One of the most primitive actions known is the consumption of lactose, (milk), from the mother after birth. Mammals have an innate predisposition towards this consumption, as it is their main source of energy. Most mammals lose the ability to digest lactose shortly after their birth. The ability 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 …show more content…
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 …show more content…
These labels indicated the lactose solution that was be placed into the mini-microfuge tubes. The varying lactose ph solutions were obtained. The four miniature pipets were then used, (one per solution,) to add 1mL of the solution to the corresponding mini-microfuge tubes. When this step is completed there were two mini-microfuge tubes that matched the paper towel. Then, once all of the solutions contained their respective lactose solutions, 0.5mL of the lactase enzyme suspension was added to the first mini-microfuge tube labeled LPH4 on the paper towel, and 4 on the microfuge tube. As soon as the lactase enzyme suspension was added to the mini-microfuge tube, the timer was started in stopwatch mode (increasing.) When the timer reached 7 minutes and 30 seconds, the glucose test strip was dipped into the created solution in the mini-microfuge tube for 2 seconds (keep timer going, as the timer is also needed for the glucose strip. Once the two seconds had elapsed, the test strip was immediately removed, and the excess solution was wiped gently on the side of the mini-microfuge tube. The timer was continued for 30 addition seconds. Once the timer reached 7:32 (the extra two seconds accounting for the glucose dip), the test strip was then compared the glucose test strip color chart that is found on the side of the glucose test strip
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.
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)
Lipid metabolism is one source of energy for the human body. We eat food containing one form of lipids, triacylglycerols. Before starting lipid metyabolism, these fats get broken down into droplets by bile salts.Triacylglycerols can be broken into fatty acids plus glycerol via hydrolysis with the help of the pancreatic lipase enzymen and then get used by cells for energy by breaking down even further. Once the pancreas and cells have enough energy and don’t need to absorb anymore, fatty acids get synthesized back into triacylgleryols. The excess triacylglycerols get stored in adipose tissue. Excess storage leads to weight gain and obesity.
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
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
In biology class, we were learning about enzymes. Enzymes are proteins that help catalyze chemical reactions in our bodies. In the lab, we were testing the relationship between the enzyme catalase and the rate of a chemical reaction. We predicted that if there was a higher percentage of enzyme concentration, then the rate of chemical reaction would increase or it would take less time. We placed 1 ml of hydrogen peroxide into four depressions. Underneath the first depression, we place 1 ml of 100% catalase and make 50% dilution with 0.5 ml of water. We take 50% of that solution and dilute with 0.5 ml of water and we repeat it two more times. there were four depressions filled with catalase: 100%, 50%, 25% , 12.5 % with the last three diluted
In dairy products and in milk, there is a sugar known as lactose. In order to digest this sugar, you need the necessary enzyme. There are several different reasons for the inability to digest lactose: primary lactase deficiency, secondary lactase deficiency, congenital lactase deficiency, and developmental lactase deficiency. Cases dealing with primary lactase deficiency are most common. As babies, there are normally more lactase enzymes produced than needed in order to digest lactose. “Worldwide, most humans lose 90% to 95% of birth lactase levels by early childhood, followed by a continuing decline during the course of a lifetime,” (Thorn). By the time children reach about three years old, the production of lactase significantly drops. In some...
The tubes of E. coli in the phenol red lactose broth one with and the other without mineral oil on top were reddish pink, meaning that the pH was alkaline. That would then mean E. coli can not utilize lactose. However, it is know that E. coli can utilize lactose (BioCoach Activity). The E. coli in a phenol red glucose broth with mineral oil on top produced a yellow color meaning it had a low pH and thus created an acid. There was also gas in the tube which meant that it produced a gas. The E. coli in a phenol red glucose broth without mineral oil was red, that would indicate that an acid was not produced. There was also no gas that was produced.
Lactose intolerance is an inherited condition as indicated by a recently distributed survey, as well as complied research that has been collected. The survey results had only a small fraction of people who were lactose intolerant, 10%. However, almost 50% of survey takers family members had intolerance toward lactose. This proves several people are not born with the lactose intolerance activated but eventually with age the trait 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.
The lac operon is a transcriptional control of lactose metabolism in bacteria. The operon contains three transcriptional genes, lac Z, lac Y and lac A, which encodes for β-galactosidase, permease and transacetylase respectively. Lac P and lac O copes for the lac promoter and the lac operator, essential to the functioning of this operon. β-galactosidase converts lactose to allolatose, while permease allow lactose to be transported into the cell. Transacetylase does not have a role in lactose usage. In the absence of lactose, there is no allolactose, converted from lactose by β-galactosidase, to the active regulatory repressor, and thus the repressor binds to the operator and transcription is inhibited, as the RNA polymerase bound to the promoter is blocked. In the presence of lactose, allolactose binds to the repressor, rendering it inactive and unable to bind to the operator, allowing the transcription of the three structural genes.
Often described as “Nature’s Perfect Food”, milk is the foundation of life for all newborn mammals (Velten 10). Milk has played a central role in the American cultural and industrial landscape over the last century, binding farms with urban consumers, placing regulators at odds with producers, and inspiring a constant dance between producers, consolidators, nutritionists and end-users about how it is marketed and sold (Smith-Howard 368). As I have become older I have gained a new yet expected intolerance to lactose. I never used to have a problem when I was little but as food economies are changing, so are our products. By the 1950s, consumers demanded standards for dairy products while also developing a growing concern about health issues caused by dairy fats (Smith-Howard 368). This puts all of us at risk for certain diseases including osteoporosis and heart disease. The females of all mammal species can produce milk but cow milk dominates commercial production. Cow’s milk was initially intended only for baby cows. It is the primary source of nutrition for young mammals before they are able to digest other types of food. Humans are the only species that drink milk after infancy.
Undigested lactose accumulates in the lumen of the small intestine because there is no mechanism for its uptake. This results in osmosis of fluid into the lumen.
Without enzymes, reactions wouldn’t occur and living organisms would die. For instance, the enzyme in the stomach breaks down large molecules to smaller molecules to absorb nutrition faster. Researchers experimented with enzyme activity with a potato extract. Researchers will test enzyme activity by increasing and decreasing pH levels, lowering and increasing temperature, and substrate concentration effects. In the first experiment, researchers hypothesized whether different pH levels would change how much Benzoquinone are created and how will the enzymes function in neutral pH levels than higher and lower levels. Researchers used potato extract and different levels of pH to test their hypothesis. In addition, researchers questioned at what temperature does the greatest amount of potato extract enzyme activity take place in. Researchers then hypothesized that the results would indicate the greatest amount of potato enzyme activity level will take place in room temperature. In this experiment, researchers used potato extract and different temperature levels to test the hypothesis. Moreover, researchers wanted to test the color intensity scale and how specific catechol oxidase is for catechol. In this experiment, researchers used dH2O, catechol solution, hydroquinone, and potato extract. Lastly, researchers tested the substrate concentration and how it has an effect on enzyme activity. In this experiment researchers used different measurements of catechol and 1cm of potato extract. Researchers hypothesized that the increase o substrate would level out the enzyme activity
Experimental Strategy: In this experiment, the yeast being used is called Saccharomyces cerevisiae. This type of yeast follows fermentation which is very unique and can tell how much carbon dioxide is produced by fermentation more accurately compared to cellular respiration. Three test tubes will be filled with a specific volume and concentration of sugar with a certain amount of yeast in each test tube. Two of the three test tubes will have similar concentrations of sugar with different amounts of yeast...