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General role of enzymes
Abstract on enzymes
Environment and enzyme activity
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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. Lactase is an enzyme that breaks down lactose, which is a sugar in milk, a disaccharide made of glucose and galactose . Lactase is present in the mucus lining of the small intestine.Lactose intolerance develops when the small intestine does not make enough of an enzyme called lactase.The body needs this enzyme to digest lactose. The lactase would help prevent gas, cramps and diarrhea for those that are lactose intolerant. The consumption of lactase is very beneficial to those that are lactose intolerant, they can take it as a supplement and it would then allow them to break down lactose and be able to consume Milk and its products without side effects.In the experiments Sucrose was used to the reason for this, is that it is similar to glucose, it is a disaccharide formed from glucose and fructose. The purpose of the following experiments is to study if the specificity of the enzyme and the effect of environment on the lactase functio... ... middle of paper ... ...the lactase concerning the pH level. We hypothesized that enzyme functions are under the influence of environmental factors, in this particular experiment it is pH. In the results, the test tubes with the pH of 4 and 7, yielded color changes with the pH of 7 having the most mg/dL. The results proved our hypothesis, we were right to conclude that because the pH was in between the pH in which the lactase is found, that it would have yielded a reaction. The reason why the pH of 7 yielded the most is because that is the the closets to the pH of the small intestine where the enzyme lactase is found. The significance of the results is that the optimal pH for the biochemical reaction to occur is at the pH of 7 and it would yield the best breakdown of lactose. This fits the bigger picture because it shows that everything must be in balance in order for a successful reaction.
Living organisms undergo chemical reactions with the help of unique proteins known as enzymes. Enzymes significantly assist in these processes by accelerating the rate of reaction in order to maintain life in the organism. Without enzymes, an organism would not be able to survive as long, because its chemical reactions would be too slow to prolong life. The properties and functions of enzymes during chemical reactions can help analyze the activity of the specific enzyme catalase, which can be found in bovine liver and yeast. Our hypothesis regarding enzyme activity is that the aspects of biology and environmental factors contribute to the different enzyme activities between bovine liver and yeast.
For example, if a person had been able to consume lactose products for their life with no problems, but in an unfortunate event had to have a portion of his or her small intestine removed, there would be a change in the number of present lactase enzymes in the stomach. Because the lactase enzyme is stored in the small intestine, the person may now experience lactose intolerance due to the decrease in the presence of lactase. Knowing where the lactase enzyme is stored can aid physicians in understanding what will happen after a procedure or the introduction of a new medication. The experiment was conducted to determine the optimal ph of lactose required to produce the maximum amount of glucose. It was predicted that the optimal ph of lactose would be most efficient at lactose ph 6, and that the lower the ph, the amount of glucose produced would increase
While the tube for specimen Cb turned a tannish white in the lower half of the tube while the top stayed the lavender inoculated tube color. Do to this evidence I determined that both specimens Ca and Cb cannot use the process Casein hydrolysis or Casein coagulation due to lack of soft or firm curds in both tubes. Since there was no casein curds formed, I concluded that specimens Ca and Cb also cannot perform the process of proteolysis. My conclusion is supported by the fact that there was no clearing of the medium. I have also determine that neither of my organisms can make the enzymes rennin, proteolytic or even proteases. I know my specimens cannot produce proteases due to the fact that there was no blue coloring in the tubes which means that the byproduct Ammonia was not produced to increase the pH. Since neither of my specimens can make these enzymes, I concluded that my specimens cannot break down lactose or casein. Although I did learn that specimen Cb can reduce litmus due to the evidence that the lower part of the tube turned a tannish white color with a purple ring at the top. This color change from a purple to a white means that the litmus was reduced turning it clear and leaving the white of the milk to show. Finally I know that specimen Ca cannot reduce litmus due to the fact that the tube had no change in
Lactase is an enzyme found in the digestive system. It is essential to the complete digestion of sugar in whole milk and milk products. Lactase specifically breaks down lactose, a complex sugar. Lactase cannot be absorbed by the body unless it is broken down by lactase into glucose and galactose. According to webMD, “Lacking lactase in their intestines, a person consuming dairy products may experience the symptoms of lactose intolerance…Abdominal cramping, flatulence (gas) and diarrhea can occur when a lactose intolerant person consumes milk products.” ("Lactase Enzyme oral : Uses, Side Effects, Interactions, Pictures, Warnings & Dosing - WebMD", n.d.) Lactase is not recommended for use in CHILDREN younger than 4 years of age. Safety and effectiveness in this age group have not been confirmed. (Kluwer, 2014)
LI was first recognized in the 1960s when researchers found black children responding unfavorably to milk in their diets (Harrison 812). Research led to the discovery that lactose, the major sugar in milk and related dairy products, was undigestible in some people because they were missing the enzyme lactase. Lactase breaks down lactose into its component monosaccharide sugars, glucose and galactose. In people missing lactase, lactose passes undigested through the small intestine. In some people, the undigested lactose passes through the remainder of their systems with no ill effects. In others, however, the undigested lactose becomes viscous and ferments in the colon (Englert and Guillory 903). The thickness of the liquid and the fermentation cause painful cramping, gas and sometimes diarrhea. Besides not being able to digest lactose, these people suffer from malabsorption, which causes them to receive little or none of milk's nutrients (Houts 110).1
Purpose: The purpose of this lab is to explore the different factors which effect enzyme activity and the rates of reaction, such as particle size and temperature.
