[Study of hydrolysis of aminoalcohol ethers, phenol and choline under the action of horse blood serum cholinesterase].

The research article investigates the process of breaking down various types of ethers including phenol and choline by the enzyme cholinesterase found in horse blood serum. It was found that the length of the chain in the aminoethers and the hydrophobicity of the molecule had effects on the efficiency of enzymatic hydrolysis.

Study of Hydrolysis Process

• The study primarily focused on the hydrolysis of different types of ethers, particularly phenol and choline, under the influence of an enzyme known as cholinesterase found in the serum of horse blood.
• These ethers ranged from those of saturated and unsaturated alcohols to others.

Effects of Chain Length

• The reactivity towards enzymatic hydrolysis was observed to decrease when the chain length of the alcohol residue in the benzoic acid aminoethers increased.
• Specifically, if the chain length is equal to 4, the compound becomes a nearly ineffective substrate for the hydrolysis process.

Role of Hydrophobicity

• Another important finding in the research is the role of hydrophobicity in the acyl residue of the ether molecule.
• Any increase in the hydrophobicity of the residue was discovered to cause a decrease in the maximum rate (Vmax) and the Michaelis constant (Km), affecting the overall enzymatic activity.

Hydrophobicity in Cholinesterase Substrates

• In the case of cholinesterase substrates specifically, the hydrophobicity of the molecule was found to increase non-productive absorption on the active surface of the enzyme, thereby reducing the rate of hydrolysis.

Cholinesterase Activity with Aminobutynol Benzoates

• One of the key findings revealed that aminobutynol benzoates undergo hydrolysis by cholinesterase at a quicker rate when compared to the ethers of corresponding aminobutanols and their homologs.