Latase Lab

Amylase experiment # 2 was done to see how the pH affected the efficacy of the enzyme. First we collected all of the materials that were necessary to make this experiment. We needed five clean test tubes, the following standard solutions, 1% Starch Solution pH 3,1% Starch Solution pH 5,1% Starch Solution pH 7,1% Starch Solution pH 9,1% Starch Solution pH 11

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

-VariablesoIndependent:The temperature of the milkoDependent:The time taken for the milk to solidifyoControlled:The same amount and type of milk usedThe same amount and concentration of enzyme mixture usedThe same test tube sizeResults:-TableAmount of enzyme mixture (mL)Amount of milk (mL)Temperature (oC)Time for milk to clot (min)Ex: 1 Ex: 2 Average2.551060+60+60+2.552034.2036.0035.12.55303.554.203.882.55402.102.252.182.55505.004.454.73Discussion:The experiment showed that changing the temperature did affect the rate at which the milk solidified. At low temperatures of 10oC and 20oC the milk took the longest to solidify and at 10oC did not even go lumpy after an hour. As the temperature increased the speed at which it reacted got faster until it reached around 40oC where the speed began to drop.

PH can affect the way fermentation occurs due to the irregularity of the acidity or alkalinity within the glucose solution. This is an enzyme-based reaction that is susceptible to pH. The aim of this experiment was to determine how pH affects the yeast fermentation rate by performing the experiment numerous times with a different pH of glucose solution which included pH 3, 5, 7, 9, 11. The hypothesis was ‘If the pH is lower than the neutral point then the fermentation reaction will occur faster?’ The experiment conducted was to measure the amount of C02 produced by the yeast going into fermentation, however varying the pH of glucose solution by using different pHs . To test this every 5 minutes the volume of gas in the test tube was observed and recorded until a period of 30 minutes had been. The end results

Background and Introduction: Enzymes are proteins that process substrates, which is the chemical molecule that enzymes work on to make products. Enzyme purpose is to increase the rate of activity and speed up chemical reaction in a form of biological catalysts. The enzymes specialize in lowering the activation energy to start the process. Enzymes are very specific in their process, each substrate is designed to fit with a specific substrate and the enzyme and substrate link at the active site. The binding of a substrate to the active site of an enzyme is a very specific interaction. Active sites are clefts or grooves on the surface of an enzyme, usually composed of amino acids from different parts of the polypeptide chain that are brought together in the tertiary structure of the folded protein. Substrates initially bind to the active site by noncovalent interactions, including hydrogen bonds, ionic bonds, and hydrophobic interactions. Once a substrate is bound to the active site of an enzyme, multiple mechanisms can accelerate its conversion to the product of the reaction. But sometimes, these enzymes fail or succeed to increase the rate of action because of various factors that limit the action. These factors can be known as temperature, acidity levels (pH), enzyme and/or substrate concentration, etc. In this experiment, it will be tested how much of an effect

Enzymes are proteins which can catalyse chemical reactions without changing themselves. The enzyme lipase breaks down the fat in dairy products such as full-cream milk for people who are lactose intolerant. Lipase acts on its specific substrate, lipids produces fatty acids. If enzyme concentration increases, random collisions between the substrates and active sites of enzyme increase due to the increasing amount of active sites which allow more collisions to happen, so the rate of breakdown of lipids to simpler substances will increase. During the experiment, sodium carbonate solution and pH indicator phenolphthalein will be added ahead of

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. While not all persons deficient in lactase have symptoms, those who do are considered to be lactose intolerant.

Lactose is a sugar that can be put into smaller molecules, glucose and galactose. Lactose is when you are not able to digest milk and dairy meaning that the enzyme lactase that breaks down lactose is not functioning properly. ONPG was used as a substitute for lactase because even though it is colorless it helps show enzyme activity by turning yellow. This experiment measured the absorbance ONPG when exposed to lactase within an environment of different salinity’s. The enzyme, lactase, was obtained by crushing a lactaid pill and then was added into four cuvettes. ONPG and salt solution of different concentrations were added and their levels of absorption was measured by a spectrophotometer. The results showed that higher salt concentrations have a lower level of absorption. There were 4 cuvettes and within those cuvettes that solutions within them were being tested and the results showed the more salt solution added with the lactase the lower the absorbance. The less salt solution there was a higher rate of absorbance. The data supported the hypothesis that with increasing NaCl concentration there would be a decrease in enzyme activity.

