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An Assay for Measuring the Activity of Escherichia coli Inducible Lysine Decarboxyase
Published on: December 19, 2010
New enzymatic methods for selective assay of L-lysine using an L-lysine specific decarboxylase/oxidase from
Asami Sugawara1, Daisuke Matsui2, Miwa Yamada1
1Department of Biological Chemistry and Food Science, Faculty of Agriculture, Iwate University, 3-18-8 Ueda, Morioka 020-8550, Japan.
Abstract:
We developed new enzymatic methods for the selective assay of L-lysine by utilizing an oxidase reaction and a decarboxylation reaction by the L-lysine-specific decarboxylase/oxidase (L-Lys-DC/OD) from Burkholderia sp. AIU 395. The method utilizing the oxidase reaction of this enzyme was useful for determination of high concentrations of L-lysine. The method utilizing the decarboxylase reaction, which proceeded via the combination of the L-Lys-DC/OD and putrescine oxidase (PUO) from Micrococcus rubens, was effective for determination of low concentrations of L-lysine. Both methods showed good linearity, and neither was affected by other amino acids or amines. In addition, the within-assay and between-assay precisions of both methods were within the allowable range. The coupling of L-Lys-DC/OD with PUO was also useful for the differential assay of L-lysine and cadaverine. These newly developed methods were applied to the assay of L-lysine in biological samples and found to be effective.
