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Production of Fructosyl Lysine Oxidase fromFusarium oxysporumS-1F4 on Autoclave-browned Medium
Author(s) -
Yasuyoshi Sakai,
Nobuyuki Yoshida,
Yoshiki Tani,
Nobuo Kato
Publication year - 1996
Publication title -
bioscience biotechnology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1271/bbb.60.150
Subject(s) - lysine , amadori rearrangement , browning , cycloheximide , chemistry , enzyme , glycation , biochemistry , autoclave , fusarium oxysporum , food science , protein biosynthesis , biology , botany , amino acid , organic chemistry , receptor
In Fusarium oxysporum S-1F4, fructosyl lysine oxidase (FLOD) was induced with N epsilon-fructosyl N alpha-Z-lysine (epsilon-FL), which is a model compound of a glycated protein, and the induction was inhibited by the addition of cycloheximide in the growing cells. FLOD formation was greatly enhanced in an autoclave-browned medium containing glucose and L-lysine. Some Amadori compounds formed from glucose and L-lysine during autoclaving were assumed to induce the enzyme. After optimization of the culture conditions, FLOD produced in the browned medium was comparable to that in the medium with epsilon-FL.

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