Investigation of the effect of CMC and alcohol and temperature on thermolysin enzyme stability

Thermolysin enzyme is a heat-resistant metalloproteinase enzyme that binds (EC 3.4.24.4) a peptide containing hydrophobic amino acid leucine and phenylalanine. This enzyme`s immobilization is very important. Enzyme immobilization enhances the stability and reuse of the enzyme and improves the properties of the enzyme and facilitates the enzyme readiness of the product. In order to study the adsorption in the presence of ethanol, different concentrations of ethanol were investigated with enzyme. To investigate the presence of CMC, the enzyme was mixed with different percentages of CMC solution and the casein (substrate) was mixed with different amounts. The effect of CMC and alcohol on the enzymatic solution of CMC was obtained. The effect of CMC and alcohol was investigated. The effect of CMC 2%, 4%, 6%, 8% and 10% with 1% casein on the enzyme was investigated. In this study, it was shown that thermolysin increases activity and stability against temperature rise and then decreases at very high temperatures, and alcohol causes enzyme instability. CMC increases the activity and stability of the thermolysin enzyme, but the presence of CMC can increase the stability and resistance of the thermolysin enzyme to alcohol. CMC has been shown to stabilize thermolysin.