the outcome of enzyme activity Introduction In this project I will monitor the rate of activity of Catalase. Catalase is an Enzyme which in the right conditions catalyses the decomposition of Hydrogen Peroxide into water and oxygen; 2H2O2 + Catalase >>> 2H2O + O2 Catalase is found in all cells and protects them from Hydrogen Peroxide which is a dangerous waste product that needs to be eliminated. Without Catalase living things could not survive. What are Enzymes? Enzymes are found in the
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INTRODUCTION Enzymes are a protein serving as a catalyst‚ a chemical agent that changes the rate of the reaction without being consumed by the reaction. Enzymes are proteins made up of long chains of amino acids. These form complex shapes. The enzymes are individuals‚ like the different players on a ball team‚ they have different specific structures and jobs. As one ball player may be very tall and one short‚ the specific different shape of the active site on an enzyme is unique and prepares it
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above to save your report) Activity: Enzyme Activity Predictions 1. Sucrase will have the greatest activity at pH 6 2. Sucrase will have the greatest activity at 60 °C (140 °F) 3. Sucrase activity decreases with increasing sucrose concentration. Materials and Methods Effect of pH on Enzyme Activity. 1. Dependent Variable. amount of product (glucose and fructose) produced 2. Independent Variable. pH 3. Controlled Variables. temperature; amount of substrate (sucrose) present; sucrase
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LAB: Substrate Concentration Affecting the Rate of Enzyme Activity: Through the Experiment of Beef Liver Puree and Hydrogen Peroxide Research Question Does different amount of substrate affect the rate of enzyme activities? Purpose To examine how different types of concentration (Hydrogen Peroxide) affect the rate of enzyme activity. Hypothesis We believe that if there is more substrate concentrated‚ then there will be an increase in the rate of enzyme activity. This is because
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BIOLOGY IA A Factor That Will Affect Enzyme Activity The Question Effects on Enzyme activity: investigating the effects of mixing Hydrogen Peroxide with Catalase extracted from potatoes at different temperatures‚ and then comparing the results with the same method‚ except to replace the Potato juice with MnO2 Hypothesis Since enzymes are a type of protein‚ they will be destroyed at high temperatures and activity rates will go down at low temperatures. Also‚ if done at low temperature
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Biology Digestive Enzyme Experiment “Design an experiment in which you will investigate a digestive enzyme’s effect on digestion” Research Question: To determine the effect of enzyme concentration on the rate of digestion. This will be done by increasing the concentration of the enzyme diastase and investigate its effect on the rate of starch digestion. The rate will be determined by the amount of time it takes to completely digest the powdered starch‚ the complete digestion will be indicated by
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AIM The aim of this investigation is to explore the effect of different concentrations of bile salts on the time taken for the lipase enzyme to break down fat. BILE Bile is a brownish bitter alkaline fluid produced by the liver and made by the hepatocytes from water‚ bile salts‚ bile pigments cholesterol and phospholipids and stored in the gall bladder. Bile is directly connected with digestion. It is released sporadically into the small intestine (duodenum) which is part of the gut in order
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Simple Experiments on the Enzyme Catalase Aim: The aim of this practical is to use three different techniques to investigate the effect of different concentrations of the enzyme catalase on the rate of breakdown of hydrogen peroxide. Background information Catalase is an enzyme which is found in all living organisms. This enzyme catalases the decomposition of hydrogen peroxide into water and oxygen. Cells continually produce a poisonous by-product of metabolising‚ called hydrogen peroxide. This
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the effects of temperature on the enzyme activity was that the reaction’s rate would increase as the temperature increased‚ until they go over the optimum temperature where the enzymes denature and the reaction’s rate quickly drops to zero. At 5 degree C the rate is 0.00059mole PNP/min. This then increases to 0.01031mmoles PNP/min at a temperature of 50 degree C. The rate then drops drastically to -0.00215moles PNP/min. This point is where the enzymes have been denatured and have no activity‚ shown
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milk‚ serum and certain tissues such as the liver. This enzyme catalyzes the hydrolysis of α (1-4) linkages in starch by breaking it down to maltose and some glucose. As the starch is broken down‚ the coiled structure of α-amylase is unfolded. Therefore‚ iodine will no longer be able to form the blue complex with the α-amylase. It can be assumed that the decrease in color (absorbance) is proportional to the product formed. In this experiment‚ the absorbance of the starch-iodine complex wil be measured
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