In part II of the lab six small glass tubes were obtained in a test tube rack. Ten drops of distilled water were then added to test tube 1, five drops to tubes 2-4, and no drops in tubes 5 and 6. Five drops of 0.1M HCl were added to test tube 5 and five drops of 0.1M NaOH to test tube 6. Five drops of enzyme were then added to all tubes except tube 1. Tube 3 was then placed in the ice bucket and tube 4 was placed in the hot bucket at 80-900C for five minutes, the remaining tubes were left in the test tube rack. After the five minutes five drops of 1% starch was added to every tube and left to sit for ten minutes. After ten minutes five drops of DNSA were then added to all the tubes. All the tubes were then taken and placed in the

Enzyme reactions are an important part of any chemical reaction, but any environmental factors that come can cause it to a great change in the reaction. The purpose for this experiment was to see what concentration of NaCl would cause the greatest change of reaction in lactase (enzyme) activity and what concentration would be the greatest change. In order to observe and analyze the change in enzyme activity a spectrophotometer was used to observe the absorption in a 420nm wavelength to look for the absorption maximum in each different concentration. We found that a twenty percent concentration (the highest amount we could use) caused the slowest reaction of lactase activity between all of the concentrations used. To further better the results

“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 nausea, bloating, and diarrhea to name a few. This enzyme is produced

The main purpose of this lab is to identify and separate the main components of milk. To do this an understanding of the properties of these components in needed to separate them from one another. We will be separating the components with their polarity or non-polarity and the temperature at which specific components precipitate. To do this we will be using hot plates, gravity filters and vacuum filters1, water and ice baths, and blot drying.

Lactase is an enzyme that breaks down lactose. Lactose is the sugar found in milk. It is made up of two monosaccharides: glucose and galactose. Therefore it is a disaccharide that needs to break down in order to be digested. However some people are “Lactose Intolerant” or lack lactase in their bodies. This means that they cannot consume lactose-contained food or drinks or they need help digesting it. People who are lactose intolerant must be very selective to make sure that they do not eat food or drinks with lactose. There are pills though, which are purchased by lactose intolerant people. This pill helps the people break down the sugar lactose into its smaller components.

Lactose intolerance occurs when the body has a hard time digesting dairy products. Lactose is a milk sugar and is broken down by enzymes in the intestinal track, allowing the enzymes to be used as an energy source. Lactase is an enzyme which breaks down lactose. Lactose intolerance occurs when the intestine does not contain lactase (Jackson). Low lactose activity in the small intestine, allows undigested lactose to pass into the colon, where the bacteria are able to convert the sugar into hydrogen gas and organic acids. This causes symptoms such as bloating and cramping (“Lactose Intolerance”). The two causes of lactose intolerance are primary lactase deficiency and secondary lactase deficiency. In primary lactase deficiency the level of lactase enzyme falls as a person gets older. This does not allow the person to tolerate the amount of lactose that they were used to. This affects around 70 percent of the population. Secondary lactase deficiency is a temporary condition in which the level of lactase drops due to a problem in a person’s digestive

Abstract – Yogurt is a product of lactic acid and lactose. In order to produce yogurt, milk is pasteurized (at 45 degrees Celsius) and the inoculum is added followed by incubation. Over a period of 7 days, yoghurt fermentation was attempted using lactobacillus cultures. A liter of milk was supplied and plain yoghurt was used as a starter culture as it contains the necessary bacteria to ferment lactose and produce lactic acid. The milk was added to a flask: then boiled, cooled and inoculated. The milk was incubated for a week and all the while the milk was tested for changes in pH, density, mass and physical changes. The values obtained were then used to determine the growth kinetics of Lactobacillus bulgaricus.