Purification and properties of a heat-stable inulin fructotransferase from Arthrobacter ureafaciens.
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.
Haraguchi
Kazutomo
K
National Food Research Institute, 2-1-12 Kannondai, Tsukuba-shi, Ibaraki 305-8642, Japan. haraguti@nfri.affrc.go.jp
Yoshida
Mitsuru
M
Ohtsubo
Ken'ichi
K
D001173:Arthrobacter / Q000145:classification / Q000201:enzymology*; D004789:Enzyme Activation; D004795:Enzyme Stability; D006602:Hexosyltransferases / Q000096:biosynthesis / Q000737:chemistry* / Q000145:classification / Q000302:isolation & purification*; D006358:Hot Temperature; D008970:Molecular Weight; D013045:Species Specificity; D013696:Temperature
D006602:Hexosyltransferases; C097478:inulin fructotransferase (DFA I-producing)