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Merck
CN

L3888

Sigma-Aldrich

D -莱氏乳杆菌乳酸脱氢酶

lyophilized powder, 150-500 units/mg protein

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别名:
(R)-乳酸:NAD+ 氧化还原酶, D-LDH
CAS号:
EC 号:
MDL编号:
UNSPSC代码:
12352204
NACRES:
NA.54

生物来源

bacterial (Lactobacillus leichmannii)

质量水平

形式

lyophilized powder

比活

150-500 units/mg protein

组成

Protein, ~50% biuret

异质活性

Malic dehydrogenase <0.5% of base activity

储存温度

−20°C

应用

在食品工业,主要催化作用是将NADH和H+转化成NAD+ ,心肌黄酶将无荧光的刃天青转化成强荧光物质试卤灵,以测量食品中D-乳酸的含量。

生化/生理作用

D-乳酸脱氢酶催化丙酮酸转化成 D-乳酸,同时将NADH氧化成NAD+。D-乳酸脱氢酶还可以催化逆反应,将D-乳酸转化成丙酮酸,同时将NAD+还原成NADH。

单位定义

D-乳酸脱氢酶催化丙酮酸转化成 D-乳酸,同时将NADH氧化成NAD+。 D-乳酸脱氢酶还可以催化逆反应,将 D-乳酸转化成丙酮酸,同时将NAD+ 还原成NADH。
在pH 7.0、25℃条件下,一单位酶每分钟可将1.0 μmM丙酮酸还原成D-乳酸。

外形

含有磷酸缓冲盐的冻干粉

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable

个人防护装备

Eyeshields, Gloves, type N95 (US)

法规信息

常规特殊物品

分析证书(COA)

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Gerrit Stuivenberg et al.
Journal of food science and technology, 59(9), 3419-3427 (2022-07-26)
Recent studies suggest histamine and d-lactate may negatively impact host health. As excess histamine is deleterious to the host, the identification of bacterial producers has contributed to concerns over the consumption of probiotics or live microorganisms in fermented food items.
Arnaud Mourier et al.
Biochimica et biophysica acta, 1777(10), 1283-1288 (2008-07-22)
Aerobically grown yeast cells express mitochondrial lactate dehydrogenases that localize to the mitochondrial inner membrane. The D-lactate dehydrogenase is a zinc-flavoprotein with high acceptor specificity for cytochrome c, that catalyzes the oxidation of D-lactate into pyruvate. In this paper, we
Fei Su et al.
Journal of bacteriology, 193(17), 4563-4564 (2011-06-28)
Bacillus coagulans 2-6 is an efficient producer of lactic acid. The genome of B. coagulans 2-6 has the smallest genome among the members of the genus Bacillus known to date. The frameshift mutation at the start of the d-lactate dehydrogenase
Takenori Shibahara et al.
Acta crystallographica. Section F, Structural biology and crystallization communications, 67(Pt 11), 1425-1427 (2011-11-22)
A dye-linked D-lactate dehydrogenase from the aerobic hyperthermophilic archaeon Aeropyrum pernix was crystallized using the hanging-drop vapour-diffusion method with polyethylene glycol 8000 as the precipitant. The crystals belonged to the monoclinic space group P2(1), with unit-cell parameters a = 63.4
Martin Engqvist et al.
The Journal of biological chemistry, 284(37), 25026-25037 (2009-07-10)
The Arabidopsis thaliana locus At5g06580 encodes an ortholog to Saccharomyces cerevisiae d-lactate dehydrogenase (AtD-LDH). The recombinant protein is a homodimer of 59-kDa subunits with one FAD per monomer. A substrate screen indicated that AtD-LDH catalyzes the oxidation of d- and

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