Application and pH stability of acetyl CoA oxidase

The acetyl CoA oxidase present in the red blood cell membrane of living organisms has two different forms of existence, one is long-chain acetyl CoA oxidase, and the other has high similarity to long-chain acyl CoA in human liver. The first type of long-chain acyl CoA is more common and plays an important regulatory role in the metabolism of fatty acids in red blood cell membranes. This enzyme regulates various important biological processes such as phospholipid acylation and deacetylation, red blood cell membrane protein acylation, and plays an important regulatory role in the online stereofatty acid β oxidation and membrane acylation reactions in the body.

People have cloned various acetyl CoA oxidases from different organisms. In 1999, Kiran et al. cloned a new acetyl CoA oxidase from human red blood cells and studied its structure and function. This protein has similar structural and functional characteristics to various known acetyl CoA oxidases. It is highly homologous to various long-chain acetyl CoA oxidases in the protein sequence of red blood cells, and also plays an extremely important role in various fatty acid metabolism processes such as fatty acid beta oxidation and red blood cell membrane acylation.

PH stability of acetyl CoA oxidase

CN201310728420.7 uses acetate, phosphate, Tris, and glycine/NaOH buffer solutions to adjust the pH from 4.0 to 10.5 and determine the pH stability of acetyl CoA oxidase. As shown in the figure below, the optimal pH for acetyl CoA oxidase is 9.5. The following figure shows the effect of different pH buffer solutions on ACS1 activity; （-◆-：Acetate； -■-：Phosphate； -▲-：Tris； -X -: Glycine).

Application of Acetyl CoA Oxidase

CN201811336556.2 discloses a serum free fatty acid content determination kit and method based on microcalorimetry. The reagents of the kit include reagent 1 composed of Tris, HCl, and water, reagent 2 composed of acetyl CoA oxidase, ATP, MgCL, CoA, and DTT, reagent 3 composed of pyrophosphate enzyme, reagent 4 composed of ascorbic acid, and reagent 5 composed of ammonium molybdate, antimony potassium tartrate, water, and concentrated sulfuric acid; The principle of this method is to use the pyrophosphate produced during the decomposition and synthesis of acyl CoA by pyrophosphatase to produce orthophosphate, and then indirectly determine the content of free fatty acids by measuring the orthophosphate content using molybdenum antimony colorimetric method. The present invention improves the conventional enzymatic method, reduces the measurement cost, simplifies the measurement steps, and has lower instrument requirements and costs compared to traditional measurement methods. It meets the measurement conditions of ordinary laboratories, has a lower detection limit, a wide range of applications, stable color development, and good repeatability.

Desheng is a professional manufacturer of enzyme preparations, capable of producing a variety of enzyme preparation products. The enzyme preparation products provided are mainly used as reagents

Box testing raw materials, advantageous products include alpha glucosidase, glucose oxidase, cholesterol esterase, and acetyl CoA oxidase. The raw materials of Desheng enzyme preparations have higher enzyme activity compared to industrial grade enzymes. The company will transport them in ice packs during transportation to ensure the enzyme activity of the products.