Inulin fructotransferase (DFA III-producing) from Leifsonia sp. T88-4

An inulin fructotransferase (DFA III-producing) [EC 2.4.1.93] from Leifsonia sp. T88-4 was purified and characterized, for the first time. The enzyme was purified from culture supernatant of the microorganism 32.4-fold with a yield of 11.3% using a DEAE–Toyopearl chromatography and two times of Supe...

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Bibliographic Details
Published in:Carbohydrate polymers 2006-10, Vol.66 (1), p.75-80
Main Authors: Haraguchi, Kazutomo, Yoshida, Mitsuru, Ohtsubo, Ken’ichi
Format: Article
Language:English
Subjects:
Biological and medical sciences
Biotechnology
DFA III (difructose dianhydride III)
difructose dianhydride
enzyme activity
Enzyme engineering
Fundamental and applied biological sciences. Psychology
Improved methods for extraction and purification of enzymes
Inulin
Leifsonia
Methods. Procedures. Technologies
physicochemical properties
purification
transferases
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Summary:An inulin fructotransferase (DFA III-producing) [EC 2.4.1.93] from Leifsonia sp. T88-4 was purified and characterized, for the first time. The enzyme was purified from culture supernatant of the microorganism 32.4-fold with a yield of 11.3% using a DEAE–Toyopearl chromatography and two times of Super Q-Toyopearl chromatography. The enzyme showed maximum activity at pH 5.0 and 65 °C. This maximum temperature was highest in the inulin fructotransferase (DFA III-producing) reported to date. The enzyme activity was stable up to 60 °C after 30 min heat treatment. The molecular mass of the enzyme was estimated to be 44 kDa by SDS–PAGE and 74 kDa by gel filtration, and was considered to be a dimer. The N-terminal amino acid sequence (16 amino acid residues) was determined as METNVYDVTDVGVPGR. The K m value of the reaction at pH 5.0 and 60 °C was estimated to be 1.0 mM.
ISSN:0144-8617
1879-1344
DOI:10.1016/j.carbpol.2006.02.027