Lactase Enzyme Analysis

The enzyme is a protein that acts as a catalyst, lowering the activation energy needed for reactions to progress in cells. The reaction can still occur without the presence of the enzyme, but at a much slower rate. Activation energy is considered the minimum amount of energy needed for a chemical reaction to occur, yielding products from a given set of reactants. The shape of enzymes determines its function and which substrate the enzyme binds to and catalyzes is determined by the shape of its binding groove. If the shape is lost possibly due to denaturation, the enzyme cannot function anymore. The substrate is the reactant(s) of the reaction that is/are bound by the enzyme. While an active site is a region of the enzyme where binding to substrate

Lactase is at its most active during infancy and is vital for the infant's survival when milk is the main source of nutrition. The enzyme then becomes less active after the weaning phase and in adults this decline in activity is referred to as "lactase non-persistence." Conversely, the lactase persistent state describes when a high level of lactase activity is maintained beyond the weaning phase and throughout life (Mandal, 2013). Based on what I know about the effect of temperature on the enzymatic activity of lactase, if the lactase used in the lab was extracted from human cells, I hypothesize that the enzymes would work according to the human body, at a optimum temperature of 37 degrees Celsius. While I hypothesize that the effect of the pH on the enzymatic activity of lactase it can be used because the optimum pH for it is 2-7, the same as the small intestine. However, if the enzyme was extracted from bacterial cells, the pH would be higher and it could work in the lab. Knowing that lactase is specific for lactose, each enzyme has their own substrate to bind to. I predict that the effect of EDTA will be negative when added to a lactase for a mediated