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Action of amylase on starch
The breakdown of starch by amylase
The breakdown of starch by amylase
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Recommended: Action of amylase on starch
Purpose: The purpose of this lab is to test an enzyme amylase from digestion system, which it has a big part in breaking down carbs into maltose, glucose and others. And our data by end of the lab could lead us to the specific conditions which are required for amylase in order to do its job perfectly.
Hypothesis:
Carbohydrates:
Starch + Amylase: amylase duty is to digest starch by catalyzing hydrolysis, which lead the starch to form into Maltose, which is around the same size as two joined glucose molecule, so base on this If we mix amylase by itself with starch it will be the most active reaction for breaking down of starch compare to our other compounds mix.
Peptide:
Pepsin help digesting proteins from the food we eat, and it's doing
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Starch + Amylase + HCL
Dark Purple
Yellow green
4. Starch + Boiled Amylase
Purple Blue
Brown
Table 1: Carbohydrates table, testing for Starch by Lugols (iodine) and Benedicts reagent
Peptides
Incubation Conditions
Appearance of Egg White after incubation
1. Protein + Pepsin @ 37℃
╳
2. Protein + Pepsin + Acid @ 37℃
✔
3. Protein + Pepsin + Acid @ 0℃
╳
4. Protein + Acid @ 37℃
╳
5. Protein + pepsin + NaOH @ 37℃
╳
Table2:Protein/Pepsin, testing for dissolveness of egg white with help of pepsin and others ╳= Not Dissolved, ✔= dissolve (partially as it was reported)
Lipids:
Incubation conditions
Initial pH (time 0)
Final pH (time @ 1 hour)
1. Cream + bile salts
10
8
2. Cream + Lipase
5
5
3. Cream + bile salts + lipase
5
5
Table 3: Lipids/Fat/lipase table, testing for change of pH by having cream and lipase and bile salt in different orders.
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But now we have the rest of the result isn't bad to understand why the other tubes end up with that color and what happened with their starch inside. Starch + Boiled Amylase, Once the amylase reach certain temperature it will cause it proteins in enzyme to denature which cause changing in shape and not having the ability to work properly. So adding starch and Boiled Amylase will also cause the starch to not be broken down properly which cause a brown color looking at final, than Starch + Amylase + HCl: Due to presence of HCl, it will unfold the amylase, which it disrupt the shape of its active site, in consequence the enzyme is not functional anymore, so adding HCl to amylase will interrupt the amylase in order of breaking down starch, which caused it a yellow green after boiling, and last but not least is Starch + DI H2O: Since adding H2O to starch won’t cause a change in starch so we expect Lugol’s iodine solution to turn purple/black indicating unhydrolyzed starch and it turned out to be blue at the end
Of the pH values tested, which is the optimal pH? Use the results in Data Table 3 to support your answer. Hypothesize how the structure of the lactase relates to the results in Data Table
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.
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
The effects of low pH, in guinea-pigs digestive tract, showed a similar effect to that of human lactase in a low pH environment. The pH levels tested in the guinea-pigs experiment were 2.5, 3.0, 3.5, and the control was 6.5. As the pH became
The purpose of this experiment was to discover the specificity of the enzyme lactase to a spec...
The Effect of pH on the Activity of Catalase Planning Experimental Work Secondary Resources Catalase is a type of enzyme found in different types of foods such as potatoes, apples and livers. It speeds up the disintegration of hydrogen peroxide into water because of the molecule of hydrogen peroxide (H2O2) but it remains unchanged at the end of the reaction.
The independent variable for this experiment is the enzyme concentration, and the range chosen is from 1% to 5% with the measurements of 1, 2, 4, and 5%. The dependant variable to be measured is the absorbance of the absorbance of the solution within a colorimeter, Equipments: Iodine solution: used to test for present of starch - Amylase solution - 1% starch solution - 1 pipette - 3 syringes - 8 test tubes – Stop clock - Water bath at 37oc - Distilled water- colorimeter Method: = == ==
enzyme. As I'm sure you are well aware, enzymes do not get used up in
According to the graph on amylase activity at various enzyme concentration (graph 1), the increase of enzyme dilution results in a slower decrease of amylose percentage. Looking at the graph, the amylose percentage decreases at a fast rate with the undiluted enzyme. However, the enzyme dilution with a concentration of 1:3 decreased at a slow rate over time. Additionally, the higher the enzyme dilution, the higher the amylose percentage. For example, in the graph it can be seen that the enzyme dilution with a 1:9 concentration increased over time. However, there is a drastic increase after four minutes, but this is most likely a result of the error that was encountered during the experiment. The undiluted enzyme and the enzyme dilution had a low amylose percentage because there was high enzyme activity. Also, there was an increase in amylose percentage with the enzyme dilution with a 1: 9 concentrations because there was low enzyme activity.
at a volume of 4cm3. The preliminary work also proved to me that my basic method worked without any setbacks that may affect my results. Variables:.. The variables involved in the rate of reaction between amylase and starch are. The volume of amylase The volume of starch
Investigating the Effect of Enzyme Concentration on the Hydrolysis of Starch with Amylase Aim: Investigate the effect of enzyme concentration on the rate of an enzyme-controlled reaction. Using amylase and starch as my example. Introduction: I am investigating the effect of the concentration of the enzyme, amylase on the time taken for the enzyme to fully breakdown the substrate, starch to a sugar solution. The varied variable will be the concentration and all other variables are going to be fixed. The different concentrations will be: 0.5% 0.75% 1.0% 1.5% 2% An enzyme is a class of protein, which acts as a biological catalyst to speed up the rate of reaction with its substrates.
Enzymes are proteins that help speed up chemical reactions. Some enzymes associated with carbohydrate breakdown are sucrose, lactose, maltase, and amylase. They aid in turning carbohydrate into glucose. The body uses glucose for energy, especially within the cells. Lipids or fats must be emulsified by bile found in the liver, and will be broken down into fatty acids and glycerol, and the body is able to absorb them. The enzyme associated with lipid breakdown is lipase. Protein that is ingested use the enzymes proteases and peptidases to help break up the protein and make amino acids in the
The sugar molecule lactose is found in dairy products and people with 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 breakdown of lactose stops. Lactose intolerance occurs when this breakdown fails due to insufficient or ineffective lactase. The experiment will stimulate the process
In this lab, it was determined how the rate of an enzyme-catalyzed reaction is affected by physical factors such as enzyme concentration, temperature, and substrate concentration affect. The question of what factors influence enzyme activity can be answered by the results of peroxidase activity and its relation to temperature and whether or not hydroxylamine causes a reaction change with enzyme activity. An enzyme is a protein produced by a living organism that serves as a biological catalyst. A catalyst is a substance that speeds up the rate of a chemical reaction and does so by lowering the activation energy of a reaction. With that energy reactants are brought together so that products can be formed.
The primary function of the enzyme in this experiment was to enhance the rate of the reaction to get optimum results which were achieved. As was expected before starting the experiment, in every case, the amount of product formed increased with time until the reaction came to a stop and no change was seen in concentration of substrate or product. So overall the experiment was a success in my opinion with no major mistakes as all data could be calculated and