Enzymes are protein catalysts that speed up chemical reactions without being used up. They work by binding to specific substrate molecules in a "lock and key" fashion. The enzyme-substrate complex undergoes chemical changes to produce products, and the unchanged enzyme is then released to catalyze another reaction. Enzyme activity is optimized at specific temperatures and pH levels. Investigations can examine how varying these conditions affects the rate of enzymatic reactions by measuring the time taken for an enzyme like amylase to digest starch substrates.
Enzymes are protein catalysts that speed up chemical reactions without being used up. They work by binding to specific substrate molecules in a "lock and key" fashion. The enzyme-substrate complex undergoes chemical changes to produce products, and the unchanged enzyme is then released to catalyze another reaction. Enzyme activity is optimized at specific temperatures and pH levels. Investigations can examine how varying these conditions affects the rate of enzymatic reactions by measuring the time taken for an enzyme like amylase to digest starch substrates.
Enzymes are protein catalysts that speed up chemical reactions without being used up. They work by binding to specific substrate molecules in a "lock and key" fashion. The enzyme-substrate complex undergoes chemical changes to produce products, and the unchanged enzyme is then released to catalyze another reaction. Enzyme activity is optimized at specific temperatures and pH levels. Investigations can examine how varying these conditions affects the rate of enzymatic reactions by measuring the time taken for an enzyme like amylase to digest starch substrates.
Enzymes are protein catalysts that speed up chemical reactions without being used up. They work by binding to specific substrate molecules in a "lock and key" fashion. The enzyme-substrate complex undergoes chemical changes to produce products, and the unchanged enzyme is then released to catalyze another reaction. Enzyme activity is optimized at specific temperatures and pH levels. Investigations can examine how varying these conditions affects the rate of enzymatic reactions by measuring the time taken for an enzyme like amylase to digest starch substrates.
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ENZYMES
What Are Enzymes?
• Enzymes: • Are catalysts that speed up the rate of a chemical reaction without being changed or used up in the reaction • Are proteins • Are biological catalysts (biological because they are made in living cells, catalysts because they speed up the rate of chemical reactions without being changed) • Enzymes are necessary to all living organisms as they maintain reaction speeds of all metabolic reactions (all the reactions that keep an organism alive) at a rate that can sustain life • For example, if we did not produce digestive enzymes, it would take around 2 – 3 weeks to digest one meal; with enzymes, it takes around 4 hours Biological catalysts Biological catalysts • Many chemical reactions(metabolic reaction) can be speeded up by substances called enzymes(catalyst). • Enzymes increase the rate of a chemical reaction without being changed itself. • Without enzymes, the reactions would take place very slowly, or not at all. Examples of enzymatic activity Large molecule of food is broken down into smaller by enzymes These enzymes are also found in plants • Not all enzymes help to break things down. • Many enzymes help to make large molecules from small ones. • For example; phosphorylase enzyme makes starch from glucose. Naming enzyme • Enzymes are named according to the reaction that catalyze. • Sometimes they are given specific names than this. Example; amylase. How Do Enzymes Work? How Do Enzymes Work? • Enzymes are specific to one particular substrate (molecule/s that get broken down or joined together in the reaction) as the enzyme is a complementary shape to the substrate • The product is made from the substrate(s) and is released Enzyme specificity: lock and key model of enzyme activity The lock and key mechanism • The enzyme is like a lock, into which another molecule fits like a key. • Look at figure 5.2 shows how enzymes work The active site • Substrate is the substance which enzyme acts on. All enzymes have active sites. Each enzyme has an active site that fits its substrate. • Enzymes catalyze substrate and products are formed. For example; starch is substrate, amylase is enzyme and maltose is product • Starch amylase maltose
Substrate enzyme product
The active site Enzyme Specificity • Enzymes are specific to one particular substrate(s) as the active site of the enzyme, where the substrate attaches, is a complementary shape to the substrate • This is because the enzyme is a protein and has a specific 3-D shape • This is known as the lock and key hypothesis • When the substrate moves into the enzyme’s active site they become known as the enzyme-substrate complex • After the reaction has occurred, the products leave the enzyme’s active site as they no longer fit it and it is free to take up another substrate Enzyme Specificity • 1. Enzymes and substates randomly move about in solution 2. When an enzyme and its complementary substrate randomly collide – with the substrate fitting into the active site of the enzyme – an enzyme-substrate complex forms, and the reaction occurs. 3. A product (or products) forms from the substrate(s) which are then released from the active site. The enzyme is unchanged and will go on to catalyse further reactions. Properties of enzymes • 1. All enzymes are proteins • 2. Enzymes are made inactive by high temperature. • 3. Enzymes work best at a particular temperature(See figure 5.4 page 52). For example; enzymes which are found in human body usually work best at about 37 centrigrade. Properties of enzymes • 4. Enzymes work best at particular pH. See figure 5.5 page 52) • 5. Enzymes are catalysts: they are not changed, can be used over and over again. • 6. Enzymes are specific: Each kind of enzyme will only catalyze one kind of chemical reaction. Temperature and enzyme activity • Most chemical reactions happen faster at higher temperature. WHY? • However enzymes are damaged by high temperatures. After optimum temperature the shape of enzymes are broken. It is called denaturation. It cannot catalyze reaction any longer. Optimum temperature: The temperature at which enzyme works fastest. Temperature and enzyme activity • For examples; • Human digestive system enzymes have an optimum around 37°. • Plants’ enzymes have optimum around 28°C to 30 °C. • Enzymes of bacteria have optimum as high as 75°C. Ph and enzyme activity • The ph of a solution affects the shape of an enzyme. • Most enzymes are their correct shape at a ph about 7 neutral • If the ph becomes very acidic or very alkaline, then they are denatured. Enzyme Investigations • Amylase is an enzyme that digests starch (a polysaccharide of glucose) into maltose (a disaccharide of glucose). • Starch can be tested for easily using iodine solution. Using iodine to test for starch Investigating the Effect of Temperature on Amylase
• Starch solution is heated to a set temperature
• Iodine is added to wells of a spotting tile • Amylase is added to the starch solution and mixed well • Every minute, droplets of solution are added to a new well of iodine solution • This is continued until the iodine stops turning blue-black (this means there is no more starch left in the solution as the amylase has broken it all down) • Time taken for the reaction to be completed is recorded • Experiment is repeated at different temperatures • The quicker the reaction is completed, the faster the enzyme is working • https://www.youtube.com/watch?v=1Fa2sSIt4_I Investigating the effect of temperature on enzyme activity Investigating the Effect of pH on Amylase Activity
• Place single drops of iodine solution in rows on the tile
• Label a test tube with the pH to be tested • Use the syringe to place 2cm3 of amylase in the test tube • Add 1cm3 of buffer solution to the test tube using a syringe • Use another test tube to add 2cm3 of starch solution to the amylase and buffer solution, start the stopwatch whilst mixing using a pipette • After 10 seconds, use a pipette to place one drop of mixture on the first drop of iodine, which should turn blue-black • Wait another 10 seconds and place another drop of mixture on the second drop of iodine • Repeat every 10 seconds until iodine solution remains orange-brown • Repeat experiment at different pH values – the less time the iodine solution takes to remain orange-brown, the quicker all the starch has been digested and so the better the enzyme works at that pH Investigating the effect of pH on enzyme activity