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应用
来自产碱杆菌属的胆碱氧化酶已用于：
- 在一项研究中研究用几丁质膜构建的胆碱生物传感器及其在测定胆碱酯酶抑制活性中的应用
- 胆碱氧化酶与共价结合黄素的光反应的光谱研究。
- 作为磷酸盐缓冲液 (PBS) 缓冲液的成分，用于测定脑组织匀浆中的胆碱乙酰转移酶 (ChAT) 活性
- 通过 ATX 活性试验测定自分泌运动因子 (ATX) 产生的胆碱，通过 PLD 活性试验测定磷脂酶-D (PLD) 产生的胆碱
生化/生理作用
胆碱氧化酶可利用甜菜碱醛作为中间体而分子氧作为次要电子受体，催化胆碱至甘氨酸-甜菜碱的四电子氧化。该酶还可接受甜菜碱醛作为底物。这使得对将胆碱转化为醛中间体、＆amp; 甜菜碱醛转化为甘氨酸-甜菜碱的反应机制研究成为可能。该酶是一种分子量约为72,000 Da（凝胶过滤）或66,000 Da（SDS凝胶电泳）的黄酮蛋白。
物理属性
等电点：4.1 ± 0.1
米氏常数：2.84 x 10-3M (胆碱), 5.33 x 10¯3M (甜菜醛)
结构：一摩尔的FAD与一摩尔的酶共价结合
抑制剂：对氯苯甲酸，Cu++，Co++，Hg++，Ag+
最适pH：8.0 – 8.5
最适温度：40 – 45°C
pH稳定性： pH 7.0 – 9.0 (30°C, 2小时)
热稳定性： 低于37°C (pH 7.5, 10分钟)
米氏常数：2.84 x 10-3M (胆碱), 5.33 x 10¯3M (甜菜醛)
结构：一摩尔的FAD与一摩尔的酶共价结合
抑制剂：对氯苯甲酸，Cu++，Co++，Hg++，Ag+
最适pH：8.0 – 8.5
最适温度：40 – 45°C
pH稳定性： pH 7.0 – 9.0 (30°C, 2小时)
热稳定性： 低于37°C (pH 7.5, 10分钟)
单位定义
一单位的酶在37°C、pH 8.0条件下每分钟内可将1 μ摩尔的胆碱氧化成甜菜碱，并同时生成1 μ摩尔的H2O2。注：在通过胆碱氧化酶进行胆碱向甜菜碱的转化过程中，每μ摩尔的胆碱将产生2μ摩尔的H2O2。
警示用语：
Danger
危险声明
预防措施声明
危险分类
Resp. Sens. 1
储存分类代码
11 - Combustible Solids
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
从最新的版本中选择一种：
分析证书(COA)
Lot/Batch Number
Bo-Chuan Hsieh et al.
Journal of pharmaceutical and biomedical analysis, 45(4), 673-678 (2007-03-03)
An amperometric flow-injection choline biosensor was assembled utilizing natural chitinous membrane as the supporting material for biocatalyst immobilization, and the membrane was purified from Taiwanese soldier crab, Mictyris brevidactylus. The chitinous membrane (<50.0 microm in thickness) was covalently immobilized with
M Ohta-Fukuyama et al.
Journal of biochemistry, 88(1), 197-203 (1980-07-01)
Choline oxidase from Alcaligenes sp. catalyzed the oxidation of choline and betaine aldehyde to betaine with concomitant consumption of oxygen and production of hydrogen peroxide. The values of Km for choline and betaine aldehyde were 0.87 and 6.2 mM, respectively.
S Pundir et al.
Analytical biochemistry, 427(1), 26-32 (2012-05-09)
A bienzymatic choline biosensor was constructed by coimmobilizing acetylcholinesterase (AChE) and choline oxidase (ChO) onto nanocomposite of carboxylated multiwalled carbon nanotubes (c-MWCNTs) and zirconium oxide nanoparticles (ZrO(2)NPs) electrodeposited on the surface of a glassy carbon electrode (GCE) and using it
S Ikuta et al.
Journal of biochemistry, 82(6), 1741-1749 (1977-12-01)
Choline oxidase was purified from the cells of Arthrobacter globiformis by fractionations with acetone and ammonium sulfate, and column chromatographies on DEAE-cellulose and on Sephadex G-200. The purified enzyme preparation appeared homogeneous on disc gel electrophoresis. The enzyme was a
Giovanni Gadda
Biochimica et biophysica acta, 1646(1-2), 112-118 (2003-03-15)
Choline oxidase catalyzes the four-electron oxidation of choline to glycine-betaine, with betaine-aldehyde as intermediate and molecular oxygen as primary electron acceptor. The enzyme is capable of accepting betaine-aldehyde as a substrate, allowing the investigation of the reaction mechanism for both
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