LABORATORY REPORT Activity: Enzyme Activity Name: Natalie Banc Instructor: Elizabeth Kraske Date: 09.26.2016 Predictions 1. Sucrase will have the greatest activity at pH 6 2. Sucrase will have the greatest activity at 50 °C (122 °F) 3.
LABORATORY REPORT Activity: Enzyme Activity Name: Natalie Banc Instructor: Elizabeth Kraske Date: 09.22.2016 Predictions 1. Sucrase will have the greatest activity at pH 6 2. Sucrase will have the greatest activity at 50 °C (122 °F) 3. Sucrase activity increases with increasing sucrose concentration Materials and Methods Effect of pH on Enzyme Activity 1. Dependent Variable amount of product (glucose and fructose) produced 2.
How Does the Type of Enzyme Affect How Much Apple Juice is Extracted From Applesauce Question: How does the type of enzyme affect how much apple juice is extracted from applesauce? Hypothesis: If seven drops of pectinase, cellulase, and a mixture of both are stirred ten times into 100 mL of applesauce and left for 5 minutes, then pectinase will catalyze the apple juice the fastest. IV: Type of enzyme (pectinase, cellulase, mixture of both) DV: Amount of applesauce extracted as measured in mL after 5 minutes Materials Needed: 1.400 Grams of applesauce 2.Pectinase
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
Introduction When a chemical reaction occurs anywhere in the universe, it needs energy. The human body is no exception. For some reactions, the energy required to start the reaction is Enzymes are special proteins designed to assist in the breaking down of macromolecules. They do so by holding the macromolecule in place at the active site, therefore lowering the amount of energy it takes to start the chemical reaction. There are different enzymes for each macromolecule; Pectinase and Cellulase are both examples of enzymes, and were the enzymes tested in this lab.
Enzymes are biological catalysts made of proteins that accelerate chemical reactions by lowering their activation energy therefore increasing the activity rate of the enzyme and more substrates turned into products. The ‘Catalase’ enzyme that was used during this experiment was obtained from peroxisome found in celery which are organelles found in bacteria, plant, and animal cells. It is involved in the breaking down of certain substances and the diminish of reactive oxygen species and that includes hydrogen peroxide (H2O2) which can be a byproduct of the metabolism of oxygen. Hydrogen peroxide is toxic to the cell and so the catalase enzyme is utilised to break down H2O2 to form oxygen molecules and water free of free radicals.
Enzymes consist of an active site, this active site is unique to the substrate which it binds to. The active site is a tertiary structure which defines what substrate can bind to the active site. The active site is therefore highly specific. The structure and function of enzymes are compared to the lock and key hypothesis, where the lock is the enzyme and the key being the substrate. Another theory which has been presented is the induced fit hypothesis, where the tertiary structure in the active site changes slightly when bonded to the substrate to strengthen the bond between the active site and the substrate.
ABSTRACT: The purpose of the experiments for week 5 and week 6 support each other in the further understanding of enzyme reactions. During week 5, the effects of a substrate and enzyme concentration on enzyme reaction rate was observed. Week 6, the effects of temperature and inhibitor on a reaction rate were monitored. For testing the effects of concentrations, we needed to use the table that was used in week 3, Cells.
Some enzymes can make their conversion of substrate to product occur many millions of times faster. An extreme example is orotidine 5'-phosphate decarboxylase, which allows a reaction that would otherwise take 78 million years to occur in milliseconds. Enzymes are usually much larger than their substrates. Sizes range from just 62 amino acid residues, for the monomer of 4-oxalocrotonate tautomerase, to over 2,500 residues in the animal fatty acid synthase. Only small portion of their structure (2-4 amino acids) is involved in catalytic activity.
In 1856, a scientist name claude Bernard has identified lipase [1]. Lipases are serine hydrolases containing G-X1-S-X2-G sequences as the catalytic part of the particle, where G = glycine, S = serine, X1 = histidine, X2 = glutaminic or aspartic acid. Such structure is characteristic also for serine proteases. The knowledge of their 3-dimensional structure plays a significant role in designing and structuring lipases
Enzymes are reliant on their structure to perform their tasks, so when the structure of the enzyme is changed it can no longer perform its task. When the enzyme can no longer perform its function due to a change in structure, the enzyme has been denatured(Meyertholen, Edward). To test whether processing foods effects enzyme activity, bromeliads and jello
It is an important step in restoring health and well-being by helping to remedy to digestive problems. Food (plant) enzymes and pancreatic (animal) enzymes complement to boost digestion and absorption of essential nutrients. Enzymes are protein molecules which are used (like catalysts) by different parts of the body to perform all of its chemical reactions converting substrate into product. Catalysts are simple inorganic molecules. The human body, typically, makes 22 digestive enzymes capable of digesting carbohydrates, sugars, proteins, and fats.
SPECIFIC ACTIVITY MEASURING ENZYME KINETICS Enzymes are proteins that act as catalysts in reducing the amount of activation energy for a reaction to take place, activation energy that is needed for get reactions begins since several reactions. Do not take place at all. If they thermodyanamically possible. Enzymes catalyse specific reaction in a particular site known as the active site.
Introduction: Enzymes are proteins that function as catalysts, meaning that they increase the speed of a reaction without being changed themselves. The enzyme has two main jobs in a reaction that cause the reaction to increase. The first job is to bring substrates (the substances that the enzyme will be reacting on that bind to the active site in the beginning a reaction) together in an orderly fashion so that they can interact during the reaction. It’s second job is to decrease the energy needed for a reaction to take place. These tasks can be completed more efficiently in specific temperatures or with specific pH levels.
All substrates, if not specifically stated, are designated as A,B,C and D. All products are designated as P,Q,R. Different forms of enzymes are represented by E,F,G. E is the form of the enzyme that is free or at least most nearly free of any form of the substrates or products. Kineticists recognize two general mechanism for multisubstrate reactions: Sequential Mechanisms Non Sequential Mechnisms 1. Sequential Mechanisms
