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Effects of ph on enzyme catalysed reactions
Effects of temperature on enzymes
Effects of temperature on enzymes
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Recommended: Effects of ph on enzyme catalysed reactions
Laboratory 6: Lactase Enzyme Lab Report
Introduction
Enzymes are types of proteins that work as a substance to help speed up a chemical reaction (Madar & Windelspecht, 104). There are three factors that help enzyme activity increase in speed. The three factors that speed up the activity of enzymes are concentration, an increase in temperature, and a preferred pH environment. Whether or not the reaction continues to move forward is not up to the enzyme, instead the reaction is dependent on a reaction’s free energy. These enzymatic reactions have reactants referred to as substrates. Enzymes do much more than create substrates; enzymes actually work with the substrate in a reaction (Madar &Windelspecht, 106). For reactions in a cell it is important that a specific enzyme is present during the process. For example, lactase must be able to collaborate with lactose in order to break it down (Madar & Windelspecht, 105).
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).
The purpose of the foll...
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...remain the same at 4ºC and 25ºC. The final result of this experiment was that glucose was more present in environments of higher temperatures. Our hypothesis and predictions were wrong because lower temperatures do not break down the enzymes because they become denatured. The enzyme activity decreases once the temperature decreases, as well. Enzyme activity increases when there is a rise in temperature, which is why lactose is broken down in much higher temperatures, resulting in a high presence of glucose.
References
Dritsas, Lawrence. (2013). Physiology and the Dairy Market. Financial Times, 1: 10.
McCracken, Robert D. (1971). Lactase Deficiency: An Example of Dietary Evolution. Current Anthropology, 12(4-5): 481.
Madar, Sylvia S., & Windelspecht, Michael. (2014). Inquiry into Life, Metabolism: Energy & Enzymes (pp. 104-107). New York: McGraw Hill.
After conducting this experiment and collecting the data I would have to say that the optimal temperature for enzyme activity would have to be room temperature which in my experiment was thirty-four degrees Celsius. I came to this answer because the glucose test strip showed that at room temperature there was more glucose concentration that at either of the other temperatures. Due to temperature extremes in the boiling water the enzymes could no longer function because the breakdown of lactose stopped. The cold water also hindered the breakdown of the lactose but as the water warmed the enzymes were more active which can be seen in the results for the cold water at 20 minutes B. Describe the relationship between pH and the enzymatic activity of lactase.
The results of this experiment showed a specific pattern. As the temperature increased, the absorbance recorded by the spectrophotometer increased indicating that the activity of peroxidase enzyme has increased.At 4C the absorbance was low indicating a low peroxidase activity or reaction rate. At 23C the absorbance increased indicating an increase in peroxidase activity. At 32C the absorbance reached its maximum indicating that peroxidase activity reached its highest value and so 32 C could be considered as the optimum temperature of peroxidase enzyme. Yet as the temperature increased up to 60C, the absorbance decreased greatly indicating that peroxidase activity has decreased. This happened because at low temperature such as 4 C the kinetic energy of both enzyme and substrate molecules was low so they moved very slowly, collided less frequently and formed less enzyme-substrate complexes and so little or no products. Yet, at 23 C, as the temperature increased, enzyme and substrate molecules
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
The affects of pH, temperature, and salt concentration on the enzyme lactase were all expected to have an effect on enzymatic activity, compared to an untreated 25oC control. The reactions incubated at 37oC were hypothesized to increase the enzymatic activity, because it is normal human body temperature. This hypothesis was supported by the results. The reaction incubated to 60oC was expected to decrease the enzymatic activity, because it is much higher than normal body temperature, however this hypothesis was not supported. When incubated to 0oC, the reaction rate was hypothesized to decrease, and according to the results the hypothesis was supported. Both in low and high pH, the reaction rate was hypothesized to decrease, which was also supported by the results. Lastly, the reaction rate was hypothesized to decrease in a higher salt concentration, which was also supported by the results.
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)
Lactose intolerance (LI) is the inability of some humans to digest the lactose sugar contained in most dairy products and foods made with dairy products. LI has numerous readily apparent physical symptoms such as gas, cramps and diarrhea (Houts 110). More importantly, LI may lead to malnutrition in those people affected because of the loss of milk's important nutrients. Not everyone is affected by LI. In fact, genetic background rather than any other health or cultural factor seems to best predict LI. The inability of humans to digest lactose has enormous health consequences, particularly among the poor populations of the U.S. and the developing third-world countries.
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.
needed to activate the reacting molecules. They are specific that usually act on only one type of substrate, so each of them just. perform one particular reaction. Furthermore, only a small amount of enzyme is needed every time to speed up a reaction. Enzymes are globular proteins that have a precise three-dimensional structure.
However, the decrease varied depending on the temperature. The lowest temperature, 4 degrees Celsius, experienced a very low decrease of amylose percentage. Temperature at 22 degrees Celsius and 37 degrees Celsius, both had a drastic decrease in amylose percentage. While the highest temperature, 70 degrees Celsius, experienced an increase of amylose percentage. In conclusion, as the temperature increases the percentage of amylose decreases; however, if the temperature gets too high the percentage of amylose will begin to increase. The percentage of amylose increases at high temperatures because there is less enzyme activity at high temperatures. However, when the temperature is lower, more enzyme activity will be present, which results in the decrease of amylose percentage. This is why there is a decrease of amylose percentage in 4, 22, and 37 degrees Celsius. In this experiment the optimal temperature is 37 degrees Celsius, this is because this is the average human body temperature. Therefore, amylase works better at temperatures it is familiar
The enzymes have active sites on their surfaces to allow the binding of a substrate through the help of coenzymes to form enzyme-substrate complex. The chemical reaction thus converts the substrate to a new product then released and the catalytic cycle proceeds.
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.
Enzymes work by lowering the activation energy required by molecules to start the reaction off. Enzymes also react (reversibly) with substrates (The molecule(s) that the enzyme is catalysing) this is done by forming Enzyme-substrate complex, which is then broken down into products. As well as being affected by temperature and pH enzymes optimum rate of reaction is also changed by competitive and non competitive inhibitors. Competitive inhibitors inhibit the enzyme so that enzyme-substrate complex’s cant form until it’s unblocked or there is a change in concentration in substrate, this means it takes longer to reach the optimum rate of reaction.
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. In my hypothesis for comparison #4 the measurements would go up again with every 15 min. intervals because of the high tempeture and also be higher that then Controlled Table’s measurements. Hypothesis was right for the first part but was wrong for the second part of the comparison, the measurements did increase in the table’s personal flask but the measurements did not get higher than the Controlled Table’s measurements, see chart below. In conclusion, I feel that the substitution of glucose for sucrose made the enzymes work just as hard as the Controlled Table’s flask but just not as much because sucrose was too strong for the enzymes to
In this lab, it was determined how the rate of an enzyme-catalyzed reaction is affected by physical factors such as enzyme concentration, temperature, and substrate concentration affect. The question of what factors influence enzyme activity can be answered by the results of peroxidase activity and its relation to temperature and whether or not hydroxylamine causes a reaction change with enzyme activity. An enzyme is a protein produced by a living organism that serves as a biological catalyst. A catalyst is a substance that speeds up the rate of a chemical reaction and does so by lowering the activation energy of a reaction. With that energy reactants are brought together so that products can be formed.
In 1985, scholars S. Boyd Eaton and Melvin J. Konner published a paper in the New England Journal of Medicine entitled ‘Paleolithic Nutrition’ that provided insight to he evolution of human nutritional requirements. Although...