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Updated: Sep 20, 2026

Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins
Published on: June 20, 2019
Purification and properties of a heat-stable inulin fructotransferase from Arthrobacter ureafaciens
Kazutomo Haraguchi1, Mitsuru Yoshida, Ken'ichi Ohtsubo
1National Food Research Institute, 2-1-12 Kannondai, Tsukuba-shi, Ibaraki 305-8642, Japan. haraguti@nfri.affrc.go.jp
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.

