Enzyme Lab Report

INTRODUCTION
When engaging in this enzyme experiment, there were various steps that were involved in the process of breaking down starch that was present in the fungal and bacterial amylase. First let’s begin by defining what exactly is an enzyme? Well, an enzyme is a biological catalyst that is produced by a cell, thus allowing for these cells to speed up their chemical reactions. Enzymes are very important to us in our everyday lives, they are needed for all our body functions and can be found in our blood, intestinal fluids, the mouth, and stomach. (Vorvick, 2017). This experiment will help us determine if there is any correlation between optimal temperature and catabolization. In order for chemical reactions to occur, the enzyme must lower its activation energy

Hydrophilic and hydrophobic features as well as shape and charge determine how specific an enzyme is. When enzymes accelerate and they alter the substrates to change the state of transition (Cooper, 2000). There is a model called “lock and key”, in that model if the reactant has the same figure as the active site it can easily bind with the enzyme that is present. Enzymes can alter their shape to better fit substrate molecules, which helps in the binding process of the enzyme and substrate, which is referred to as “induced fit model” (Garcia et al, 2004). Optimal temperatures vary between different enzymes, there are countless amounts of enzymes, each with their precise conditions in which they function smoothly. Depending on what type of environment the organism Is in, the optimal temperature of the enzyme will mirror. When reflecting back to the experiment, the results showed that the Fungal and the Bacterial amylase did not have the same optimal temperature because of its different environments. The moment that the temperature reaches a greater optimal, the active site will start to lose its shape, which is known as denaturing, leading to the substrates not being able to bind