There are more than one forms of fermentation; yeast fermentation is probably the most common method. This process is used in many everyday products today. Yeast was first discovered in 1676‚ but was used before. It has also led to numerous scientific advances. Yeast expands‚ especially well with a good amount of sugar‚ the more of the amount the greater it expands. Yeast is a single-celled organism‚ a fungus to be more specific. They consume carbohydrates‚ mainly sugars‚ and produce carbon dioxide
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Yeast fermentation Hypothesis - Yeast cells perform fermentation when supplied with a source of energy. Materials Two 250 mL Erlenmeyer flask Water‚ Sugar solution Bromothymol blue solution plastic tubing Rubber tubing Two rubber stopper 50 mL graduated cylinder Medicine dropper Blank slide
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C11356616 Lab Partners Name: Charlotte Weir Experiment Name: Yeast Fermentation Experiment Date: 2nd and 9th November 2011 Submission Date: 23rd November 2011 Title Yeast Fermentation Purpose To allow for fermentation of the yeast‚ Saccharomyces Cerevisiae‚ in Grape and Apple juice. Materials provided Test-tube containing Grape juice and a Durham tube Test-tube containing Apple juice and a Durham tube Plate culture of the yeast‚ Saccharomyces Cerevisiae Sterile swabs Method As per
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Catalase is a common enzyme found in the bodies of all living organisms in contact with oxygen. It is involved in reacting with hydrogen peroxide to convert it into water and oxygen and can do so with millions of hydrogen peroxide particles each second. These types of enzymes have many uses in bodily systems commonly known as proteins that speed up the rate of the metabolic process by regulating the chemical process which helps digest food and break down toxic substances. The most favourable conditions
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Title: Enzyme Catalysis of Hydrogen Peroxide by Catalase Problem and Objectives: How do different temperatures and different levels of pH affect the reaction rate of the enzymes in chicken liver? Demonstrate the activity of an enzyme in living tissue‚ observe the effects of changes in temperature and pH on the activity of an enzyme‚ perform analyses for the presence of an enzyme in tissues‚ and analyzing relationships between environmental conditions and enzyme activity. Background: Cells produce
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trend O2 production and reaction velocity increased with increasing catalase concentration‚ however‚ the 33% percent catalase concentration showed a drop of 0.175 mL O2/s compared to the 25% catalase concentration (figure 1.2). The velocity of 25% catalase was 0.275 mL/s‚ 33% was 0.1 mL/s‚ 50% was 0.435 mL/s‚ and 75% catalase was 0.575 mL/s (figure 1.1). The 50% catalase concentration produced the most O2 overall however the 75% catalase concentration had the fastest initial reaction velocity. Experiment
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Catalase Enzyme Lab Samiya Hussein March 9‚ 2012 Introduction In order to receive the necessary amounts of energy required for daily function‚ the digestive system must break down proteins‚ fats and carbohydrates. In doing so‚ the body produces poisonous chemicals; however‚ the cells aren’t harmed. This is because enzymes are used to break down these chemicals. The name of the enzyme that was the main focus of the lab is catalase. Catalase is responsible for catalyzing hydrogen peroxide
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experiment shows the effects of changing the pH level has on Catalase. As predicted‚ the farther away the pH levels got from the optimum pH (7.2)‚ the lower the reaction rate. At a pH of 7.2‚ the foam of the reaction measures 6cm. At a ph of 3 it measures 2.5 cm‚ at a pH of 5 it measures 2.75 cm‚ at ph 9 it measures 2.3 and at 11cm it measures 2cm. pH measures the hydrogen ion concentration of a substrate. By changing the pH of the catalase‚ the enzyme was denatured. Denaturing is the result of altering
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In this experiment we are trying to determine the effect temperature has on catalase activity. We started out with five test tubes and then labeled them as we went about‚ after we added a catalase extract to each tube. Once added to each test tube they all sat in their respected temperature for ten minutes‚ so they could have a full effect. Once the time was up each was then collected and then we began to shake them from side to side for the foaming to start. When the foam settled‚ we discovered
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enzyme; this is where the magic happens. Substrate is what is being broken apart by the enzyme. In this case‚ the enzyme is catalase and the substrate is hydrogen peroxide‚ or 2H2O2. As the catalase and the substrate interact‚ the substrate is brought into the catalase and broken apart into water and oxygen. This process may be able to happen naturally‚ but the enzyme‚ catalase‚ speeds up the process.
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