Lab #6: Specificity of Enzyme Lactase Laboratory Report Introduction Enzymes are biomolecules that catalyze or assist chemical reactions. ("Enzyme Information - Disabled World", n.d.,) Without enzymes it would be impossible for an organism to carry out chemical reactions. Enzymes are proteins that carry a chemical reaction for a specific substance or nutrient. For example, the digestive enzymes help food to be broken down so it can be absorbed. Enzymes can either initiate the reaction or
to digest lactose is determined by the presence of an enzyme called lactase, which is found in the lining of the small intestine. An enzyme is a small molecule or group of molecules that act as a catalyst (catalyst being defined as a molecule that binds to the original reactant and lowers the amount of energy needed to break apart the original molecule to obtain energy) in breaking apart the lactose molecule. In mammals, the lactase enzyme is present
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
nurturance, this ability ceases. This inability to break down lactose is known as lactase non-persistence. Lactase Non-persistence is the wild type in the population surprisingly even though a vast majority of the population is lactase non persistent. Individuals with the ability to digest the lactose found in milk are considered lactase persistent or lactose tolerant. The LCT is responsible for encoding the production of lactase the enzyme responsible for breaking down lactose. However, ultimately the gene
product. Lactase is an enzyme that breaks down lactose, a milk disaccharide of galactose and glucose. Lactase can only be found inside the inner walls of the small intestine. Some people stop making lactase after a certain age, the person then becomes lactose intolerant. Lactose intolerant is when a person is unable to break down the sugar molecules of milk, with symptoms that include bloating, cramps, and diarrhea. The purpose of the experiment is to test the specificity of the enzyme lactase. To test
will activate since it has been inherited. Also majority of the survey takers are North American or European and in high school. Ethnicity, culture and age all have a large impact on whether or not the lactase enzyme is being produce, specifically in mammals. A selective advantage of not producing lactase as an adult is simply saving energy for the body to use elsewhere. Young children need dairy products which contain lactose because it helps their bodies grow by providing healthy nutrients like fats
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. While not all persons deficient in lactase have symptoms, those who do are considered to be lactose intolerant
takes a toll on daily life. Individuals constantly have to be aware of what they are eating as well as how much you are consuming. With this disorder, each person has to learn to manage it correctly. From person to person, the inability to digest lactase varies by how their body handles it and why. Many people believe that the solution to their lactose intolerance problem is to cut dairy out of their diet completely. However, this may be worse for them. Due to a lack of consumption of dairy products
stems from the body’s decreased expression of the LAC gene, which is used to create the enzyme lactase, which begins to diminish with age, starting from as early as the toddler years. Lactase, which is produced in the lining of small intestine, is needed in order to digest the complex sugars presented in milk, namely lactose. As expression of the LAC gene decreases, the resulting enzyme levels of lactase also dwindle. Resulting in the difficulties when digesting these sugars in milk products. The
and activity of life”[1]. They are each very specific, and will only work when a particular substrate fits in their active site. An active site is “a region on the surface of an enzyme where the substrate binds, and where the reaction occurs”[2]. “Lactase is an enzyme that breaks down lactose, the sugar in milk. It is produced by the cells lining of the small intestine. Most people are born producing it, but often make less of it as they age, which causes lactose intolerance the symptoms for this include
The active site exhibits specificity for the substrate of the enzyme. The enzyme should bind and catalyze the reaction for its specific substrates better than with any other substrates. Therefore, the following experiment is testing the ability of lactase to specifically bind and interact with lactose compared to maltose. Materials and Methods: Enzyme Specificity To begin with the experiment, two microfuge tubes were labeled.
Lactose Intolerance are unable to digest lactose because the enzyme lactase is unable to split the sugar molecule into glucose. Lactase is an enzyme that breaks lactose down into galactose and glucose. Lactase functions best between 21 and 48 degrees Celsius (or 70 and 120 degrees Fahrenheit). Cooler temperatures will slow down lactase’s function, whereas high temperatures can denature it or lactase will lose its shape. If lactase is rendered nonfunctional because of temperature or pH extremes, the
Lactase is at its most active during infancy and is vital for the infant's survival when milk is the main source of nutrition. The enzyme then becomes less active after the weaning phase and in adults this decline in activity is referred to as "lactase non-persistence." Conversely, the lactase persistent state describes when a high level of lactase activity is maintained beyond the weaning phase and throughout life (Mandal
digest the main carbohydrate in milk, lactose, after weaning (Ingram et. al, 2008). Lactase is the small intestinal enzyme responsible for breaking down lacrosse into the absorbable monosaccharides glucose and galactose. The presence or absence of lactase is a genetic polymorphism; individual are either lactase persistent or lactase nonpersistent. Individuals who are lactase nonpersistent do not absorb lactase in the intestines, so it travels to the colon, where it is metabolized by bacteria.
Data table 1 Well plate Contents Glucose concentration A 3 drops 5% sucrose + 3 drops distilled water Negative B 3 drops milk+3 drops distilled water Negative C 3 drops 5% sucrose +3 drops lactase Negative D 3 drops milk +3 drops lactase 15+ E 3 drops 20% glucose +3 drops distilled water 110 ++ Questions B. In this exercise, five reactions were performed. Of those reactions, two were negative controls and one was a positive control. Describe which of the reactions were controls and if they
Joshua Valerio Principles of Biology Section: Thursday 08:00 29 October 2015 Discussion 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
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
affected by the mutation. Primary Lactose Intolerance - This is more common in certain races : African, Asian and American Indians. In this case the amount of lactase ( which breaks down lactose ) made by the body decreases after childhood. Meaning that you would need to eat lactose for life, or you could take pills to increase the lactase in your body. Secondary Lactose Intolerance
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
activity. This is good as the products are easy to separate from the enzyme so the enzyme can then be re-used which also reduces costs. Enzyme immobilisation is used a lot in the production of milk for lactose intolerant people. Immobilised lactase hydrolyses the milk sugar lactose to produce glucose and galactose.