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Process properties of an l-amino acid oxidase from Hebeloma cylindrosporum for the synthesis of phenylpyruvic acid from l-phenylalanine.
Journal of Biotechnology ( IF 4.1 ) Pub Date : 2020-07-09 , DOI: 10.1016/j.jbiotec.2020.07.005
Keiko Oike 1 , Harald Gröger 1
Affiliation  

The biocatalytic oxidation of amino acids represents an attractive approach towards the synthesis of α-keto acids, which are interest for various industrial applications. As l-amino acids are readily available from fermentation processes, these natural amino acids can serve as substrates in combination with an l-amino acid oxidase. Besides an aqueous phase as reaction medium, a further advantage of such a process is the utilization of air as oxidation agent. In this study, we studied the organic-synthetic properties of a literature-known recombinant l-amino acid oxidase from the fungus Hebeloma cylindrosporum with respect to its suitability to catalyze the formation of α-keto acids exemplified for the synthesis of phenylpyruvic acid starting from l-phenylalanine as a substrate. In our study the enzyme displayed a reasonable operational stability in the reaction system and as well as promising applicability data with respect to substrate and product inhibition. In a biotransformation, 20 mM of substrate were converted after 4 h reaction. The formation of undesired by-products was suppressed using a commercially available catalase enzyme.



中文翻译:

来自 Hebeloma cylindrosporum 的 l-氨基酸氧化酶的工艺特性,用于从 l-苯丙氨酸合成苯丙酮酸。

氨基酸的生物催化氧化代表了合成 α-酮酸的一种有吸引力的方法,这些方法对各种工业应用都很感兴趣。由于l-氨基酸很容易从发酵过程中获得,这些天然氨基酸可以作为与l-氨基酸氧化酶组合的底物。除了水相作为反应介质之外,这种方法的另一个优点是利用空气作为氧化剂。在这项研究中,我们研究了来自真菌Hebeloma cylindrosporum的文献中已知的重组l-氨基酸氧化酶的有机合成特性。关于其催化α-酮酸形成的适用性,举例说明了以l-苯丙氨酸为底物合成苯丙酮酸。在我们的研究中,酶在反应系统中表现出合理的操作稳定性,以及关于底物和产物抑制的有希望的适用性数据。在生物转化中,20 mM 的底物在反应 4 小时后被转化。使用市售的过氧化氢酶抑制了不需要的副产物的形成。

更新日期:2020-09-03
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