- Cellulomonas sp. CS1-1으로 부터의 $eta$-Glucosidase의 합성조절과 그의 효소학적 성질
- ㆍ 저자명
- 이희순,민경희,배무
- ㆍ 간행물명
- 산업미생물학회지
- ㆍ 권/호정보
- 1988년|16권 2호|pp.119-125 (7 pages)
- ㆍ 발행정보
- 한국미생물생명공학회
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- 정기간행물| PDF텍스트
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- 기타
Cellulomonas sp. CS1-1 생성의 $eta$-glucosidase는 cell-bound 효소이었으며, Avicelase와 Carboxymethyl-cellulase (CMCase)는 extracellular 효소로 존재함을 확인하였다. Cellobiose나 CMC 최소배지에서의 균의 생장은 cellobiose보다 glucose 첨가시에 현저히 증가하였다. Cellobiose나 CMC 최소배지에서의 $eta$-glucosidase 생합성은 glucose 첨가로 현저히 억제되었으나, CMC 최소배지에 cellobiose를 첨가하였을 경우, glucose에 의한 억제 효과와는 반대로, 효소의 생성은 오히려 촉진되었다. 그 외의 탄소원에 관한 영향을 조사한 결과 CMC, 전분, maltose 등의 첨가도 glycerol, arabinose, xylose, trehalose의 첨가시 보다 효소의 생성이 증가되었다. 이상의 결과로 $eta$-glucosidase 생합성은 glucose에 의하여 catabolite repression을 받았으며, cellobiose, CMC, starch등은 다른 당류보다 효소생성을 현저히 유도하였으므로, 이 효소는 inducible enzyme임을 알 수 있었다. 효소생성에 미치는 질소원을 조사한 결과는 yeast extract가 peptone이나 ammonium sulfate보다 효소생성을 증가시켰다. 효소의 특성을 조사한 결과, 50mM MgCl$_2$가 포함된 10mM potassium phosphate buffer (pH 7.0)에서 효소의 역가가 증가하였고, 최적 pH는 6.0이었고 최적온도는 42$^{circ}C$ 이었다. p-nitrophenyl-$eta$-D-glucoside의 농도에 대한 glucose의 Km값은 0.265mM 이었고 $eta$-D(+)-glucose에 대한 Ki값은 9.0 mM 이었다.
$eta$-Glucosidase of Cellulomonas sp. CS1-1 in cellular compartment was localized with cell-bound form while Avicelase and carboxymethylcellulase (CMCase) were appeared with extracellular enzyme. Cell growth on cellulose or CMC minimal broth was increased by glucose addition. $eta$-Glucosidase production on cellobiose or CMC minimal broth was repressed by the addition of glucose. However, on CMC minimal broth, the enzyme production was specially stimulated by cellobiose addition. $eta$-Glucosidase production was also induced by CMC, starcth and maltose compared with glycerol, arabinose, xylose and trehalose. From the above results, it was concluded that glucose effect on $eta$-glucosidase biosynthesis showed catabolite repression, but enzyme production was induced by cellobiose, CMC, and starch, indicating that $eta$-glucosidase is inducible enzyme. Yeast extract stimulated $eta$-glucosidase production more than peptone and ammonium sulfate. $eta$-Glucosidase activity was increased with 50mM MgCl$_2$in 10mM potassium phosphate buffer (pH 7.0). Optimum conditions for enzyme activities were pH 6.0 and 42$^{circ}C$, Km value of $eta$-glucosidase for p-nitrophenyl-$eta$-D-glucosidase was 0.256mM and Ki for $eta$-D(+)-glucose was 9.0mM.