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J Biotechnol ; 391: 50-56, 2024 Aug 10.
Artigo em Inglês | MEDLINE | ID: mdl-38852680

RESUMO

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.


Assuntos
Estabilidade Enzimática , Enzimas Imobilizadas , Estruturas Metalorgânicas , Cinética , Estruturas Metalorgânicas/química , Enzimas Imobilizadas/química , Enzimas Imobilizadas/metabolismo , Concentração de Íons de Hidrogênio , Aminoácido Oxirredutases/química , Aminoácido Oxirredutases/metabolismo , Zircônio/química , Aminoácidos/química , Aminoácidos/metabolismo , Adsorção , Temperatura
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