1. What are some common risks‚ and vulnerabilities commonly found in the System/Application Domain that must be mitigated with proper security countermeasures? Unauthorized access to data centers‚ computer rooms and wiring closets‚ servers must be shut down occasionally for maintenance causing network downtime‚ data can be easily lost or corrupt and recovering critical business functions may take too long to be useful. 2. If your company makes software to accept credit card payments‚ what standard
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An experiment was run to determine which enzyme (pectinase‚ and cellulase or combinations of the two enzymes) maximizes juice production and would be most cost effective. The proposed hypothesis was if the enzyme‚ pectinase‚ is added to apple juice‚ then the more juice will be extracted than if cellulase were added because pectinase holds the cell wall together and if it is separated apart from each other‚ then the more juice would be able to flow out. The experimental data show that during the ten
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Erin Arroyo Lab report June 11‚ 2013 Biology 123 Professor K Title: Scientific Investigation of the Peroxidase Enzyme & Temperature Abstract: In this lab we tested the effect temperature has on the rate of enzyme activity. The way we figured this out was by taking four different temperatures and testing the different absorbance levels they produced every 20 seconds for two minutes straight using a spectrophotometer. The important part of this experiment was the temperature
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concentration of substrate‚ on the activity of the enzymes. By conducting these three separate experiments also‚ three graphs are able to be obtained where the trend of each factor affecting on the enzyme activity is shown and described clearly. II. Hypothesis Experiment 1 (Effect of Temperature): As the temperature increases‚ the height of the bubble will increase too‚ indicating a faster rate of reaction. Experiment 2 (Effect of pH): Enzymes are affected by changes in pH. Extremely high or
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The objectives of this experiment were to investigate the activity of enzymes‚ components that influence the enzyme’s activity‚ identify an unknown phosphatase‚ influence of inhibitors‚ and determine if inhibition is competitive or noncompetitive. A spectrophotometer evaluated the measurement of color change over a period time due to product being formed. Determining unknown phosphatase and effects from different inhibitors were determined by varying the pH and substrate concentrations. The unknown
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Danny Fish 10/9/11 Chemical Testing To identify An Unknown The hypothesis tested was that depending on the solution presented‚ which would test positive for one of the following‚ proteins‚ carbohydrates‚ or lipids through use of chemical testing. (Sudan IV‚ Benedicts’ Solution‚ Iodine‚ Biuret’s) . In order to gain more information for the hypothesis‚ one must know how to test for said macromolecule. Each of the above stated molecules has their own individual solution that will in turn identify
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hydrogen peroxide and potatoes (enzymes)? Introduction The enzyme used for this experiment is Catalase. Catalase is inside mostly any living organism which uses oxygen. Its job is to break down hydrogen peroxide‚ into oxygen and water. (Formula) 2H2O2 ---> 2H2O + O2 (lab manual). There are limiting factors which if altered‚ can alter the procedure of the reaction‚ such as temperature‚ pH‚ and the concentration of either the enzyme or the substrates. Enzymes are specialized class of protein
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LAB 1: What temperature does the enzyme actually work properly in? (Hypothesis) If the temperature is below 40 but above 20‚ then the liver will show bubbles. If the temperature is raised higher than the optimum temperature‚ then an extreme decline in enzyme activity would occur following by the quick denaturing of the enzyme‚ rendering it is permanently useless. Also about 37°C is body temperature. The liver that was at 25°C had a huge amount of bubbles (a 4 on the scale) and the 0°C
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Abstract The main goal of the enzyme kinetics experiment was to see how the phosphatase-catalyzed hydrolysis of p-nitrophenyl produced p-nitrophenol in the presence of phosphate and fluoride ion inhibitors of various concentrations. The calculated Km constant was found to be 0.22 for all reactions. The Vmax values for each inhibition ion were 0.00986 for the phosphate ion and 0.00436 for the fluoride ion. The inhibitor constant‚ Ki‚ was determined to be 0.0967 for the phosphate ion. The inhibitor
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for 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
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