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Purification and properties of an extracellular inulinase‐like β‐fructosidase from Bacillus stearothermophilus
Author(s) -
Belamri M.,
Sassi A. Hadj,
Savart M.,
TantaouiElaraki A.,
Cottin P.
Publication year - 1994
Publication title -
letters in applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.698
H-Index - 110
eISSN - 1472-765X
pISSN - 0266-8254
DOI - 10.1111/j.1472-765x.1994.tb00969.x
Subject(s) - inulinase , invertase , inulin , extracellular , enzyme , bacillales , sucrose , bacillaceae , biochemistry , sepharose , molecular mass , chemistry , chromatography , biology , bacteria , food science , bacillus subtilis , genetics
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 (M r ) 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 K m 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.