Alkaline phosphatase is a phosphomonoesterase that produces a free inorganic phosphate group, this enzyme is found in many organisms, both prokaryotes and eukaryotes. Calf intestinal alkaline phosphatase (CIAP) regulates bicarbonate secretion, detoxifies lipopolysaccharides, regulates gut microbes and dephosphorylates proinflammatory nucleotides by removing phosphates from the 5’ and 3’ positions from molecules such as nucleotides, proteins and alkaloids (Singh et al., 2020). It was suggested that magnesium may play a role in enhancing the activity of CIAP however that has not been confirmed. Therefore, this project aims to identify the effect of magnesium ions on the activity of CIAP . We hypothesize that CIAP activity in a 5mM of MgCl2solution will increase with increasing concentration of pNPP substrate, as measured by the Vmax (velocity and efficiency) and Km (affinity) constants through enzyme kinetics analysis. The conclusion obtained from this project is that magnesium does behave as an activator by increasing the Vmax from 0.105 uM/min to 0.164 uM/min.
