Amylase Lab Report

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.

There are certain ways to identify an enzyme by the name for each, for example they usually end with the suffix -ase. For instance, amylase (present in saliva), lipase, or protease. Enzymes were first discovered in the mid-19th century by a chemist Louis Pasteur. Louis realized that the enzymes were responsible for converting grapes into wine during the fermentation process. It is because of this that they were originally known as “Ferments” (Enzymes. 2011).

The best conditions are cold temperature, high concentration and a high pH.The conditions would be different for different enzymes because all proteins are different. 6. How would you design an experiment to show how much faster H2O2 decomposes in the presence of an enzyme then it does without the enzyme? Use the same system and just add it with water and compare both of them. 7.

The results for my organism Escherichia coli consist of performing several tests to determine the organism’s characteristics. One of the tests I chose to perform is a starch hydrolysis test this is a differential test to help determine if the organism can produce enzymes amylase used absorb starch. This test helps to determine if E. coli can break down starch, and if it can we know that it has the ability of producing coenzymes called Amylase use in breaking down glucose bonds. If the organism can break down glucose then it produces a necessary enzyme called amylase used in breaking sugar bonds apart because they are to large to enter the cells. To determine the results in this test iodine is used after the medium has been inoculated and incubated so that the organism has time to absorb the starch in the plate.

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.

1% glucose, 1% maltose and 1% lactose all progressively get positive results by changing colours to reddish brown at the end of this experiment. In this case the aldehyde functional group that is present in the products (monosaccharides and some disaccharides) in this reaction is able to reduce copper in the presence of alkali and this produces colour changes while converting to an aldose sugar. Honey is made of fructose and glucose which instantly turned brown after the test-tube was placed in the boiling water because of its active aldehyde and carbonyl group. The copper (II) sulphate present in the Benedict’s solution reacts with electrons from the aldehyde group which results in a redox reaction to from cuprous oxide, a red brown precipitate that seen in all of the above mentioned solutions (Hill, 1982). Beer also gave positive results because it contains aldehydes and ketones (i.e. acetone, trans-2-butenal, furfual) during its beer production process where the sugars are converted through fermentation (Hill, 1982).

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

By using a spectrophotometer to measure absorbance at 420 nm, the rate of enzyme activity after all reactions have come to a stop can be

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

Having been put in a group according to a Belbin questionnaire, concurring to a score, a role is given, which was applied during the experiment. In this group activity, I worked with other students to investigate the effect of temperature on turnip peroxide enzyme. Taking a look at the experiment as a group a decision was made on who does what, so that we are prepared to start the experiment as soon as we settle into the lab. We worked as a team to plan and carry out an investigation, having coming up with instructions as a step to step of how to do the experiment. Carrying out an experiment with a group to investigate enzyme peroxide from turnips, this enzyme helps with the division of hydrogen peroxide developed in the cells during aerobic

5 water bath were set up each to10 °C. (5 were used do the experiment faster) 5 cm3 of starch solution were added into the 5 test tubes that were labeled test tubes. Then 5 cm3 of amylase enzyme was added into the other 5 test tubes that were labeled. Put one of the starch solution test tube (preferably the one labeled 1) and one of the test tube containing amylase into the water bath (10 °C).

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

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.

Starch is the storage form in plants and glycogen is the storage form of glucose in animals and in animals as glycogen, for times when the organism will need it [1].  The structure of glucose has following components[1]: 1. There are 2 basic functional groups: one of them is aldehyde and other is hydroxyl groups. Because of the presence of these two polar functional groups, glucose (and other monosaccharides) is highly soluble in water (1.5 g/mL at 25 ºC).

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