Literature review Research question is how different temperatures affect the catalase enzyme. What is an enzyme? Enzymes are macromolecular biological catalysts. Enzymes speed up chemical reactions. Substrates are molecules that enzymes could act upon and the enzyme converts the substrates into different molecules known as products.
These conditions may denature the enzyme, decreasing its rate of reaction. A conformational change to the activity site of an enzyme will cause the activity of the enzyme to decline significantly. This is because substrate a change in the conformational of the active site of an enzyme prevents the substrate from binding to the enzyme. Sodium chloride affects the charged interactions interactions between the amino acids of the enzyme, deteriorating the active site of the enzyme. However, the enzyme will only deteriorate if there is a high concentration of sodium chloride and not if S3odium chloride is simply present.
The fastest pH was 6 (total:34.5), and it seems that there wasn’t a large change which resulted in a stable structure. The temperature in our experiment was not very high which didn’t result in denaturation of peroxidase. The temperature seemed to be a constant that didn’t affect the experiment. If the temperature was higher in pH 3 and low in pH 10, then it would cause pH 3 to denature even more which would make the pH 3 total about 4.0. Substrate concentration basically means the amount used for the substrate.
They are proteins that are complexly folded to allow smaller molecules to fit into them; this active site is where substrate molecules bind. Enzymes must collide with one another at a precise position with enough activation energy. The active site must bind to the reacting molecule, or the substrate (1). Enzyme-catalyzed reactions require lower activation energy. The activity of an enzyme is affected by its environmental factors, and any change results in an alteration in the rate of the reaction caused by the enzyme (2).
The function of an enzyme is determined by its structure, thus the order in which the amino acids are in make up the enzymes specific shape. The precise way that the amino acids are twisted and folded creates a distinctive shape of the enzymes active site. This active site is now open for substrates which are reactant molecules. Once the substrates go into the enzymes active site they bond together and then leave the enzyme, making the enzyme ready for another set of substrates. The function of enzymes is to speed up reactions by lowering the amount of activation energy needed to get the reaction started.
What was observed with the addition of hydrochloric acids? What did it do to the enzyme? -With the addition of hydrochloric acid I observed that a part of the bead turned white, while the other transformed into a navy blue Colour, with a pH of 2, hydrochloric acid granted amylase to denature, it partially turned white, because it simplified the starch on the paper the alternative obtained a navy blue Colour, because it did not simplify starch deeming it not to execute its function. Analysis: Once iodine was dropped onto the circle, which was labeled “Water”, it transformed into a dark blue Colour, due to the fact that it didn’t consist of any form of starch. Once iodine was dropped onto the circle labeled “ Saliva”, it transformed into a white/ yellow Colour, due to it granting the starch to break down properly, it transformed white as a result of there being no starch, hence it executed its main action.
Each enzyme has an ideal environment, and if the environment of an enzyme changes, the enzyme’s ability could decrease. A factor that could decrease an enzyme’s ability could be a shift in pH level or temperature. In our experiment, we tested whether the change in pH or the change in temperature affect the function of amylase, which is
This luciferin is a tetrapyrrole and differs to chlorophyll due to the type of metal ions present in its structure. Light emission from Dinoflagellates is pH-sensitive. This is mainly due to two factors. Due to the tertiary structure of the luciferase, a change in H+ ion concentration causes the luciferase to lose conformation, exposing its active site to the luciferin. Also, the luciferin molecule can be protected until the pH is suitable for it to bind to the protein.
Yara Mneimneh Ms. Nasrin Vali Biology 11 B 9. October. 2016 Osmosis Investigation Introduction Osmosis is the passive movement of water molecules across a selectively permeable membrane, from a region of low solute concentration to a region of high solute concentration. Osmosis is different than diffusion, since the net movement of the water is due to the solute concentration rather than the molecules. In this experiment, two types of solutions will be tested to examine the effect on osmolarity.
Introduction 1.1 Aim: To determine the kinetic parameters, Vmax and Km, of the alkaline phosphatase enzyme through the determination of the optimum pH and temperature. 1.2 Theory and Principles (General Background): Enzymes are highly specific protein catalysts that are utilised in chemical reactions in biological systems.1 Enzymes, being catalysts, decrease the activation energy required to convert substrates to products. They do this by attaching to the substrate to form an intermediate; the substrate binds to the active site of the enzyme. Then, another or the same enzyme reacts with the intermediate to form the final product.2 The rate of enzyme-catalysed reactions is influenced by different environmental conditions, such as: concentration