A novel extracellular β-fructosidase produced by Bacillus stearothermophilus has been identified and purified. The purified enzyme, obtained by using successive QEAE Sepharose fast flow and Sephacryl S300 HR columns, has a 600 kDa relative molecular weight (Mr) and is composed of 60 kDa subunits indicating a multimeric structure. The pH and temperature for optimal activity are 6.5 and 65°C respectively, the enzyme being thermostable at this temperature. The apparent Km values for sucrose and inulin are 3.56 mmol l-1 and 1 mmol l-1 respectively, the total invertase/total inulinase ratio being 4.
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Belamri et al. (1994) studied this question.
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