.31
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Abstract

Proteolytic enzymes perform hydrolysis of the peptide bonds in the protein and most commonly use in the industry. Pseudoxanthomonas sp. WD12 and WD32 were previously isolated as protease producers from a rotten wood sample. Here, we report the secreted proteolytic enzymes. The optimum enzyme reaction temperature for the secreted crude enzyme from the strain WD12 and WD32 were $50^{\circ}C$ at pH 9.0 and $45^{\circ}C$ at pH 8.0, respectively. The enzyme activities of both strains were increased by addition of KCl, NaCl, $CaCl_2$ or $MnSO_4$, and decreased by addition of $AgNO_3$, $CuSO_4$, $FeCl_3$ or $AlCl_3$. Secreted enzymes of both strains were most strongly inhibited by addition of $FeCl_3$ or $CuSO_4$. Taken together these results, WD12 could be a candidate strain of industrial alkaline protease production.

단백질 분해효소는 단백질 내 아미노산의 펩티드 결합을 가수분해하며, 산업분야에서 가장 많이 사용되는 효소이다. 이전의 논문에서 부패한 나무로부터 Pseudoxanthomonas sp. WD12와 WD32를 분리하였다. 분비된 단백질 분해효소의 특성을 조사한 결과 WD12는 pH 9.0, $50^{\circ}C$, WD32의 경우 pH 8.0, $45^{\circ}C$에서 최적 활성을 나타내었다. 최적조건하에서 최고의 활성은 WD12는 768 unit/mL로 WD12의 활성이 WD32보다 2.6배 높았다. 금속 이온에 대한 분비효소 영향을 조사한 결과 두 균주 모두 KCl, NaCl, $CaCl_2$, $MnSO_4$를 첨가했을 때 활성이 증가하였으며, $AgNO_3$, $CuSO_4$, $FeCl_3$, $AlCl_3$를 첨가했을 때는 감소하였고, 최고의 활성은 $MnSO_4$의 첨가했을 때 두 균주 모두 활성 증가를 보인 반면 $FeCl_3$, $CuSO_4$는 활성저해를 보였다. 신종으로 생각되는 WD12 균주의 효소는 알칼리성 조건의 산업 환경에서 이용가능 하다고 생각된다.

Keywords

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