Fructosyl amino acid oxidase
First Claim
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1. A fructosyl amino acid oxidase enzyme having the following physicochemical characteristics:
- a) it catalyzes the oxidation of an amadori compound in the presence of oxygen to generate α
-ketoaldehyde, amine derivatives and hydrogen peroxide;
b) it is active on fructosyl lysine and fructosyl valine, wherein the activity on fructosyl lysine is the same as or higher than the activity on fructosyl valine;
c) it is stable in the pH range of about 4.0 to 13.0 with optimal activity at a pH of 8.5;
d) it is stable in the temperature range of about 20°
to 50°
C. with optimal activity at a temperature of 30°
to 35°
C.;
e) the molecular weight is about 106,000 daltons when estimated by gel filtration with Superdex 200 pg;
f) a covalently-bound flavin adenine dinucleotide is required as a coenzyme for activity; and
g) the isoelectric point of the enzyme is 6.8 as measured by disc electrofocussing.
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Abstract
A novel fructosyl amino acid oxidase derived from genus Fusarium, which is active on both of fructosyl lysine and fructosyl valine, a process for producing the enzyme, an assay of an amadori compound using the enzyme, a reagent or a kit containing the enzyme is provided.
43 Citations
3 Claims
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1. A fructosyl amino acid oxidase enzyme having the following physicochemical characteristics:
-
a) it catalyzes the oxidation of an amadori compound in the presence of oxygen to generate α
-ketoaldehyde, amine derivatives and hydrogen peroxide;b) it is active on fructosyl lysine and fructosyl valine, wherein the activity on fructosyl lysine is the same as or higher than the activity on fructosyl valine; c) it is stable in the pH range of about 4.0 to 13.0 with optimal activity at a pH of 8.5; d) it is stable in the temperature range of about 20°
to 50°
C. with optimal activity at a temperature of 30°
to 35°
C.;e) the molecular weight is about 106,000 daltons when estimated by gel filtration with Superdex 200 pg; f) a covalently-bound flavin adenine dinucleotide is required as a coenzyme for activity; and g) the isoelectric point of the enzyme is 6.8 as measured by disc electrofocussing. - View Dependent Claims (2, 3)
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Specification