Arianna Diazwightman - Biology Lab Report PID - 5869132 Gabby Vazquez, Catalina Ortega, and Jerry Lab Section 41 Table 5 Lemme Break It Down Ft. Amylase The effects of temperature on the ability of an enzyme to break down starch. Abstract In this lab, the optimal environment for an enzyme was observed in bacterial and fungal amylase. An enzyme is a substance produced by a living organism that is coded by proteins to catalyze chemical reactions throughout the body. Enzymes are what make the chemical reactions in living organisms possible. Enzymes act as catalysts to reactions, they lower the activation energy needed for reactions. However, enzymes require particular environments to function, and without proper conditions, enzymes …show more content…
This was performed by placing test tubes in different temperatures, each with starch and amylase, and then using iodine to test how much starch was hydrolyzed. This experiment was executed in order to understand that each enzyme has an optimal temperature and without that optimal temperature, that particular enzyme would not be able to catalyze any reactions properly. The primary goal of the lab was to understand that if an enzyme is in an environment that is too cold or hot the enzyme will denature, thus being unable to perform its function ( Alberte, et al., 2012 ) It was found that for bacterial amylase, the optimal temperature was 55 °C and in fungal amylase, the optimal temperature was 25 °C. These findings can be applied to a number of commercial applications, and actually, enzymes hold a great amount of industrial and commercial importance. In fact, pancreatic enzymes were patented in 1913, but were later replaced by enzymes from Bacillus subtilis in detergents. Known for being able to retain its shape in temperatures up to 60 °C, this made this enzyme very valuable in the detergent business. Enzymes are also widely used in the food and agricultural business, the chemical industry, analytical methods, pharmaceutical industry, and of course for medical research. Many of these enzymes come in the form of yeast, fungi and bacteria which makes research on these …show more content…
Four test tubes were filled with 1% bacterial amylase and 30mL of .05M phosphate buffer solution. Then four test tubes were filled with 3% fungal amylase and 30mL of .05M phosphate buffer solution. The bacterial and fungal procedures were performed at different times. The bacterial amylase was tested first. The test tubes were then placed in baths of either 0, 25, 55, or 85 °C. They were allowed 5 minutes to acclimate. Then the results at 0 minutes were measured by using a pipette and placing 3 drops of the solution in a spot plate, along with 3 drops of iodine. Then the tube with just starch was mixed with the amylase. This was repeated at all the temperatures. Then the results were obtained using the same methods for the next ten minutes at intervals of two minutes. The whole process was then repeated again with the fungal amylase. Then the results were obtained by observing the spot plates that had the hydrolyzed starch and iodine. Using a color chart with a scale from 1-5 the data was translated into quantitative data, with a 1 meaning that the starch was completely hydrolyzed and a 5 meaning that no hydrolization had
Catalase Activity on Substrate Based On Gas Pressure Production Rate Name of the Class Author’s Name Date Enzymes are organic compounds which act as catalysts and speed up biological reactions in biological organisms. They are not destroyed or changed during the reaction but rather they are used over and over again to catalyze many more reactions. Their activity may be affected and altered by factors such as temperature, substrate concentration, enzyme concentration and Ph.
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.
The effect of pH on the speed of enzyme interaction with substrate chemicals Hypothesis: About pH: If the pH level is less than 5, then the speed of the enzyme reaction will be slower. About temperature: If the temperature stays the same, then the speed of the enzyme reaction will not be completely affected. Background information: The function of enzymes is to speed up the biochemical reaction by lowering the activation energy, they do this by colliding with the substrate.
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. Independent Variable pH 3. Controlled Variables temperature, amount of substrate (sucrose) present, sucrase + sucrose incubation time Effect of Temperature on Enzyme Activity 1.
The iodine test determines the presence of starch in biological materials. It is predicted that, if starch is not present, the solution with iodine remains yellow. However, if starch is present the solution with iodine becomes a blue-black colour. Plants have starch as the storage polysaccharide (glucose units held together by glycosidic bonds) while animals have the equivalent of glycogen. In this experiment, the dark blue colour is visible because of the helical amylose and amylopectin reacting with iodine (Travers et al., 2002).
