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Effect of enzyme concentration on enzyme kinetics
Effect of enzyme concentration on enzyme kinetics
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More handpicked essays just for you.
Effect of enzyme concentration on enzyme kinetics
Effect of enzyme concentration on enzyme kinetics
Don’t take our word for it - see why 10 million students trust us with their essay needs.
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.
Background: Many people experience excessive gas, bloating, and discomfort in the intestinal areas. While there are other contributing causes, food is the one variable that mainly causes these problems, such as: broccoli, beans, dairy products, grains, etc. Beans, for example, contain oligosaccharides that makes it hard for the body to digest. These carbohydrate rich foods makes digesting difficult because they all contain high-fiber, starch, lactose, etc. Beano® is a product that helps aid in digestion.
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.
The major component of beano, alpha-galactosidase (α-GAL), is a catalytic lysosomal enzyme catalyzes the removal process of an a-galactose molecule from glycopeptides, glycolipids and polysaccharides. It also contains the enzyme that the body doesn’t have to digest the sugar that beans contain, therefore eliminating gas and bloating(RUSH,2013). The temperature of an enzyme determines its efficiency, the higher the temperature the more intercellular collisions take place, and those in turn increase the reactions between enzyme and substrate(Jacobs,2013). This experiment was conducted to evaluate which temperature is most optimal for glucose production where Beano is concerned. To start off groups will take 6 test tubes, labeled 0°c, 21°c,
The substrate for beta-galalactoside is ortho-nitrophenyl-B-galactoside. ONPG is structured similarly to lactose. The purpose of the experiment was to add a competitive inhibitor to observe if the reaction rate would slow down. A competitive inhibitor is when the inhibitor binds to the active site on the enzyme and prevents the binds of the substrate
This lab was designed to study the generation of β-Galactosidase over a 2 lab period, so it got 2 sections; first part was to measure the levels β-galactosidase produced in E.coli K12 cells specifically using IPTG a molecular biology reagent to determine the time of induction of the lac operon. The second part of this experiment was to observe the effects of alternative inducing agents, glucose and antibiotic addition on the induction of β-galactosidase in E.coli K12; this experiments goal was to detect the effect of alternate induction agents, antibiotic and glucose adding on to inducing of β-galactosidase in E.coli. The β-galactosidase is normally switched off in E.coli except in the presence of lactose; the enzyme β-galactosidase breaks down lactose into galactose and glucose. (Matthews 2005). The lac operon or lactose operon is essential for the transportation of lactose in E.coli.
As illustrated in Figure 1 and 2, the volume of gas collected for both glucose and maltose produced similar carbon dioxide at a rapid pace of 0.5 min. The results indicate that there is no significant difference between the metabolic rate of glucose and maltose, due to its incubation time. However, the trials for lactose showed no signs of gas production. As shown in Figure 4, glucose had produced the most gas per minute with an average respiration rate of 6.4 mL/min, while lactose produced a negligible amount of gas of 2.6 mL/min, compared to maltose with an average respiration rate of 5.2 mL/min.
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.
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).
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.
Usually, the microbial enzymes have various potential uses in industries and medicine. The microbial enzymes are also more reliable than plant and animal enzymes as they are more stable and active. Also the microorganisms demonstrate an alternative source of enzymes because they can be cultured in large quantities in a short time by fermentation and owing to their biochemical diversity and susceptibility to gene manipulation. Industries are looking for new microbial strains in order to produce different enzymes to fulfil the current enzyme
ADVANCED GLYCATION END PRODUCTS Advanced glycation end product as an oxidative process that occurred in food perserved or heated the presence of reducing sugars were first observed in early 1900s which non-enzymatically make the food proteins insoluble with yellowish fluorescent products attached to them. This process is known as Maillard reaction named on its discoverer the Louis C. Maillard in 1912 (Finot ., 2005). The Maillard reaction is the one of physiological significance. In vivo, it is also observed that human protein non-enzymatically glycated in the presence of physiologic sugars. One of the best characterized glycation product known to occur in the body is glysocylated hemoglobin.
Introduction Galactosemia is a condition that happens when a naturally occurring sugar called galactose cannot be digested by the body. When galactose cannot be digested, it builds up in the body and causes damage to the liver, brain, eyes, kidneys, central nervous system, and other body systems. Galactose is mainly found in dairy products but is also in many other foods. The diet for galactosemia involves avoiding foods and drinks that contain galactose.
The difference in diastatic malt products and non diastatic malt products is the difference in ezyme activity. Diastatic malt products have a considerable amount of enzymatic activity. The action of B amylase on undamaged/ungelatinised starch is extremely slow. A amylase attacks starch very quick.
INTRODUCTION: Arginase is an enzyme- enzymes are biological catalyst which drives a reaction at the speed of life. Arginase is a hydrolase, hydrolases catalyze hydrolysis reactions, this is determined via the E.C number (Nelson and Cox 2008). Arginase has the EC number is 3.5.3.1 (Schomburg 2015). The enzyme ‘commission number’ is the arithmetical classification that is used for enzymes which indicates the chemical reaction they catalyze.