Abstract
We have investigated the enzymatic characterization of recombinant β-fructofuranosidase from Bifidobacterium longum JCM1217. This recombinant protein was expressed in Escherichia coli, and showed high activity of hydrolysis on fructo-oligosaccharides with a low degree of polymerization. The molecular mass of the purified recombinant protein was estimated to be about 64,000 by SDS-PAGE and 59,600 by MALDI TOF-MS. The optimum pH and pH stability of the enzyme were 5.7 and 5.0-7.9, respectively. The temperature stability of the enzyme was indicated up to 50°C. The Km (mM), Vmax (μmol/min/mg of protein), k0 (s-1) and k0/Km (mM-1 s-1) for 1-kestose, sucrose, neokestose, nystose, fructosylnystose and inulin were 1.2, 97, 96.4 and 80.3, 38, 64, 63.6 and 1.7, 2.1, 109, 105.3 and 50.1, 4.2, 52, 51.7 and 12.3, 3.1, 66, 65.6 and 21.2, 16.5, 72, 71.6 and 4.3, respectively. This recombinant protein had a high affinity for fructo-oligosaccharides.
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