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Literature summary for 1.17.1.9 extracted from

  • Bommarius, A.S.; Karau, A.
    Deactivation of formate dehydrogenase (FDH) in solution and at gas-liquid interfaces (2005), Biotechnol. Prog., 21, 1663-1672.
    View publication on PubMed

Application

Application Comment Organism
biotechnology study on stability of recombinant enzyme in homogeneous aequeous solution, at gas-liquid interfaces in a bubble column, and under shear stress. Level of enzyme stability in solution also depends on the enzyme variant employed. Mutants C23S and C23S/C262A perform much better than wild-type in quiescent solution and reactors with little mechanical stress. Mutant C23S/C262A is less stable than wild-type at high stress levels in the Couette viscometer or the bubble column [Candida] boidinii

Protein Variants

Protein Variants Comment Organism
C23S in biotechnological applications, enzyme mutant performs much better than wild-type in quiescent solution and reactors with little mechanical stress [Candida] boidinii
C23S/C262A in biotechnological applications, enzyme mutant performs much better than wild-type in quiescent solution and reactors with little mechanical stress. Less stable than wild-type at high stress levels in the Couette viscometer or the bubble column [Candida] boidinii

Organism

Organism UniProt Comment Textmining
[Candida] boidinii
-
expression in Escherichia coli
-