Discuss enzymes under the following headings:.
Enzymes are biological catalysts because they speed up chemical reactions without being affected themselves. They are composed of protein and have an active site, which is complementary in shape to the enzymes substrate. The primary structure of enzymes is a chain of amino acids linked by peptide bonds, this chain is called a polypeptide chain, and the secondary structure is where the chain folds to form the alpha helix. This folding is allowed by hydrogen bonds. The tertiary structure is further folding of this structure forming globular proteins.
Enzymes either build up large molecules from smaller molecules, synthesis reactions, or break down large molecules into smaller molecules, degradation. Enzymes are specific, so only one substrate can fit into the active site, this is called the lock and key hypothesis.
As the enzymes active site is complementary in shape to its substrate, the enzyme and substrate join together to form the enzyme-substrate complex, the enzyme then moves away from the products of the degradation process. Enzymes control biological pathways both inside and outside of cells, for example, food digestion enzymes.
There are many factors that affect enzyme activity. Most enzymes of the body have an optimum p.H which is neutral or slightly alkaline with the exception of pepsin which has an optimum p.H at an acid p.H 2. Outside this narrow p.H range enzymes do not work as well and some become denatured and do not work at all. Another factor that affects enzyme activity is temperature. At low temperatures the reaction is slow and as the temperature increases so does the rate of reaction, until it reaches its optimum temperature where the enzymes activity has reached a maximum. As temperature then gets higher, the reaction rate slows and the enzyme finally denatures. Gene mutation also affects enzyme activity. These mutations can cause essential metabolic pathways to be stopped as the mutation codes for an "enzyme" of the wrong shape, or an "enzyme" is not present, an example of this is PKU.
Factors that affect enzyme activity. ... The Affect of PH on enzyme activity. A change in pH can also affect enzyme activity. ... Reversible inhibitors usually bind to enzymes non- covalently and irreversible inhibitors are usually bound to the enzyme, therefore permanently disabling the enzyme. ... Enzymes are...
For Boiled and Canned pineapple we knew that the heat denaturalizes the enzyme making it to lost its function so we predicted that the gelatin that contained both of the pineapples would stay in solid since the enzymes couldn't preform its job. ... As a result we have concluded that bromelin enzymes in pineapple's which weren't heated successfully breaks down the animal proteins found in gelatin turning the solid into a liquid. ... As a result the top part of the gelatin came to solid because there wasn't enough bromlein enzymes to break down the animal fat in the gelatin....
The application of enzymes in industry and medicine. Enzyme technology is best described as the technology associated with the application of enzymes as the tools of industry, agriculture and medicine. ... In the absence of enzymes, hydrolysis by digestive enzymes would take more than 30 years. ... Enzymes can be immobilised, i.e., an enzymes can be linked to an inert support material without loss of activity that facilitates reuse and recycling of the enzyme. ... The appeal in enzymes lies in the fact that unlike chemical catalysts, enzymes are environmentally friendly and safe. ...
Enzymes Enzymes are large molecules of amino acids that have various shapes and functions. ... Immobilised enzymes: An immobilised enzyme is an enzyme literally that has been attached to a support that takes the form of small beads. ... Chemical (covalent) attachment of the enzyme to a supporting material. 2. Gel entrapment: the enzyme is mixed with gel-forming ingredients and when the gel forms the enzyme remains "trapped" in the gel matrix. ... The disadvantages of immobilisation are: • losses of enzyme activity can occur during the making of the beads • diffusion of ...
Enzymes are biological catalysts. ... In this case, and enzyme acts as that catalyst on certain other substances. ... There are two certain factors that relate to an enzymes chemical structure. ... The specificity of the enzyme directly relies on the structure, because the structure dictates what the enzyme is compatible with and what it isn't compatible with. The chemical structure of an enzyme relates to the catalytic activity because the active site, a small pocket on the surface if the enzyme, triggers the catalytic process. ...
Enzyme Kinetics Abstract This experiment was performed to determine the factors that influence enzyme reaction rates. ... When reaction flasks reached the appropriate temperature the enzyme was added. ... "This shape is very important to the enzyme's catalyzing efficiency and many environmental conditions can affect the shape of enzymes and thus their efficiency (Neilands, 1955)." ... Enzymes: Units of Biological Structure and Function. ... Outlines of Enzyme Chemistry. ...
Enzymes are used in the production of many things. ... Enzymes are be used to aid in many production processes. In the medical field they use enzymes such as prolactazyme, which breaks down dairy products, as enzyme supplements to treat specific enzyme deficiencies. ... We also use enzymes to help us break down and digest food. Our body uses enzymes to carry out necessary functions and industry can benefit by providing enzymes where there are deficiencies. ...
Malonate ions inhibiting the enzyme succinate dehydrogenase. ... The inhibitors get attached to the active site of the enzyme. It competes with the substrate molecule or for the enzyme. It does not alter the structure of the enzyme. ... A competitive inhibitor competes for the enzyme's attention and a noncompetitive inhibitor stops the enzyme from working. ...
Once the enzyme binds to the substrate, the enzyme will act as a catalyst, speed up the reaction and release the products (Biology 12, pg 50). The rate of Enzyme activity must also be controlled, because excessive enzyme activity can cause such things as cancer and other diseases (Enzymes, 2015). ... Feedback inhibition is when there are a group of enzymes a substrate must go through, changing at each one until the very last enzyme. ... Since the substrate cannot bind to the first enzyme it will not be able to bind to the other enzymes in the chain. ... As it is known, Catalase is an enzyme ...