49971
D-Lactic Dehydrogenase from Lactobacillus leichmannii
suspension, yellow, ~1000 U/mL
Synonym(s):
(R)-Lactate:NAD+ oxidoreductase, D-Lactate Dehydrogenase
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About This Item
biological source
bacterial (Lactobacillus leichmannii)
form
suspension
specific activity
≥30 U/mg protein
concentration
~1000 U/mL
impurities
L-Lactat Dehydrogenase, none detected
3.2 M Ammonium sulfate solution (pH ~6.2)
color
yellow
storage temp.
2-8°C
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.
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.
Unit Definition
1 U corresponds to the amount of enzyme which will reduce 1 μmol of pyruvate to D-lactate per minute at pH 7.0 and 25 °C
Physical form
only partially soluble in water or buffer
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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