Some properties of a β-galactosidase from an extremely thermophilic bacterium
作者： D. A. Cowan , R. M. Daniel , A. M. Martin , H. W. Morgan
关键词: Chemistry 、 Bacteria 、 Thermus 、 Biochemistry 、 Thermophilic organism 、 Reagent 、 Strain (chemistry) 、 Product inhibition 、 Thermophile 、 Enzyme
摘要: An inducible β-galactosidase from an extremely thermophilic organism, Thermus strain 4−1A, has been isolated and partially purified. There were significant dissimilarities to T. aquaticus β-galactosidase. It had a pl of 4.5, was inhibited by sulphydryl inhibitors number transition metals, activated EDTA SH-containing reagents. The showed strong product inhibition, weaker inhibition some other mono- disaccharides. very stable up 90°C at pH 8. On immobilization diazonium linkage porous glass, the optimum (6.0), KM with ONPG (5mM) not altered.
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