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New enzymatic methods for selective assay of L-lysine using an L-lysine specific decarboxylase/oxidase from Burkholderia sp AIU 395

机译:使用来自Burkholderia sp AIU 395的L-赖氨酸特异性脱羧酶/氧化酶选择性测定L-赖氨酸的新酶方法

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摘要

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. (C) 2014, The Society for Biotechnology, Japan. All rights reserved.
机译:我们通过利用Burkholderia sp。的L-赖氨酸特异性脱羧酶/氧化酶(L-Lys-DC / OD)的氧化酶反应和脱羧反应,开发了选择性检测L-赖氨酸的新酶方法。 AIU 395.利用这种酶的氧化酶反应的方法可用于测定高浓度的L-赖氨酸。利用脱羧酶反应的方法,该方法通过将L-Lys-DC / OD和来自微球菌的腐胺氧化酶(PUO)结合进行,对于测定低浓度的L-赖氨酸有效。两种方法均显示出良好的线性,并且均不受其他氨基酸或胺的影响。此外,两种方法的测定内和测定间精度均在允许范围内。 L-Lys-DC / OD与PUO的偶联也可用于L-赖氨酸和尸胺的差异分析。这些新开发的方法应用于生物样品中L-赖氨酸的测定,发现是有效的。 (C)2014,日本生物技术学会。版权所有。

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