Study of Glycation Process of Human Carbonic Anhydrase II and Investigation of Effect of Fasting On Enzyme Activity by Using Spectroscopic Methods

Glycation is the non-enzymatic reaction between the carbonyl groups in sugar and free amino groups in proteins. this reaction leads to changes in structure and functions of proteins. Advanced glycation end products (AGEs) is the final stage in this process, which is highly oxidizing and destructive nature, causing many diabetic complications.

In the present investigation, the effect of fasting upon the glycation process of human Carbonic anhydrase II under physiological conditions (37 °C and pH 7.4) was studied recruiting various techniques including Ultraviolet–visible spectroscopy, fluorescence spectroscopy and CD Spectroscopy. To address this question, different samples of control carbonic anhydrase (without glucose and 3-beta-hydroxybutyrate), carbonic anhydrase with glucose, carbonic anhydrase in the presence of only 3-beta-hydroxybutyrate (BHB) and carbonic anhydrase along with glucose and 3-beta-hydroxybutyrate were incubated for 35 days under physiological conditions.

The results indicate that 3-beta-hydroxybutyrate, which is greatly increased in the body during fasting, functions as an inhibitor of the glycation process and decreases the impacts of glucose binding to the protein and prevents the formation of AGEs and preserve enzyme activity.

Fasting can play an important role in maintaining the health of the body and eliminating the complications of the disease, with a significant increase in the production of 3-beta-hydroxybutyrate as an inhibitor of the glycation process.