55 degrees celcius Table 6: Effect of Sucrose Concentration on Sucrase Activity Optical Density 35 g/L 30 g/L 25 g/L 20 g/L 15 g/L 10 g/L 5 g/L 0 g/L 1 1.007 0.974 0.950 0.926 0.849 0.734 0.515 0.003 2 1.002 1.011 0.947 0.937 0.834 0.766 0.496 0.002 3 0.980 0.998 0.944 0.932 0.838 0.754 0.495 0.001 average 0.996 0.994 0.947 0.932 0.840 0.751 0.502 0.002 Effect of Sucrose Concentration on Sucrase Activity 5. State how sucrase activity changes with increasing sucrose concentration. First sucrase activity increases greatly. After 10 g/l sucrase activity continues to increase but at a slow rate until it reaches 30 g/l. At 30 g/l to 35 g/l sucrase activities mostly stayed the same
Enzymes speed up chemical reactions enabling more products to be formed within a shorter span of time. Enzymes are fragile and easily disrupted by heat or other mild treatment. Studying the effect of temperature and substrate concentration on enzyme concentration allows better understanding of optimum conditions which enzymes can function. An example of an enzyme catalyzed reaction is enzymatic hydrolysis of an artificial substrate, o-Nitrophenylgalactoside (ONPG) used in place of lactose. Upon hydrolysis by B-galactosidase, a yellow colored compound o-Nitrophenol (ONP) is formed.
Introduction: Enzymes are biological catalysts that increase the rate of a reaction without being chemically changed. Enzymes are globular proteins that contain an active site. A specific substrate binds to the active site of the enzyme chemically and structurally (4). Enzymes also increase the rate of a reaction by decreasing the activation energy for that reaction which is the minimum energy required for the reaction to take place (3). Multiple factors affect the activity of an enzyme (1).
A scale of zero to five was used to describe the reactions, with zero being no reaction at all, one being a slow reaction, and five being a very fast reaction. The materials used were a test tube rack, six test tubes, a test tube clamp, forceps, a graduated cylinder, four small pieces of liver, one piece of potato, one piece of hamburger meat, approximately forty milliliters of hydrogen peroxide in a forty milliliter beaker, a splint, and matches. An ice bath and boiling water was required for testing, where a hot plate was used to boil the water. Each test tube given a label, which were “cold”, “room”, “hot”, “warm”, “potato”, “meat”, and
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
Bio Chem lab Report 04 Enzyme Biochemistry Group Member: Chan Man Jeun Duncan (16002621) Law Sze Man (16000478) Introduction Enzyme is a protein base structure substance in our body. It works at a biocatalyst that will catalyzing the chemical reaction, which helps to speed up the chemical reaction. Enzyme could only function in specific shape, and the shape of enzyme is depending on the environment, therefore it is hard for an enzyme to function well in an extreme environment. The aim of this experiment is to see can the enzyme functions normally in different environment(pH, temperature and salt concentration) via using starch solution, amylase from saliva, 0.5M HCl solution, 0.5M NaOH solution and NaCl solution, and using iodine solution
Research question What is the effect of temperature Amylase activity? Word count-1453 Background research Enzymes are biological catalysts that speed up a chemical reactions. They do this by decreasing the activation energy(the energy needed to start the reaction) of a chemical reaction. The enzyme present in our saliva is called Amylase. Amylase increases the rate of reaction by decreasing the activation energy needed to hydrolyse the starch molecules.
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
Along with being found in plants, they are also present in liver cells, kidney cells, leukocytes and erythrocytes. For the concentration of enzyme experiment, the hypothesis was if the concentration of an enzyme increases, then the enzyme activity will increase as well. The hypothesis was proven to be true, because there are more enzymes to react with substrates. For the enzyme—factors affecting, the hypothesis concluded was if the temperature increases, than the enzyme activity will increase. This however was proven wrong, because enzymes become unstable at higher temperatures.
In order to utilize casein, bacteria cells secrete proteolytic exoenzymes (amylases, proteases, pectinases, lipases, xylanases and cellulases) outside of the cell that hydrolyze the protein to amino acids. The amino acids can then be used by cells after crossing the cell membrane via transport proteins [169]. Starch hydrolysis test is used to differentiate bacteria based on their ability to hydrolyze starch with the enzyme α-amylase or oligo-l, 6-glucosidase. These enzymes hydrolyze starch by breaking the glycosidic linkages between the sugar subunits. It aids in the differentiation of species from the genera Corynebacterium, Clostridium, Bacillus, Bacteroides, Fusobacterium and members of Enterococcus [170].