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J Biotechnol ; 391: 50-56, 2024 Aug 10.
Article in English | 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.


Subject(s)
Enzyme Stability , Enzymes, Immobilized , Metal-Organic Frameworks , Kinetics , Metal-Organic Frameworks/chemistry , Enzymes, Immobilized/chemistry , Enzymes, Immobilized/metabolism , Hydrogen-Ion Concentration , Amino Acid Oxidoreductases/chemistry , Amino Acid Oxidoreductases/metabolism , Zirconium/chemistry , Amino Acids/chemistry , Amino Acids/metabolism , Adsorption , Temperature
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