Enzyme Literature Review

Boston Pearson). Enzymes work by lowering the activation energy of the reaction making the reaction produce faster. Enzymes begin to catalyze chemical reactions with the binding of the substrate to the active site on the enzyme. The products are released from the enzyme surface to regenerate the enzyme for another reaction cycle. The active site has a unique geometric shape that is complementary to the shape of a substrate molecule, similar to the fit of puzzle pieces.

Substrate concentration basically means the amount used for the substrate. The substrate in our experiment was 0.1% hydrogen peroxide. The 0.1% is the concentration amount. Just like temperature and pH, substrate concentration can speed the reaction only up to a certain limit. When we mixed pH 3 enzyme tube with substrate tube, we used 0.3 mL of hydrogen peroxide, but if we were to increase the amount, then the experiment would have been faster.

Temperatures that are too high denature the enzyme and halt the enzyme’s activity (2). Catalase denatures starts to denature at fifty five degrees Celsius (2). Reactions in the human body produce hydrogen peroxide as a product (1). Since hydrogen peroxide is poisonous to the human body, catalase catalyzes hydrogen peroxide into water and oxygen (2 H2O2 → 2 H2O + O2) (1). According to the collision theory, a reaction can only occur if particles collide with sufficient energy to overcome the activation energy and with correct geometrical orientation (3).

The competitive inhibitor that was added was lactose. We predicted this because competitive inhibitors block and bind to the active site so it will slow down the binding of the desired substrate. An alternative hypothesis that came up was that the reaction of substrate would stay consistent as if no inhibitor was added. The enzyme could reject the inhibitor if it does not fit in the active site, causing the substrate to bind as it normally would. Our results showed that with the addition of lactose, the reaction did slow down a considerably

Through catalyzation, the process of speeding up chemical reactions, enzymes attach to a substrate/molecule and break it down so that it can be used throughout the organism. Enzymes break down substrates in a very efficient way; through an assembly line (3). One enzyme starts off by attaching itself to a substrate at the active site, where the two undergo chemical reactions.

It takes non-acidic potassium iron out of the stomach and replaces it with an acidic hydrogen ion, which makes things acidic. By putting more hydrogen ions into the stomach, the pump makes its contents more acidic. But acid secretion into the stomach stops when a person takes a proton pump inhibitor that stops the proton pump from working. PPIs stop cells in the lining of the stomach producing too much acid. This can help to prevent ulcers from forming or assist in their healing process.

Over the weeks of testing, within each day there consisted systematic errors that would result in increased or decreased values specific to those conditions. This included the calibration of the pH probes, as well as the temperature and location of the trials. Trials on hotter days or under the sun will increase in temperature quicker, affecting the reliability of that result. Over the coming days of trials, the systematic error adds inconsistently until the error becomes random on a global view. Other indeterminate random error consists in the apparatus and measuring accuracy, fluctuating at half the measurement of the lowest measurements made.

INTRODUCTION: Arginase is an enzyme- enzymes are biological catalyst which drives a reaction at the speed of life. Arginase is a hydrolase, hydrolases catalyze hydrolysis reactions, this is determined via the E.C number (Nelson and Cox 2008). Arginase has the EC number is 3.5.3.1 (Schomburg 2015). The enzyme ‘commission number’ is the arithmetical classification that is used for enzymes which indicates the chemical reaction they catalyze. EC 3 are hydrolases, which forms two products from the substrate via hydrolysis.

In response to this decline, pancreas liberate a second islet hormone, glucagon, produced by alpha cells which works opposite to insulin and help the body to regulate the utilisation of glucose and fat. When blood sugar level drops a few hours after eating, the production of glucagon in the pancreas is triggered that stimulates the liver to convert stored glycogen into glucose and release back them into bloodstream. This process is known as glycogenolysis. In addition to the conversion of glycogen, glucagon also inhibits the liver from intake of glucose from the bloodstream and keeps glucose levels stable during hypoglycemia. Glucagon also causes the liver to undergo gluconeogenesis, a process that allows it to absorb non-carbohydrates substrate, amino acids, from the blood and convert them into glucose.

Enzymes are proteins that catalyze chemical reaction, and they work best at their optimal conditions (optimum pH, temperature etc.) but when the environment is not close to the optimum conditions, the enzymes denature and do not function anymore1. An excellent example would of the effect of temperature on yeast fermentation would be that the bacterial cells if exposed to very high temperature (above the optimal) would no longer function since their enzymes are denatured. The yeast would produce the most Carbon dioxide in the optimal temperature (45 °C ±1/°C) and other temperatures below the optimal temperature would not produce sufficient Carbon dioxide and any temperature above will produce too much that it will lead to the sinking of the bread and death of yeast because its enzymes have been denatured, therefore the reaction will stop. The bread will certainly sink if is not exposed to the right temperature the yeast will not ferment

Introduction: Enzymes are needed for survival in any living system and they control cellular reactions. Enzymes speed up chemical reactions by lowering the energy needed for molecules to begin reacting with each other. They do this by forming an enzyme-substrate complex that reduces energy that is required for a specific reaction to occur. Enzymes determine their functions by their shape and structure. Enzymes are made of amino acids, it 's made of anywhere from a hundred to a million amino acids, each they are bonded to other chemical bonds.

Observing the effects of a catalyst on an enzyme’s rate of reaction Leong, M., Kim, E., Nair, A. Achilly, K., 9/22/2015 Introduction: An enzyme is a protein that acts as a biological catalyst. A catalyst increases the rate of reaction by reducing the activation energy required (Reece 2005). Catalase, an enzyme produced by most living organisms, catalyzes the decomposition of H2O2 in our bodies in order to maintain homeostasis. Enzyme activity involves the binding of an enzyme to a substrate at its active site. Each active site is different and unique to its substrate, which is often thought similar to a lock and key.

6. How would you design an experiment to show how much faster H2O2 decomposes in the presence of an enzyme then it does without the enzyme? Use the same system and just add it with water and compare both of them. 7. Explain why the enzyme is still active even though the liver cells from which you obtained the enzyme were no longer living?

Proteins are considered negative buffers and pair well with hydrogen. An intracellular blood buffer like hemoglobin is used because it binds well with hydrogen ions and carbon dioxide. The venous blood, or hemoglobin that isn’t saturated with oxygen, is a better buffer than arterial blood. The phosphate buffer system is important because it regulates the pH in the cytosol. Dibasic phosphate and ammonia are considered renal buffers.

Beta-3 receptors are located in the fat cells. When taking beta blockers they block B1 and B2 receptors therefore the effects of norepinephrine and epinephrine. By blocking these neurotransmitter effects, beta blockers reduce heart rate, decrease blood pressure, and help blood vessels open up to improve blood flow. (Ogbru & Mark, 2015) This class of medications are important because they the most commonly used medications for cardiovascular diseases. Some of the common diseases that beta blockers treat are angina, heart failure, high blood pressure, atrial fibrillation, and myocardial