• 자연과학논문집
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• 제18권1호
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• pp.29-38
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• 2007

호 알칼리성이며 고온성인 Bacillus cereus TA-11이 세포내로 생성하는 invertase의 생합성 조절 양상을 조사하였다. Bacillus cereus TA-11의 세포내 invertase는 10 mM sucrose의 180분 처리와 25 mM raffinose의 90분 처리에서 각각 효율적으로 유도되었다. 또한 glucose는 sucrose에 의한 invertase의 유도를 억제하였고 cAMP첨가는 catabolite repression을 감소시키지 못하였다.

• Journal of Applied Biological Chemistry
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• 제50권4호
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• pp.196-201
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• 2007

An intracellular invertase was purified to homogeneity from the cell extract of an alkalophilic and thermophilic Bacillus sp. TA-11, which was classified as a new species belonging to Bacillus cereus based on chemotaxanomic and phylogenetic analyses. The purified enzyme with a recovery of 26.6% was determined to be a monomeric protein with a molecular weight of 23 kDa by SDS-PAGE and 26 kDa by gel filtration. The maximum enzyme activity was observed at pH 7.0 and $50^{\circ}C$, and the purified enzyme was stable at the pH range of 5.0 to 8.0 and below $60^{\circ}C$. $K_m$ and $V_{max}$ values of the enzyme for sucrose were 370 mM and 3.0 ${\mu}M$ per min, respectively. The enzyme activity was significantly inhibited by bivalent metal ions ($Hg^{2+}$, $Cd^{2+}$ and $Cu^{2+}$) and sugars (glucose and fructose).