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Purification and Properties of Intracellular Invertase from Alkalophilic and Thermophilic Bacillus cereus TA-11
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2007
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Intracellular InvertaseBiosynthesisEngineeringCellular EnzymologyBiochemistryMaximum Enzyme ActivityBiocatalysisNatural SciencesBacteriologyBiotechnologyEnzyme CatalysisThermophilic BacillusImmobilized EnzymeMicrobiologyMolecular MicrobiologyEnzyme ActivityStructure-function Enzyme KineticsEnzymatic Modification
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 , and the purified enzyme was stable at the pH range of 5.0 to 8.0 and below . and values of the enzyme for sucrose were 370 mM and 3.0 per min, respectively. The enzyme activity was significantly inhibited by bivalent metal ions (, and ) and sugars (glucose and fructose).