Background information:. Enzyme Enzymes are protein molecules that act as the biological catalysts. A Catalyst is a molecule which can speed up chemical reactions but remains unchanged at the end of the reaction. Enzymes catalyze most of the metabolic reactions that take place within a living organism. They speed up the metabolic reactions by lowering the amount of energy.
Proteins are one of the main building blocks of the body. They are required for the structure, function, and regulation of the body’s tissues and organs. Even smaller units create proteins; these are called amino acids. There are twenty different types of amino acids, and all twenty are configured in many different chains and sequences, producing differing protein structures and functions. An enzyme is a specialized protein that participates in chemical reactions where they serve as catalysts to speed up said reactions, or reduce the energy of activation, noted as Ea (Mader & Windelspecht).
Alkaline Phosphatase (APase) is an important enzyme in pre-diagnostic treatments making it an intensely studied enzyme. In order to fully understand the biochemical properties of enzymes, a kinetic explanation is essential. The kinetic assessment allows for a mechanism on how the enzyme functions. The experiment performed outlines the kinetic assessment for the purification of APase, which was purified in latter experiments through the lysis of E.coli’s bacterial cell wall. This kinetic experiment exploits the catalytic process of APase; APase catalyzes a hydrolysis reaction to produce an inorganic phosphate and alcohol via an intermediate complex.1 Using the Michaelis-Menton model for kinetic characteristics, the kinetic values of APase were found by evaluating the enzymatic rate using a paranitrophenyl phosphate (PNPP) substrate. This model uses an equation to describe enzymatic rates, by relating the
Enzymes have the ability to act on a small group of chemically similar substances. Enzymes are very specific, in the sense that each enzyme is limited to interact with only one set of reactants; the reactants are referred to as substrates. Substrates of an enzyme are the chemicals altered by enzyme-catalysed reactions. The extreme specific nature of enzymes are because of the complicated three-dimensional shape, which is due to the particular way the amino acid chain of proteins folds.
Lactase, a type of enzyme usually found in the small intestine, breaks down lactose into sugars such as galactose and glucose. People that are lactose intolerant cannot consume anything containing dairy because they cannot break down lactose, a sugar found in milk. Those that are lactose intolerant lack the enzyme lactase. Without lactase, the body does not have the ability to break down lactose, which leads to a person having an upset stomach and diarrhea. Adults are more likely to be lactose intolerant than children because of the metabolic change in the body (Dritsas). The lack of lactase that people have can be compensated by taking pills to help break down lactose that is consumed; with the help of a lactase pill the body can now absorb galactase and glucose properly (McCracken, 481).
Lactose Intolerance Lactose intolerance is the inability to digest significant amounts of lactose, the predominant sugar of milk. This inability results from a shortage of the enzyme lactase, which is normally produced by the cells that line the small intestine. Lactase breaks down milk sugar into simpler forms that can then be absorbed into the bloodstream. When there is not enough lactase to digest the amount of lactose consumed, the results, although not usually dangerous, may be very distressing.
Their table had 15 mL glucose, 10 mL RO water, and 10 mL of yeast which they then placed in an incubator at 37 degrees Celsius. In conclusion, I feel that the absence of RO water in the flask made the enzymes work a little harder than when the RO water was in the mixture of the flask. Comparison #4 is between the Controlled Table and Table #5. The mixture for that table’s flask was 15 mL Sucrose, 10 mL of RO water and 10 mL of yeast, which the flask was then placed in an incubator at 37 degrees Celsius.
Lactose is found naturally in all kinds of milk and milk products as the carbohydrate; it can also be found in certain forms of foods. In a lactose tolerant person, the ileum secretes enzyme lactase, which catalyzes the digestion of lactose to form monosaccharides called galactose and glucose. Under normal circumstances, the body can absorb the simpler forms of sugar into the bloodstream. A deficiency in enzyme lactase causes a state of ineffective lactose breakdown. Two main conditions can cause lactose intolerance. Individuals experiencing a deficiency in lactase and lactose malabsorption are at a higher risk of developing the intolerance (Deng, Misselwitz, Dai & Fox, 2015). Lactose deficiency causes the small intestine to produce insufficient
The Application of Enzymes in Industry and Medicine Enzymes are proteins, made up of polypeptide chains of amino acids. They are biological catalysts to regulate the speed of many processes, and are used in industry and medicine, but in different ways. Enzymes are globular proteins, with their structure held together by hydrogen bonds and can therefore be denatured easily if these bonds are broken. This is because their structure is very important in the way they work. They have an active site, which is the area in which substrates are broken down into product molecules, and if this is altered the enzyme can no longer function.