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

Code: l3888-2.5ku D2-231

Not available outside of the UK & Ireland.

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-...


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$337.85 EACH

Not available outside of the UK & Ireland.

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.

biological sourcebacterial (Lactobacillus leichmannii)
compositionProtein, ~50% biuret
foreign activityMalic dehydrogenase ﹤0.5% of base activity
formlyophilized powder
Quality Level200
specific activity150-500 units/mg protein
storage temp.−20°C
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Cas Number9028-36-8
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