用于封装氨基酸脱氢酶的氨基酸金属有机框架的动力学和稳定性研究

IF 4.1 2区 生物学 Q2 BIOTECHNOLOGY & APPLIED MICROBIOLOGY
Lingling Dong , Yu Xiong , Xiaoyan Xiang , Feixuan Li , Qidi Song , Shizhen Wang
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引用次数: 0

摘要

采用物理吸附法将 Zr-MOFs 固定化为嗜热和嗜卤氨基酸脱氢酶(Zr-MOFs-NTAaDH),用于 L-高苯丙氨酸的生物合成。在 70°C 时,Zr-MOFs-NTAaDH 的活性是游离酶的 3.3 倍。在 pH 值为 11 时,Zr-MOFs-NTAaDH 的酶活性保持在 4.16 U/mg 的水平,是 NTAaDH 的 7.8 倍。动力学参数表明,与游离酶相比,Zr-MOFs-NTAaDH 的催化效率提高了,Zr-MOFs-NTAaDH 的 kcat 是游离酶的 12.3 倍。经过 7 次循环后,Zr-MOFs-NTAaDH 的活性保持在 68%。Zr-MOFs-NTAaDH 对离子液体的耐受性很高,这表明它在工业应用方面具有巨大潜力。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Kinetic and stability studies of amino acid metal-organic frameworks for encapsulating of amino acid dehydrogenase

Kinetic and stability studies of amino acid metal-organic frameworks for encapsulating of amino acid dehydrogenase

Zr-MOFs was applied for the immobilization of hyperthermophilic and halophilic amino acid dehydrogenase (Zr-MOFs-NTAaDH) by physical adsorption for the biosynthesis of L-homophenylalanine. Activity of Zr-MOFs-NTAaDH was enhanced by 3.3-fold of the free enzyme at 70°C. And the enzyme activity of Zr-MOFs-NTAaDH was maintained at 4.16 U/mg at pH 11, which was 7.8 folds of that of NTAaDH. Kinetic parameters indicated catalytic efficiency of Zr-MOFs-NTAaDH was increased compared to the free enzyme as kcat of Zr-MOFs-NTAaDH was 12.3-fold of that of free enzyme. After 7 recycles, the activity of Zr-MOFs-NTAaDH remained 68 %. And Zr-MOFs-NTAaDH exhibited high ionic liquid tolerance which indicated the great potential for industrial application.

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来源期刊
Journal of biotechnology
Journal of biotechnology 工程技术-生物工程与应用微生物
CiteScore
8.90
自引率
2.40%
发文量
190
审稿时长
45 days
期刊介绍: The Journal of Biotechnology has an open access mirror journal, the Journal of Biotechnology: X, sharing the same aims and scope, editorial team, submission system and rigorous peer review. The Journal provides a medium for the rapid publication of both full-length articles and short communications on novel and innovative aspects of biotechnology. The Journal will accept papers ranging from genetic or molecular biological positions to those covering biochemical, chemical or bioprocess engineering aspects as well as computer application of new software concepts, provided that in each case the material is directly relevant to biotechnological systems. Papers presenting information of a multidisciplinary nature that would not be suitable for publication in a journal devoted to a single discipline, are particularly welcome.
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