Imobilizing Enzymes

In this lab or experiment, the aim was to determine the following factors of enzymes: (1) the effects of enzymes concentration the catalytic rate or the rate of the reaction, (2) the effects of pH on a particular enzyme, an enzyme known and referred throughout this experiment as ALP (alkaline phosphate enzyme) and lastly (3) the effects of various temperatures on the reaction or catalytic rate. Throughout the experiment 8 separate cuvettes and tubes are mixed with various solutions (labeled as tables 1,3 & 4 in the apparatus/materials sections of the lab) and tested for the effects of the factors mentioned above (concentration, pH and temperature). The tubes labeled 1-4 are tested for pH with pH paper and by spectrophotometer, cuvettes 1a-4a was tested for concentration and cuvettes labeled 1b-4b was tested for temperature in four different atmospheric conditions (4ºC, 23ºC, 32ºC and 60ºC) to see how the enzyme solution was affected by the various conditions. After carrying out the procedures the results showed that the experiment followed the theory for the most part, which is that all the factors work best at its optimum level. So, the optimum pH that the enzymes reacted at was a pH of 7 (neutral), the optimum temperature that the reactions occurs with the enzymes is a temperature of 4ºC or

These results shown from this experiment led us to conclude that enzymes work best at certain pH rates. For this particular enzyme, pH 7 worked best. When compared to high levels of pH, the lower levels worked better. The wrong level of pH can denature enzymes; therefore finding the right level is essential. The independent variable was the amount of pH, and the dependent being the rate of oxygen. The results are reliable as they are reinforced by the fact that enzymes typically work best at neutral pH

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.

Hold the IKI spray bottle 25 - 30 cm away from the paper towel, and mist with the IKI solution.

ith the myosin have been activated by the ATP, they will bind the action binding site.

Enzymes are a key aspect in our everyday life and are a key to sustaining life. They are biological catalysts that help speed up the rate of reactions. They do this by lowering the activation energy of chemical reactions (Biology Department, 2011).

We then tested the last set of test tubes containing milk and lactase, we did this to find which ones would present the most glucose concentration results, when placed in different temperatures, 4°C, boiling and room temperature. What we wanted to know was how far temperature could affect lactase to perform its enzymatic activity. We hypothesized that if the lactase is placed in a high or low temperature outside its active range, the temperatures would have a negative impact on the functions of the enzyme. If the temperature has an affect on lactose then we would see some temperatures in which lactase will be function able. We came to a conclusion that enzymes work at a temperature that is closest to body temperature (25°C); boiling water (100°C) denatures the enzyme, while the enzyme is not able to function properly if

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.

The bond of the molecule substrate is broken by the enzyme. (2) Lactase broke apart the substrate of lactose into different molecules called galactose and glucose. The enzyme takes in substrates to the active zone of the enzyme. Then the substrates interact with each other and create new products and then the products are released. (3) Our hypothesis was that if we take a lactase pill and use it in different temperatures and pH levels it would work best at pH 7 and will become denatured in the boiling water bath.

allows it to bind to the same site on the enzyme (b). But there is no

The purpose of this lab is to examine the specificity of the lactase enzyme to a specific substrate and how it can denature due to the rise in temperature.

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

Enzymes are necessary to chemically change and digest molecules in order to be absorbed and used by the body to function. They are catalysts of the body which increase rate of reaction without undergoing a chemical change, and have active sites where the substrate molecules fit. The substrate has a complementary shape that fits with the particular active site and have various uses, such as rennin for example. Rennin is found in the gastric juice of humans and it begins the digestion of milk. In this experiment, junket tablets containing rennin will be added to a sample of milk, curdle it, and replicate the first stage of its

The purpose of this lab report is to investigate the effect of substrate concentration on enzyme activity as tested with the enzyme catalase and the substrate hydrogen peroxide at several concentrations to produce oxygen. It was assumed that an increase in hydrogen peroxide concentration would decrease the amount of time the paper circle with the enzyme catalase present on it, sowing an increase in enzyme activity. Therefore it can be hypothesised that there would be an effect on catalase activity from the increase in hydrogen peroxide concentration measured in time for the paper circle to ride to the top of the solution.

Most biological reactions require catalysts such as enzymes to accelerate the rate of the product formation. Enzymes are proteins that have highly specific and complex structures that enable them to catalyze reactions in a highly effective and regulated manner. One of the most important biological catalysts is β-galactosidase. β-galactosidase is essential in the breakdown of the substrate lactose. Lactose is a disaccharide found in milk. β-galactosidase catalyzes this catabolic reaction, breaking lactose into two monosaccharides; glucose and galactose. Hydrolysis is used to cleave the oxygen bridge connecting the two sides of the lactose molecule.