Lab Report

Introduction

All chemical reactions in living organisms are catalyzed by group of unique proteins known as enzymes. They are made up of twisted and coiled polypeptide chains with irregular components which give it a globular shape. The surface of the enzyme is irregular, and there are clefts and crevices between some of the wider convolutions of the polypeptide chain. Depending of the shape, size, charge and other characteristics of the enzyme, various other molecules can fit into these nooks, forming temporary complex with the enzyme molecule. This region where substrate binds with enzyme and where catalysis occurs is called activation site.

For the enzyme to work, it must collide with a substrate. If they collide at the right place, the substrate(s) will then fit into the active site of the enzyme forming enzyme-substrate complex. The reaction, in which the substrate(s) yield(s) a product(s), occurs while the molecules are in the complexed state. Fitting into the active site puts a strain on bonds in the substrate, resulting in breakage or modification of these bonds. This is how enzymes decrease activation energy, and speed up chemical reactions. The enzyme molecule is not altered during the course of this reaction. The product(s) is/are then released from the enzyme, making it available to accept the next substrate molecule(s).

How efficiently an enzyme functions is affected by many different factors: by temperature, chemical environment (e.g., pH), presence of specific cofactors, inhibitors, concentration of substrate and enzyme concentration. The factors studied in this experiment were temperature, pH values, presence of specific cofactors, enzyme concentration, and substrate concentration. The state at which an enzyme works best is referred to as its optimal condition, because the condition favors the most active shape for the enzyme.

As temperature increases, the rate of an enzyme-catalyzed reaction increases as well. However, once the enzyme exceeds...