![]() ![]() Methods Temperature experiment Microfuge tubes were labelled with 0, 40, 60, or 100. Thirdly, since lactase is specific the the substrate lactose (Lactose Intolerance and Health, Evidence Report/Technology Assessment Number 192) we hypothesized that lactose would have a higher metabolic rate than maltose.įinally, since EDTA is most commonly added cofactor to laboratory solutions to bind and remove metal ions from the solution in order to slow undesired enzymatic reactions (Unit 7: Enzymes lab) we assumed that the breakdown of lactose into glucose by lactase was a desirable reaction and that EDTA would, not inhibit, but enhance the reaction. Since lactase is formed in the small intestine and the body temperature (~ 40 degrees C) is it’s optimal temperature and the normal pH of the small intestine is it’s optimal pH (pH=8) we also hypothesized that moving in either direction away from the norm would hinder the production of glucose. We hypothesized that lower temperatures would cause the enzyme to slow down and at higher temperatures it would unravel or go through denaturation, causing it to cease activity. The product that was measuring to determine the enzyme’s performance was glucose, a monomer or small molecule, of the polymers, consisting of bound monomers, lactose and maltose. ![]() The environment’s pH can range from 1-14, 7 being neutral, 7-1 being more and more acidic towards 1, and 8-14 being more and more basic towards 14. Lactase’s effectiveness was studied in an environment with differing temperatures, pHs, and while placed with a cofactor, an enzyme catalyst assistant. The main objective of this lab was to take the enzyme lactase and observe how well it acts as a catalyst to the substrates lactose and maltose while in varying environments. Once the product is released from the active site the enzyme returns to it’s original form. ![]() The substrate is then metabolized or broken down, resulting in a product, which can be utilized to energize cells. We Will Write a Custom Essay Specifically ![]()
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