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C4405

Sigma-Aldrich

Choline Oxidase from Arthrobacter globiformis

lyophilized powder, 8-20 units/mg solid

Synonym(s):

Choline: oxygen 1-oxidoreductase

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

form

lyophilized powder

specific activity

8-20 units/mg solid

mol wt

71 kDa by SDS-PAGE
83 kDa by gel filtration

storage temp.

−20°C

General description

Research area: Cell signaling. Choline oxidaseis a flavoprotein and belongs to the glucose methanol choline(GMC)-oxidoreductase family.

Application

Choline Oxidase from Arthrobacter globiformis has been used:
  • for enzymatic determination of choline (Cho) and phosphocholine (P-Cho)
  • in sphingomyelin assay to determine the concentration of sphingomyelin by measuring free choline
  • in enzyme coating for the fully-assembled recording device for electrochemical measurements

Choline oxidase from Sigma has been used in the enzymatic determination of choline in milk using a flow injection analysis (FIA) system with potentiometric detection.Choline oxidase from Arthrobacterglobiformis is suitable for the preparation of amperometric biosensors.

Biochem/physiol Actions

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 can also accept betaine-aldehyde as a substrate. This allows the investigation of the reaction mechanism for the conversion of choline to the aldehyde intermediate and of betaine-aldehyde to glycine-betaine. The enzyme is a flavoprotein with a molecular weight of approximately 83,000 Da according to gel filtration or approximately 71,000 Da according to SDS gel electrophoresis. The optimum pH is found to be around pH 7.5 and the isoelectric point (pI) around pH 4.5.

Unit Definition

One unit will form 1 μmole of H2O2 with oxidation of 1 μmole of choline to betaine aldehyde per min at pH 8.0 at 37 °C. Note: During the conversion of choline to betaine by choline oxidase, 2 μmoles of H2O2 are produced for every μmole of choline.

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Choline import into chloroplasts limits glycine betaine synthesis in tobacco: analysis of plants engineered with a chloroplastic or a cytosolic pathway
Nuccio ML, et al.
Metabolic engineering, 2(4), 300-311 (2000)
A multi-site array for combined local electrochemistry and electrophysiology in the non-human primate brain
Disney AA, et al.
Journal of Neuroscience Methods, 255, 29-37 (2015)
Anish Khan et al.
Biosensors & bioelectronics, 31(1), 433-438 (2011-12-14)
The electrochemical biosensors based on poly(o-phenylenediamine) (PoPD) and acetylcholinesterase (AChE) and choline oxidase (ChO) enzymes were fabricated on carbon fibre (CF) substrate. The electropolymerized PoPD was used to reduce the interfering substances. The electrode assembly was completed by depositing functionalized
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
J L Lima et al.
The Analyst, 125(7), 1281-1284 (2000-09-14)
The development of a FIA system for the determination of total choline content in several types of milk is described. The samples were submitted to hydrochloric acid digestion before injection into the system and passed through an enzymatic reactor containing

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