FOOD SCIENCE ›› 2005, Vol. 26 ›› Issue (3): 69-71.

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Purification and Properties of β-fructofuranosidase from Arthrobacter 10137

 TONG  Qun-Yi, ZHU  Gui-Lan   

  1. School of Food Science and Technology, Southern Yangtze University
  • Online:2005-03-15 Published:2011-09-19

Abstract: The crudeβ-fructofuranosidase prepared from Arthrobacter sp. 10137 was fractioned in a sequence of operations 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℃ in the range of pH 6.0~8.0. The Ag+ and Cu2+ strongly inhibited β- fructofuranosidase activity, while EDTA and Mg2+ had no significant effect on it.

Key words: Arthrobacter 10137, β-fructofuranosidase, purification, properties