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Kinetic and stability studies of amino acid metal-organic frameworks for encapsulating of amino acid dehydrogenase.
Dong, Lingling; Xiong, Yu; Xiang, Xiaoyan; Li, Feixuan; Song, Qidi; Wang, Shizhen.
Afiliação
  • Dong L; Department of Chemical and Biochemical Engineering, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005, China.
  • Xiong Y; Department of Chemical and Biochemical Engineering, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005, China.
  • Xiang X; Department of Chemical and Biochemical Engineering, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005, China.
  • Li F; Department of Chemical and Biochemical Engineering, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005, China.
  • Song Q; Department of Chemical and Biochemical Engineering, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005, China.
  • Wang S; Department of Chemical and Biochemical Engineering, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005, China; Xiamen Key Laboratory of Synthetic Biotechnology, Xiamen University, Xiamen, Fujian 361005, China. Electronic address: szwang@xmu.edu.cn.
J Biotechnol ; 391: 50-56, 2024 Aug 10.
Article em En | MEDLINE | ID: mdl-38852680
ABSTRACT
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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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Estabilidade Enzimática / Enzimas Imobilizadas / Estruturas Metalorgânicas Idioma: En Revista: J Biotechnol Assunto da revista: BIOTECNOLOGIA Ano de publicação: 2024 Tipo de documento: Article País de publicação: Holanda
Texto completo
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Estabilidade Enzimática / Enzimas Imobilizadas / Estruturas Metalorgânicas Idioma: En Revista: J Biotechnol Assunto da revista: BIOTECNOLOGIA Ano de publicação: 2024 Tipo de documento: Article País de publicação: Holanda