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My aim is to find out how the factor, concentration, has an effect on the rate of enzyme reaction (enzyme: Amylase) at a body temperature of 37°C.

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Introduction

Aim My aim is to find out how the factor, concentration, has an effect on the rate of enzyme reaction (enzyme: Amylase) at a body temperature of 37�C. Background Information An enzyme is a biological catalyst. It is a substance that speeds up a chemical reaction, which all life depends on. Without these enzymes these changes would go very slowly or not happen at all. Amylase is an intracellular enzyme that does its job inside the cell. Its job is to speed up chemical reactions occurring in our cells. They also control the reactions. Extracellular enzymes, once formed, may leave the cell and do its job outside. Amylase works in the mouth cavity, which comes from the salivary gland. It acts on food producing maltose. There is one theory, called the 'lock and key mechanism' to explain how the substrate (enzyme) and reactant (concentration) work together. + + Substrate Reactant 'Complex' Reaction Enzyme Product Enzymes work by reacting with a substrate to form an enzyme-substrate complex. This complex is formed at a particular part of the enzyme molecule, usually at its surface, known as the active site. The complex breaks down to form the products, leaving an unchanged enzyme molecule. Another cycle can then be catalysed. At the active site the enzyme works by reducing the activation energy that substrate molecules need to have before they can undergo the chemical change concerned. Enzymes have five important properties: > They are always proteins. This is one reason we need proteins in our food. > They are specific in their action. This means that each enzyme controls one particular reaction or type of reaction. > Heating destroys them. As they are proteins, they become denatured by heat. Most enzymes stop working if the temperature rises above about 40�C. It is denatured when its bonds holding the tertiary structure breaks. This causes the shape of the molecule to change. The change of the shape will affect its properties. > They can be reused again and again. ...read more.

Middle

Blue/ Black Blue/ Black Light Blue Light Blue Faint Blue 0.6 % Blue/ Black Light Blue Light Blue Faint Blue Faint Blue Digested 0.8 % Blue/ Black Light Blue Light Blue Faint Blue Digested This is not accurate. It only provides a vague idea because of the different shades of colours. In my preliminary work, I used a beaker to heat the starch and amylase enzyme to a temperature of 37�C (because it is body temperature). However, this did not keep the temperature constant. Therefore, in my experiment I shall use a water bath. In my preliminary work I did the above. Therefore, I am going to carry out the experiment fairly, making sure that I do not do what I did as mentioned in my previous practicals. To record reliable results I shall give a colour coding with arbitrary units. This will be more accurate than the above table because it will be helpful when I repeat the experiment. Safety * Carry all substances with care. * Remove loose clothing and tie back loose hair. * Wear a lab coat, safety goggles and gloves. * Avoid getting chemicals on your skin. If you do then immediately rinse the affected area with cold water and seek medical attention. * Amylase is a digestive enzyme. It can be dangerous if it gets on wounds. Therefore, avoid direct contact with it. * Make sure that when you put iodine it does not get on your clothing as it can leave permanent stains. * Do not swallow or drink any substances, as it can be very harmful. * Do not eat or drink during any part of the experiment. * When using matches, be sure to handle them with care. * If a bottle of a chemical is broken on the floor immediately locate and contact the lab technician. * After the experiment ensure to wash your hands thoroughly before touching any part of your body. ...read more.

Conclusion

By this I mean that at exactly 2 minutes, for example, I record the results for all the concentrations at the same time, not a few seconds later. This I did not do. My preliminary work went wrong due to the reason that I did not think about my fair testing. In my rate of reaction graph I came across two anomalous results. The reason for this may be that the results that I took were accurate as I compared the colours to the key of colours. However, the results could have been more accurate if I took closer up photos during the experiment and then scanned them onto computer and then give them arbitrary units according to the resolution. Therefore, I would get more accurate results for my concentration graphs. In turn, this would give me an accurate gradient, which would give me an accurate rate of reaction graph. The results, however, would still not be as accurate as I would like them to be. This is because I will not be able to put the amylase in all at the same time so there will be some variation in the time. As I stated in my fair testing I cannot improve my experiment properly because when measuring concentration or amylase solution there is always a drop left when putting it in a test tube. Therefore, the amount of the concentration or amylase cannot be accurate. I did not get an odd result whilst doing the experiment. However, my results are enough to make a firm conclusion. Although, they are not as accurate as they can be. To improve the investigation further I would provide more time to see exactly when the 0.2% and 0.4% concentrations reach digestion. By this I would be able to see, which one out of them will reach digestion faster. It is very likely that 0.2% will reach digestion faster than 0.4% concentration. This is because it is the lowest concentration used. I could also investigate the effect of temperature and the minimum amount of the enzyme for the reaction to proceed at a faster rate. ...read more.

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