Abstract: The crudeβ -fructofuranosidase preparation from Arthrobacter sp. 10137 was fractioned in a sequence of operation including ammonium sulfate fraction, dialysis and column chromatography with Sepharose 6B. Purification of about 18.29 fold was achieved with an overall yield of 44.81%. The pure enzyme showed a single protein band by SDS-PAGE. Its molecular weight was estimated to be about 55800 by SDS-PAGE. The optimum temperature and pH of the enzyme were 30℃ and 6.5 respectively. The enzyme was stable under 45℃ and in the range of pH 6.0～8.0. The Ag+ and Cu2+ was strongly inhibited β - fructofuranosidase activity, while EDTA and Mg2+ had no significant effect on it.

Key words: Arthrobacter 10137, &beta, -fructofuranosidase, purification, properties