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Purification and properties of a heat-stable inulin fructotransferase from Arthrobacter ureafaciens.

Authors
  • Haraguchi, Kazutomo
  • Yoshida, Mitsuru
  • Ohtsubo, Ken'ichi
Type
Published Article
Journal
Biotechnology letters
Publication Date
Jul 01, 2003
Volume
25
Issue
13
Pages
1049–1053
Identifiers
PMID: 12889813
Source
Medline
License
Unknown

Abstract

An inulin fructotransferase producing difructose dianhydride I (EC 2.4.1.200) was purified from Arthrobacter ureafaciens A51-1. It had maximum activity at pH 5.5 and 45 degrees C, and was stable up to 80 degrees C. This is the highest thermal stability for this enzyme reported to date. The molecular mass was estimated to be 38000 by SDS-PAGE, and 61000 by gel filtration. It was therefore estimated to be a dimer.

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