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된장으로부터 분리한 Bacillus subtilis CK-2가 생산하는 가수분해효소의 활성 특성

Characteristics of Hydrolytic Enzymes that Produced by Bacillus subtilis CK-2 Isolated from Doenjang

  • 이상협 (경남과학기술대학교 제약공학과) ;
  • 김철호 (경남과학기술대학교 제약공학과)
  • Lee, Sang-Hyup (Dept. of Pharmaceutical Engineering, Gyeongnam National University of Science and Technology) ;
  • Kim, Chul-Ho (Dept. of Pharmaceutical Engineering, Gyeongnam National University of Science and Technology)
  • 투고 : 2017.03.08
  • 심사 : 2017.07.19
  • 발행 : 2017.07.30

초록

이전의 논문에서 된장으로부터 섬유소와 지질, 녹말, 그리고 단백질을 포함하는 다양한 유기물을 가수분해하는 세균을 분리한 바 있다. 본 연구에서는 분리균주인 Bacillus subtilis CK-2가 생산하는 각종 가수분해효소의 조효소 특성을 확인하였다. 섬유소분해효소의 경우 적정 수소이온농도는 pH 5.0, 적정온도는 $55^{\circ}C$로 확인되었으며, pH 5.0~10.0과 $20{\sim}50^{\circ}C$의 범위에서 높은 활성을 나타내었다. 섬유소분해효소는 $Co^{2+}$ 이온에 의해 활성이 높아지며, 0.45%(w/v)의 $Co^{2+}$ 이온 농도에서 가장 높은 활성을 보였다. 녹말분해효소의 경우 적정 수소이온농도는 pH 5.0, 적정온도는 $50^{\circ}C$로 확인되었으며, pH 4.0~5.0과 $20{\sim}50^{\circ}C$의 범위에서 높은 활성을 나타내었다. 녹말분해효소는 $Co^{2+}$ 이온에 의해 활성이 높아지며, 0.2%(w/v)의 $Co^{2+}$ 이온 농도에서 가장 높은 활성을 보였다. 단백질분해효소의 경우 적정 수소이온농도는 pH 8.0, 적정온도는 $50^{\circ}C$로 확인되었으며, pH 7.0~8.5과 $20{\sim}50^{\circ}C$의 범위에서 높은 활성을 나타내었다. 섬유소분해효소는 $Mn^{2+}$ 이온에 의해 활성이 높아지며, 0.125%(w/v)의 $Mn^{2+}$ 이온 농도에서 가장 높은 활성을 보였다. 이러한 결과로부터 B. subtilis CK-가 생산하는 가수분해효소를 산업적으로 이용하기 위해서는 효소의 종류에 따라 수소이온농도와 온도, 그리고 금속이온을 적절하게 조절할 필요가 있다는 것을 알 수 있다.

In the previous paper, we isolated a bacterium that can hydrolyze various organic materials from soybean paste, including cellulose, lipids, starch, and protein. The activity and chemical properties of the crude enzymes produced by the isolate Bacillus subtilis CK-2 were further investigated. Cellulase showed the highest activity at pH 5.0 and $55^{\circ}C$. The stability of cellulase was maintained within the ranges of pH 5.0~10.0 and $20{\sim}50^{\circ}C$. Cellulolytic enzymes were activated by a $Co^{2+}$ ion, demonstrating the highest activity at a 0.45%(w/v) concentration of $Co^{2+}$. The optimal conditions for amylase were pH 5.0 and $50^{\circ}C$. The activity of amylase was stable within the ranges of pH 4.0~5.0 and $20{\sim}50^{\circ}C$. The $Co^{2+}$ ion was also necessary for amylase activity, which was the highest at a 0.2%(w/v) concentration of $Co^{2+}$. The optimal pH and temperature conditions of protease were pH 8.0 and $50^{\circ}C$. The activity of protease was stable within the ranges of pH 7.0~8.5 and $20{\sim}50^{\circ}C$. Protease activity was catalyzed by $Mn^{2+}$, which was the highest at a 0.125%(w/v) concentration of $Mn^{2+}$. The isolate B. subtilis CK-2 demonstrated a high activity of autolysin. Based on these results, we identified and suggested the optimal pH, temperature, and metal ion concentration in the use of the hydrolytic enzymes of B. subtilis CK-2 for industrial purposes.

키워드

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