Lactate dehydrogenase (LDH) was crystallized from concentrated
ammonium sulfate solution and
cross-linked with glutaraldehyde to afford long-lived enzymatically
active cross-linked crystals (LDH-CLC). The crystals were employed in an electrolytic cell for
lactate production from pyruvate, in
which the cathode consisted of a carbon electrode containing a coating
of lipoamide dehydrogenase
(LiDH) immobilized with methyl viologen under a Nafion membrane.
This cell was more effective
than a similar cell containing LDH in soluble form. An even
greater improvement in performance
was achieved by chemically binding a viologen derivative to the LiDH
and using an electrode based
on this modified enzyme in a cell containing LDH-CLC. The activity
of the LDH-CLC is much less
sensitive to pH than that of the soluble enzyme.
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