Effect of Lead Ions On Bacterial and Fungal Amylase Amylases are enzymes, which hydrolyse starch into Maltose. There are two types of amylase: Alpha amylase that degrades starch, which is a polysaccharide, into fragments 10 glucose residues long. Beta Amylase breaks these down into maltose, which is a disaccharide of two glucose molecules joined together. Both enzymes work by hydrolysis of the glycosidic link in carbohydrates. Enzyme amylase are produced from different sources but in my experiment I will be concerned with Bacterial and fungal amylase. Heavy metal ions cause inhibition of enzyme. Inhibition of an enzyme means either to slow down the rate of reaction, to increase the rate of reaction or both. Inhibitors can slow the rate of reaction in various ways. One way is that it competes with the normal substrate for binding of active sites. . Once it is attached to an enzyme molecule it prevents the normal substrate from doing so. This is known as a competitive inhibition. A quite different inhibition would be is when an inhibitor such as lead ions can attach itself permanently to the active site of the enzyme thereby excluding any possibility of normal substrate taking up its rightful space. So in this case the inhibitors are not competing with each other so this is known as non-competitive inhibition. Inhibition is not confined to be not only confined to substances, which combine with the active sites of enzyme. Some inhibitors combine with the other parts of an enzyme molecule altering the shape in such a way that substances no longer fit with the active sites. In some inhibition active sites can be used ... ... middle of paper ... ...oblems and cause damage to the body. If enzymes are in powdered form then it can cause eye problem. Wear goggles to give protection to your eyes. About harmful liquid solutions getting into your eyes, which can be very irritant so rinse your eyes immediately. Some solutions could also spill in your skin. If this happens rinse your skin immediately. You can reduce the risk by wearing disposable gloves. It is important to maintain cleanliness because minor impurities may ruin a good bio-chemical experiment. It is also very important to label different containers so we do not get the solutions mixed up. This involves less risk as it does not involve anything being heated up so less chance of skin burn. Ethical implications It would not be ethical to use a source of enzymes from animal cell sources.
The effect of a change in PH on enzymes is the alteration in the ionic
Enzymes are biological catalysts, which are proteins that help speed up chemical reactions. Enzymes use reactants, known as the substrates, and are converted into products. Through this chemical reaction, the enzyme itself is not consumed and can be used over and over again for future chemical reactions, but with the same substrate and product formed. Enzymes usually only convert specific substrates into products. Substrates bind to the region of an enzyme called the active site to form the enzyme/substrate complex. Then this becomes the enzyme/products complex, and then the products leave the enzyme. The activity of enzymes can be altered based on a couple of factors. Factors include pH, temperature and others. These factors, if they become
PH can affect the way fermentation occurs due to the chemical differences between acid and alkaline elements, particularly within a solution. In this experiment an enzyme-based reaction was examined that in order to observe this pH trend. The aim of the experiment was to determine how pH affects the yeast fermentation rate by performing the experiment numerous times with a different pH (pH's 3, 5, 7, 9, 11) in different glucose solutions. The hypothesis was ‘If the pH is lower than the neutral point, then the fermentation reaction will occur faster?.’ The experiment conducted was to measure the amount of carbon dioxide (C02) produced by the yeast during fermentation whilst modifying the pH of the glucose solution. To test this every 5 minutes
Many hazards are associated with chemicals in this lab. Most of the chemicals used are irritating when they come in contact with your eyes, skin, or body tissues. Some chemicals are more dangerous, and can be corrosive to your body tissues. In one case, a chemical, when combined with any acids, can produce a toxic gas. In order to protect against these hazards, one must wear safety goggles throughout the entire lab as well as when cleaning up after the lab. Also, one should avoid contact with the chemicals and use extreme caution when handling each of the
Abstract: Enzymes are catalysts therefore we can state that they work to start a reaction or speed it up. The chemical transformed due to the enzyme (catalase) is known as the substrate. In this lab the chemical used was hydrogen peroxide because it can be broken down by catalase. The substrate in this lab would be hydrogen peroxide and the enzymes used will be catalase which is found in both potatoes and liver. This substrate will fill the active sites on the enzyme and the reaction will vary based on the concentration of both and the different factors in the experiment. Students placed either liver or potatoes in test tubes with the substrate and observed them at different temperatures as well as with different concentrations of the substrate. Upon reviewing observations, it can be concluded that liver contains the greater amount of catalase as its rates of reaction were greater than that of the potato.
Affect of the Rate of Reaction of Amylase on Starch and How Its Affected by the Concentration of the Substrate
An enzyme is a protein that is produced by a living organism that acts as a catalyst is a substance that increases the rate of a chemical reaction without itself undergoing any permanent chemical change. Enzymes have an area with a specific shape, called the active site of the enzyme. The molecule on which the enzyme acts is called a substrate. After the reaction has taken place and the products of the reaction leave the active site, leaving the enzyme ready for another reaction . The active site of an enzyme has such a particular shape that only one kind of molecule will fit it. This is why enzymes are specific to their substrate. The digestive enzymes break down food into small particles that get absorbed by the digestive system. These are the compounds that are used for fuel, repair and growth.
