Purification and Some Properties of β-Fructofuranosidase from Bifidobacterium adolescentis G1
A unique β-fructofuranosidase was purified from the extract of Bifidobacterium adolescentis G1 by anion-exchange, hydrophobic, and gel filtration chromatographies, and preparative electrophoresis. The molecular mass was 74kDa by SDS-PAGE, and the isoelectric point was pH 4.5. The enzyme was a monome...
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Veröffentlicht in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 1993, Vol.57 (10), p.1681-1685 |
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Sprache: | eng |
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Zusammenfassung: | A unique β-fructofuranosidase was purified from the extract of Bifidobacterium adolescentis G1 by anion-exchange, hydrophobic, and gel filtration chromatographies, and preparative electrophoresis. The molecular mass was 74kDa by SDS-PAGE, and the isoelectric point was pH 4.5. The enzyme was a monomeric protein. The pH optimum was at 6.1. The enzyme was stable at pH from 6.5 to 10.0, and up to 45°C. The neutral sugar content was 1.2%. The enzyme hydrolyzed 1-kestose faster than sucrose or inulin. The hydrolytic activity was strongly inhibited by Cu
2+
, Ag
+
, Hg
+
, and ρ-chloromercuribenzoic acid. The K
m
(mM) and k
0
(s
−1
) were: 1-kestose, 1.1 and 231; sucrose, 11 and 59.0; inulin, 8.0 and 149, respectively. From the kinetic results, β-fructofuranosidase from B. adolescentis G1 was concluded to have a high affinity for 1-kestose, thus differing from invertases and exo-inulinases in substrate specificity. |
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ISSN: | 0916-8451 1347-6947 |
DOI: | 10.1271/bbb.57.1681 |