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Purification and Properties of Intracellular Invertase from Alkalophilic and Thermophilic Bacillus cereus TA-11  

Yoon, Min-Ho (Department of BioEnvironmental Chemistry, College of Agriculture and Life, Chungnam National University)
Choi, Woo-Young (Department of BioEnvironmental Chemistry, College of Agriculture and Life, Chungnam National University)
Kwon, Su-Jin (Department of Life Science and Genetic Engineering, Paichai University)
Yi, Sung-Hun (Korea Food Research Institute)
Lee, Dae-Hyung (Department of Life Science and Genetic Engineering, Paichai University)
Lee, Jong-Soo (Department of Life Science and Genetic Engineering, Paichai University)
Publication Information
Journal of Applied Biological Chemistry / v.50, no.4, 2007 , pp. 196-201 More about this Journal
Abstract
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).
Keywords
alkalophilic; Bacillus cereus; intracellular invertase; thermophilic;
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Times Cited By KSCI : 1  (Citation Analysis)
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