Alpha-Amylase

enzyme Amylase, it will not be able to denature the carbohydrates in the potato starch solution after 10 drops because enzymes are very sensitive to pH levels and lowering it too much will compromise its ability to break them down. Experimental design components: Independent variable: We will change the amount of drops of Hydrochloric acid added to the Amylase. ( 5 drops, 10 drops, 15 drops) Dependent Variable: The Amylase’s capability to break down potato starch solution. Control: The Amylase without

Abstract: In the last 10 years, the use of saliva as a diagnostic fluid has become somewhat of a translational research success story. Technologies are now available enabling saliva to be used to diagnose disease and predict disease progression. This review describes some important recent advances in salivary diagnostics and its application in various systemic diseases .This review will also stimulate future research activity. Key word: saliva ,sjogren syndrome Introduction:

The digestive enzyme amylase was analysed in two different species of gastropod (the herbivorous Turbo smaragdus and the carnivorous Cominella adspersa), in order to assess whether diet influences digestive enzyme activity. This was determined by preparing a tissue homogenate from the digestive gland of each of the species and comparing their measured absorbance to that of a standard curve that reflected the relationship between absorbance and enzyme units. Amylase activity (in units of enzyme per

optimally. Methods: The enzymes amylase, pepsin, and trypsin were each mixed with the substrates starch and albumin at pH levels of 2, 7, and 9. At 10 min intervals, the starch mixtures were treated with lugol’s solution and the albumin mixtures with biuret and ninhydrin solutions to determine whether digestion occurred. An unknown enzyme was then added to starch and albumin at the various pH and the same tests were performed to determine the identity of the unknown enzyme.

With both the stock substrate and varying enzyme solutions prepared, the Spec20 spectrophotometer was used to investigate the enzymatic activity of β-Galactosidase through an absorbance-based assay. Using LoggerPro software on the computer to analyze the absorption data, the Spec20 was calibrated before each run with 0.5 mL of the tested enzyme concentration at an absorbance of 420 nm. Data collection was then started, instantly followed by the addition of 0.5 mL of the stock 2.5 mM substrate solution

needed to determine the optimal temperature at which the enzyme amylase best functions. Since an increase in temperature speeds up the movement in molecules, the substrate is supposed to come in contact with the active site of the enzyme more quickly and frequently until the heat becomes an obstacle by denaturing the structure of these enzymes and thus changing its function. There were a total of four different temperatures at which amylase activity was observed (Table 1). In order to ensure that temperature

temperatures. We are going to measure the speed of amylase (Dependent) in different temperatures (Independent). Our goal of this lab is to find out amylase’s digest speed in different temperatures. To accomplish this goal we will need 4 test tubes with amylase and starch in it, water baths/water boiler with will be making the temperature 4, 21, 40, 60 and 100. And iodine to test the amount of leftover starch. We will be mixing starch with amylase (test tubes) in different temperatures (4, 21, 40

Abstract: This experiment for lab #4: Enzymes was having a fungal amylase and a bacterial amylase which are poured into separate sets of 24 wells, which then someone from the group pours three drops of iodine on each row representing four different temperatures (0 degrees, 40 degrees, 55 degrees, and 75-85degrees) and different times reaching from 0 to 10min. The aim for this research was to see which wells with the mixture of the amylases turned yellow, slightly yellow or black. If it turned yellow that

The purpose of this lab was to determine the optimal temperature and pH for bacterial amylase activity. A spectrophotometer, a laboratory instrument that measures the amount of light absorbed by the sample (Green et al. 2015), was used to record the percent transmittance of the various temperatures and pH levels. The percent transmittance was then used to create a visual of the optimum conditions of bacterial amylase activity (See Figures 1 and 2). After performing this experiment, one can conclude

an increasing sodium chloride (NaCl) concentration on the ability of amylase breaking down starch. It was carried out by using increasing NaCl concentrations from 0.10 to 0.50, mixing amylase and starch and adding the salt before Pasteur pipetting two droplets into iodine on a spotting tile until colour change was observed. Results show that an increasing NaCl concentration increases enzyme reaction rate. Introduction Amylase, an enzyme, breaks down starch into glucose. In this experiment the