ABSTRACT
In addition to being an essential enzyme in many different physiological processes, alkaline
phosphatase (ALP) may be used as a diagnostic tool for a wide range of diseases. A number of
variables affect the rates of enzyme-catalysed reactions, which are the subject of this kinetic
report. The enzyme ALP, which is ubiquitously found throughout the body, hydrolyses
phosphate ester groups under a wide range of pH conditions. Spectrophotometric methods to
measure absorbance were used to determine the concentration of the product. The study
investigated the effects of inhibitors and activators as well as the enzyme’s activity in response to
varying temperatures and pH levels. A competitive inhibitor was seen to regulate ALP activity,
whereas an activator greatly increased enzymatic activity. In order to determine Km and V_max,
we used Lineweaver-Burk plots to analyse the enzyme kinetics in both inhibitory and
noninhibitory environments. While ALP shows strong activity within specific physiological
parameters, our study concludes that deviations might indicate pathological conditions,
highlighting its importance in medical diagnostics. However, in order to prevent exaggerations,
additional study is needed to establish the exact therapeutic applications of the association
between ALP levels and certain diseases.
EXPLORING THE FUNCTION AS AN ENZYME AND A DISEASE BIOMARKER
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EXPLORING THE FUNCTION AS AN ENZYME AND A DISEASE BIOMARKER
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