M. Belamri et al., PURIFICATION AND PROPERTIES OF AN EXTRACELLULAR INULINASE-LIKE BETA-FRUCTOSIDASE FROM BACILLUS-STEAROTHERMOPHILUS, Letters in applied microbiology, 19(6), 1994, pp. 410-413
A novel extracellular beta-fructosidase produced by Bacillus stearothe
rmophilus has been identified and purified. The purified enzyme, obtai
ned by using successive QEAE Sepharose fast flow and Sephacryl S300 HR
columns, has a 600 kDa relative molecular weight (M(r)) and is compos
ed of 60 kDa subunits indicating a multimeric structure. The pH and te
mperature for optimal activity are 6.5 and 65 degrees C respectively,
the enzyme being thermostable at this temperature. The apparent K-m va
lues for sucrose and inulin are 3.56 mmol 1(-1) and 1 mmol 1(-1) respe
ctively, the total invertase/total inulinase ratio being 4.