Purification and properties of fructosyl lysine oxidase from Fusarium oxysporum S-1F4.

Article abstract of DOI:10.1271/bbb.59.487

Fructosyl lysine oxidase (FLOD) was examined for its use in the enzymatic measurement of the level of glycated albumin in blood serum. To isolate microorganisms having such an enzyme activity, we used N epsilon-fructosyl N alpha-Z-lysine (epsilon-FL) as a sole nitrogen source in the enrichment culture medium. The isolated fungus, strain S-1F4, showed a high FLOD activity in the cell-free extract and was identified as Fusarium oxysporum. FLOD was purified to an apparent homogeneity on SDS-PAGE. The molecular mass of the subunit was 50 kDa on SDS-PAGE and seemed to exist in a monomeric form. The enzyme had an absorption spectrum characteristic of a flavoprotein and the flavin was found to be covalently bound to the enzyme. The enzyme acted against N epsilon-fructosyl N alpha-Z-lysine and N alpha-fructosyl N epsilon-Z-lysine and showed specificity for fructosyl lysine residues.

Full text of DOI:10.1271/bbb.59.487

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Purification and Properties of Fructosyl Lysine
Oxidase from Fusarium oxysporum S-1F4
Yasuyoshi Sakaia, Nobuyuki Yoshidaa, Atsuko Isogaia, Yoshiki Tania & Nobuo Katoa
a Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto University, Sakyo-
ku, Kyoto 606–01 , Japan
Published online: 12 Jun 2014.
To cite this article: Yasuyoshi Sakai, Nobuyuki Yoshida, Atsuko Isogai, Yoshiki Tani & Nobuo Kato (1995) Purification and
Properties of Fructosyl Lysine Oxidase from Fusarium oxysporum S-1F4, Bioscience, Biotechnology, and Biochemistry, 59:3,
487-491, DOI: 10.1271/bbb.59.487
To link to this article: http://dx.doi.org/10.1271/bbb.59.487
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