D-Lactic Dehydrogenase from Lactobacillus leichmanii, lyophilized powder, 150-300 units/mg protein

D-Lactic Dehydrogenase from Lactobacillus leichmanii, lyophilized powder, 150-300 units/mg protein

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Application


In the food industry, the primary catalysis is coupled to conversion of NADH and H+ to NAD+ with diaphorase coupled with converting the non-fluorescent resazurin to the highly fluorescent substance resorufin to measure the content of D-lactate in food products.


Biochem/physiol Actions


D-lactic dehydrogenase catalyzes the conversion of pyruvate into D-lactate, with oxidation of NADH to NAD+. D-lactic dehydrogenase can also catalyze the reverse reaction, conversion of D-lactate into pyruvate with reduction of NAD+ to NADH.


Packaging


500, 2500 units in poly bottle


Physical form


Lyophilized powder containing phosphate buffer salts


Unit Definition


D-lactic dehydrogenase catalyzes the conversion of pyruvate into D-lactate, with oxidation of NADH to NAD+. D-lactic dehydrogenase can also catalyze the reverse reaction, conversion of D-lactate into pyruvate with reduction of NAD+ to NADH.


One unit will reduce 1.0 µmole of pyruvate to D-lactate per min at pH 7.0 at 25 °C.

Quality Level200
ManufacturerSIGMA-ALDRICH
CompositionProtein, ~50% biuret
Storage Temp.−20°C
Formlyophilized powder

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