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
Hauptverfasser: Muramatsu, Kei, Onodera, Shuichi, Kikuchi, Masanori, Shiomi, Norio
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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.
ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.57.1681