I blanked it with 2 cm³ water, 1 cm³ amylase and 3 drops of iodine.
Test-tube C had the best concentration according to the results. Three test-tubes were labelled A-C. Test-tube A had 1ml enzyme solution which was added to test-tube B which had 4ml buffer (pH 5 was used). 1ml of the solution from test-tube B was then added to the test-tube C which also had 4ml buffer (pH 5). Test-tube C was used as the enzyme in all the reactions. Nine test-tubes were taken out of them one was used as the the blank, labelled as test-tube 9. The blank had 5ml buffer (pH 5), 2ml hydrogen peroxide, 1ml guaiacol and no enzyme. Then, 3ml of buffer (pH 3) and 2ml of enzyme were added to test-tube 1. Test-tube 2 had 2ml hydrogen peroxide and 1ml guaiacol. Test-tube 1 and 2 were mixed. The same procedure was used for test-tube 3 as test-tube 1, but this time the buffer was pH 5. Test-tube 4 was prepared the same way as test-tube 2. Then, Test-tube 3 and 4 were mixed. Test-tube 5 was prepared as test-tube 1 but with buffer of pH 7 and test-tube 6 was prepared as test-tube 2. Next, test-tube 5 and 6 were mixed. Last but not the least, test-tube 7 was prepared as test-tube 1 but with buffer of pH 9 and test-tube 8 was prepared as test-tube 2. Then, test-tube 7 and 8 were mixed. The spectrophotometer was set to 470nm and using the blank it was set to zero. The four test-tubes with different pH’s (pH 3, pH 5, pH 7, pH 9) were read
An enzyme can be defined as a protein that acts as a catalyst in a biological system. It increases the rate of reaction by decreasing the activation energy. The catalytic power and specificity of an enzyme can be altered by the binding of certain molecules. These molecules are referred to as inhibitors. An inhibitor works to prevent the formation, or to cause the breakdown of an enzyme-substrate compound. There are two categories of inhibitors. The first being irreversible inhibitors, and the second being reversible inhibitors. Irreversible inhibitors tend to be more tightly bound, covalently or noncovalently (mostly covalently), to the enzyme than reversible inhibitors, which tend to dissociate more rapidly from the enzyme. Reversible inhibitors can be subdivided into three groups: competitive, uncompetitive, and noncompetitive.
The hypothesis is supported by the experiment in that with increased starch concentration, the amylase activity increased each time and the salivary amylase functioned best at higher concentrations of starch. Also, for the most part, the reaction followed the general trend of how at lower concentrations, the increase in reaction rate is greater, while at higher concentrations, the increase in reaction rate is less. Despite some discrepancies in trend, specifically at the 40g/L concentration, figure 1 still displays how the amylase activity eventually reaches a plateau, as mentioned in the hypothesis. From the results it appears that the point of saturation for this reaction is at the concentration 50g/L as the amylase activity rates for 50g/L
1. If gas bubbles form then fermentation occurred. Glucose. Carbon dioxide. The enzyme didn’t recognize the structure of glactose, because of the orientation of the H and OH on the carbon 4 is different than glucose. The enzyme only identifies very specific substances.
The experimental setup began by placing paper under two spot plate and label the short side Temperature (0, 25, 65, 85 Celsius) and the long side Time (0, 2, 4, 6, 8, 10 minutes) for each. Sixteen test tubes was needed to complete the experiment, 4 tubes for each amylase (Fungal and Bacterial) and 8 tubes for the starch component. Four test tubes were labeled BA for Bacterial amylase and corresponding temperatures. The same was done for the Fungal amylase (FA). The other eight test tubes remaining were labeled S with the same corresponding temperatures. 5 mL of 1.5% starch was placed into the tubes labeled FS & BS and 1 mL of bacterial amylase and fungal amylase was deposited into the test tubes that did not contain starch (FA & BA). Next,
· When I have collected my results I will place them in a table like
Enzymes are made of proteins with specific three dimensional shapes that are necessary for proper functioning. They function as catalysts, which means that they increase or decrease the rate at which chemicals react and processes occur in living organisms. Therefore they allow certain chemical reactions to occur at a faster rate then the reactions would normally occur on their own. All catalysts are enzymes, however not all enzymes are catalysts. A catalyst is a substance that accelerates a chemical reaction but does not become part of the end product. Enzymes are important because the rate at which reactions occur depends on them. Thus without enzymes, reactions would occur too slowly to keep a person alive. The basic function of an enzyme is to increase the rate of a reaction, and most enzymes act specifically with only one reactant, called a substrate, to produce products.