PURIFICATION AND PROPERTIES OF AN EXTRACELLULAR INULINASE-LIKE BETA-FRUCTOSIDASE FROM BACILLUS-STEAROTHERMOPHILUS

Citation
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
Citations number
24
Categorie Soggetti
Microbiology,"Biothechnology & Applied Migrobiology
ISSN journal
02668254
Volume
19
Issue
6
Year of publication
1994
Pages
410 - 413
Database
ISI
SICI code
0266-8254(1994)19:6<410:PAPOAE>2.0.ZU;2-8
Abstract
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.