on the rate of enzyme activity of Catalase Aim To investigate the effect of substrate concentration (manipulated by increasing concentration of hydrogen peroxide) on the rate of enzyme activity of catalase‚ produced by liver cells‚ on the decomposition of hydrogen peroxide. Introduction Enzymes are biological catalysts that increase the rates of reactions. In an enzyme-catalyzed reaction‚ the substrate binds to the active site and forms enzyme-substrate complex with the enzyme through the lock
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Discovery Restriction enzymes were discovered 40 years ago during investigations into the phenomenon of host-specific restriction and modification of bacterial viruses. Restriction enzymes protect bacteria from infections by viruses‚ and it is generally accepted that this is their role in nature. They function as microbial immune systems. When a strain of E. coli lacking a restriction enzyme is infected with a virus‚ most virus particles can initiate a successful infection. When the same strain
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Rate of Enzyme Activity Justin Hunter G. Kim September 16‚ 2011 September 26‚ 2011 Abstract Catalase is a common enzyme found in nearly all living organisms that is frequently used by cells to rapidly catalyze the decomposition of hydrogen peroxide into less reactive oxygen and water molecules. Catalase is a protein that is most commonly found in the liver. The purpose of this experiment was to determine the effect that changes in temperature and pH have on the function of the enzyme catalase
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During an undercover investigation‚ Officer Cline witnessed Defendant #1 purchase a bag of what appeared to be marijuana and LSD. When Officer Cline approached the dealer (Defendant #2)‚ he was given a similar bag. Following the purchase‚ officers approached and arrested both defendants on narcotics violations. Forensic tests later revealed that the contents of the bag were nothing more than honey and dried leaf matter and rolling paper coated with lime extract. The defense attorneys for both defendants
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MISEP Chemistry 512 – Jacobs Enzyme Catalyst Lab - Formal Report – August 8‚ 2007 ABSTRACT This investigation examined what would happen to the rate of an enzyme-catalyzed reaction if the concentration of substrate changed. We hypothesized that if the concentration increased‚ then the reaction rate would also increase. To test our question‚ we varied a combination of substrate and buffer‚ totaling 6mL‚ with a constant amount of 2 drops of catalyst. The enzyme catalyst‚ peroxidase‚ increased
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Immobilized Enzyme Immobilized Enzyme * Enzymes which are attached to small bead made of alginate are called immobilized enzyme * However‚ whatever the nature of an immobilized enzyme‚ it must comprise two essential functions‚ namely the non-catalytic functions (NCF) that are designed to aid separation and the catalytic functions (CF) that are designed to convert the target compounds within the time and space desired * Immobilized enzymes might meet the increasing demand by manufacturers
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Enzyme Activity Lab Hypothesis: 1] Are enzymes reusable? Yes‚ enzymes are reusable. 2] Which of the following do you think contain catalase? [Manganese dioxide‚ chicken meat‚ apple‚ carrot‚ potato‚ or chicken liver] I think that the manganese dioxide‚ apple‚ and carrot contain the catalase. 3] Would grinding the materials affect enzyme activity? I think that grinding the materials will increase enzyme activity. 4] Would temperature affect enzyme activity? I think that
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scale Enzyme applications 1. Detergents Bacterial proteinases are still the most important detergent enzymes. Lipases decompose fats into more water-soluble compounds. Amylases are used in detergents to remove starch based stains. 2. Starch hydrolysis and fructose production The use of starch degrading enzymes was the first large scale application of microbial enzymes in food industry. Mainly two enzymes carry out conversion of starch to glucose: alpha-amylase and fungal enzymes. Fructose
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Experiment 4: Enzyme Kinetics. Results/Discussion Week 1 Part A: Table 1. Enzyme activity for each assay of 4-nitroaniline formation. Rate of 4-nitroaniline formation Name of trial Abs/sec Abs/min M/min mol/min µmol/min #1 0.00003 0.0018 2.05x10-7 2.15 x10-10 2.15 x10-4 # 2 0.00010 0.0060 6.81x10-7 7.15x10-10 7.15x10-4 # 3 0.00020 0.0120 1.36x10-6 1.43x10-9 1.43x10-3 # 4 0.00030 0.0180 2.00x10-6 2.10x10-9 2.10x10-3
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