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Investigating the effect of enzyme concentration on the activity of trypsin evaluation
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When our group began our experiment we started with the hypothesis: “If the optimal pH for trypsin is 8, then reactions occurring in environments above or below will result in lower proteolytic activity and thereby slow reaction rates.” After testing several pH’s 5, 7, 8, 9, and 11 it is impossible to fully accept or reject our hypothesis that we set especially using the rationale about trypsin in the small intestines. By trypsin being located in the small intestines where the pH is 8 one would believe that any other pH whether above 8 or below 8 would cause for trypsin to have a slower proteolytic activity. The standard deviation showed that although there is a difference in the activity of the trypsin depending on the pH the proteolytic activity did not slow down tremendously outside of a pH of 8. It is possible that because trypsin is naturally located in the small intestines is why the optimal pH is said to be 8. However, it is unclear if trypsin would work better in other parts of the body that have a pH other than 8. which would indicate that it is possible that just because trypsin is located in the small intestines that 8 is …show more content…
The first possible human error could be the fact that we pre-incubated the trypsin and in the body there is no pre-incubation. Secondly when we began the experiment the trypsin was on ice which indicates that the trypsin is initially starting off at a cooler temperature than what it would be at if it was working inside the body. Finally, the temperature in which we used for the water bath. The temperature is one of that main issues because the trypsin went from a cool environment to a room temperature and then to a warm environment so the temperature was never stable and this alone could have a tremendous effect on the proteolytic activity of trypsin. Better control of the temperature could have resulted in more conclusive
Michael Pollan, an American author, journalist, activist, and professor of journalism at the UC Berkeley Graduate School of Journalism (Michael Pollan), writes in his book In Defense of Food, the dangers of nutritionism and how to escape the Western diet and subsequently most of the chronic diseases the diet imparts. In the chapter “Nutritionism Defined” Pollan defines the term nutritionism. Pollan’s main assertion being how the ideology of nutritionism defines food as the sum of its nutrients, and from this viewpoint Pollan goes on to write how nutritionism divides food into two categories, with each macronutrient divided against each other as either bad or good nutrients, in a bid for focus of our food fears and enthusiasms. Finally, Pollan concludes that with the relentless focus nutritionism places on nutrients and their interplay distinctions between foods become irrelevant and abandoned.
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.
a) Urinalysis with significantly increased amounts of blood (via dipstick and sediment), protein, and leukocytes as well as slightly increased bilirubin and slightly decreased pH;
In figure 2, it is clear that the protein was transferred successfully from the gel to the membrane. The blot analysis was performed to detect if the protein was expressed.
trypsin" into the food. Pepsin and trypsin are not only secreted into the intestine at this place, but are also
The pH of stomach acid ranges from 1 to 2 on the pH scale. The stomach constantly produces hydrochlo...
Alpha-1 Antitrypsin Deficiency is a hereditary condition that is passed to children by their parents through genes. The condition may cause serious lung and liver disease in adults and liver disease in infants and children. Most alpha-1 antitrypsin is produced by the liver and when there is a severe lack of protein in the blood, Alpha-1 occurs. Alpha-1 antitrypsin protects the lungs from inflammation caused by infection and inhaled irritants. Alpha-1 antitrypsin cannot be released through the liver at a normal rate because it is abnormal. This causes low levels of Alpha-1 in the blood and build-up of Alpha-1 in the liver, which leads to liver disease in some individuals.
...on dioxide, within the body, affecting the pH balance of the blood. This will then affect proteins within the body, being known as enzymes, which can only function if their surrounding environment is in balance. Any alteration to this environment, will prevent the enzymes from functioning effectively.
Growing up in rural Texas, you have to learn to care for the things that are important to you. There really is not much to entertain yourself with so many adolescents become vulnerable to trouble. Luckily for me, I grew up with the responsibilities that came with growing up on a farm. I had things to care for on a daily basis and for the longest time, the things I cared for most were animals. I exhibited livestock in my youth and this is where I spent the majority of my time. I would come home from football or basketball practice and go straight up to the barn to tend to my animals. Along with feeding and cleaning, I would often administer vaccinations and antibiotics when needed. Because of my interest in medicine and science coupled with my love for animals some could say that I was destined to become veterinarian. The major I chose, animal science, even supported that notion. However, it was not until the summer after my freshman year of undergraduate where I realized it was human medicine that my heart was yearning for.
Investigation on the Enzyme Trypsin An Investigation determining a factor affecting the rate of digestion of gelatin by the protease trypsin. Introduction An enzyme is a biological catalyst, which speeds up reactions. An example of this in the human body is trypsin (a protease produced in the pancreas and used in the stomach), which catalyses the digestion of gelatine, a protein. For this investigation, a photographic film will be the source of the gelatine. I will be able to identify when the gelatine is digested, when the photographic film turns from a dark brown colour, to being transparent.
The effect of a change in PH on enzymes is the alteration in the ionic
= Before conducting the experiment I would conduct a simple test for the protein by placing a sample of the albumen into a test tube and add biurett reagent. This contains copper (II) sulphate and sodium hydroxide.
Moderation is vital in all aspects of life and is necessary for overall health, including with one’s food intake. Protein is one of the many important nutrient building blocks that is necessary for proper growth and good health. However, eating excessive amounts of any nutrient or inadequate amounts, can cause various health concerns. Scientists have been able to estimate the amount of nutrients that the body requires. However, the amount of any particular nutrient varies from person to person, depending on your “age, sex, general health status, physical activity level, and use of medications and drugs” (Schiff 2013). It is also important to remember that consuming the required amount of nutrients that meets your dietary guidelines does not
The exocrine function of the pancreas is that it produces enzymes that aids in the digestion of food. There are three important enzymes that are crucial in helping with digestion. The first digestive enzyme is amylase. Amylase function is to break down carbohydrates. The amylase enzyme is made in two places: the cells in the digestive tract that produces saliva and the main one specifically found in the pancreas that are called the pancreatic amylase (Marie, Joanne; Media Demand, “What Are the Functions of Amylase, Protease and Lipase Digestive Enzymes”). The amylase in the pancreas passes through the pancreatic duct to the small intestines. This amylase in the pancreas completes the process of digestion of carbohydrates. Consequently, this leads to the production of glucose that gets absorbed into the bloodstream and gets carried throughout the body. The next enzyme that aids in digestion of food is protease. While amylase breaks down carbohydrates, protease breaks down protein. Protease breaks down protein into the building block form of amino acids. The three main proteases that it produces are: pepsin, trypsin and chymotrypsin (Marie, Joanne; Media Demand, “What Are the Functions of Amylase, Protease and Lipase Digestive Enzymes”). Pepsin does not occur in the pancreas but it is the catalysis in starting the digestion of proteins. Trypsin and chymotrypsin are the two proteases that occur in