금속 이온을 이용한 Bacillus Stearothermophilus 호열성 단백질 분해효소의 역가 향상 및 호열 ${\cdot}$ 호기성 소화공정에의 응용

  • Published : 2000.11.09

Abstract

Proteolytic hydrolysis is one of the main enzymatic reaction of waste activated sludge (WAS) digestion. Pretense excreted from Bacillus stearothermophilus (ATCC 31197) showed optimum temperature of $75^{\circ}C$ for maxium heat stable proteolytic activity against azo casein. The dependency of $Ca^{2+}$, $Zn^{2+}$ on heat stability of proteolytic enzymes were measured with various concentrations. It was shown that $Ca^{2+}$ ion enhanced heat stability of these enzymes. Then thermophilic aerobic digestion (TAD) was performed using B. sterothermophilus with the addition of divalent ions. Performance of TAD process with ATCC 31197 activated by $Ca^{2+}$, $Zn^{2+}$ions in terms of dissolved organic carbon (DOC) concentration, extracellular protein concentration, and scanning electrion microscopy (SEM) analysis. The best result of protein reduction concentration in digestion test was obtained with the addition of 2 mM $Ca^{2+}$ ion.

B. Stearothermophilus 단백질 분해 효소는 2가 금속 이온인 $Ca^{2+}$에 의하여 내열성이 향상되며 $75^{\circ}C$에서 최대 역가를 나타내었다. 2mM $Ca^{2+}$를 첨가하여 B. Stearothermophilus를 이용한 호열 ${\cdot}$ 호기성 소화공정 운전할 경우 각각 최대량 대비 51%와 27%의 DOC 및 세포외단백질의 분해가 이루어지는 것을 확인하였다.

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