Full Answer
What is enzyme activity lab report?
Specific enzyme activity is a measure of enzymes purity and quoted as units/ mg. the value becomes huge as an enzyme preparation becomes purer since the amount of protein (mg) is typically less, but the rate of reaction stays the same/ may increase due to reduced interference/ removal of inhibitors. Read More
How to explain the meaning of enzyme specificity?
Types of enzyme specificity
- Substrate/ absolute specificity. The specificity of enzymes for their substrate is absolute specificity. ...
- Bond specificity. Also termed as “Relative Specificity” of enzymes. ...
- Group specificity. ...
- Linkage specificity. ...
- Optical specificity. ...
- Geometrical specificity. ...
- Co-factor specificity. ...
How does enzyme structure determine enzyme specificity?
Specificity is the ability of an enzyme to choose exact substrate from a group of similar chemical molecules. The specificity is actually a molecular recognition mechanism and it operates through the structural and conformational complementarity between enzyme and substrate. Enzymes show different degrees of specificity towards their substrate.
Why does enzyme specificity promote enzyme activity?
Why does enzyme specificity promote enzyme activity? The active site of an enzyme has shape that is complementary to the substrate shape only then can enzyme and substrate interact and reaction occur. Why does a warm temperature promote enzyme activity?
How did you determine that the enzyme lactase was active?
Lactase only breaks down lactose, but not other carbohydrates, such as sucrose or maltose. To measure whether an enzyme is active, scientists can measure the end product(s) of an enzymatic reaction.
How does lactase affect enzyme activity?
Your probability of being lactose intolerant is correlated with whether your ancestors raised milk cows. The commercial product, Lactaid, contains lactase. Enzyme action can be blocked by molecules that obstruct the enzyme's active site. Herbicides and pesticides often work in this way.
Why does lactase work best at a specific temperature?
Cooler temperatures slow the rate of lactase's function, while at extremely high temperatures -- those above 135 degrees Fahrenheit, for example -- lactase can become denatured, or lose its shape. A protein's shape is responsible for its function, so when it becomes denatured, lactase loses its ability to function.
What is the specific chemical reaction that lactase catalyzes?
Lactase catalyzes the hydrolysis of the glycosidic bond in the disaccharide lactose, releasing galactose and glucose (Figure 2)5.
Is lactase specific to lactose?
Lactose is a disaccharide consisting of 2 monosaccharides, glucose and galactose, linked together via a β-1→4 bond. Hydrolysis of this bond requires a specific enzyme called lactase which digests lactose to its components allowing the uptake of glucose and galactose from the intestine.
Are enzymes reaction specific?
Each different type of enzyme will usually catalyse one biological reaction. Enzymes are specific because different enzymes have different shaped active sites. The shape of an enzyme's active site is complementary to the shape of its specific substrate or substrates. This means they can fit together.
What temperature does lactase work best at?
125 to 135 degrees FSo by definition, 125 to 135 degrees F is the "optimum temperature" (range) for lactase activity. At temperatures higher than this range, the enzyme quickly becomes denatured and therefore unable to break down the milk sugar.
Why is lactase used at low temperatures?
S. lactis lactase, however, also shows an appreciable activity at lower temperatures, down to about 4°C. This property is especially important for practical application because growth of spoilage bacteria at this temperature is very slow. Milk (or whey) thus can be treated during the usual overnight storage period.
How does temperature affect enzyme activity experiment?
As the temperature increases so does the rate of enzyme activity. An optimum activity is reached at the enzyme's optimum temperature. A continued increase in temperature results in a sharp decrease in activity as the enzyme's active site changes shape.
Is the enzyme lactase a catalyst?
The enzyme lactase acts as a catalyst to facilitate the reaction and make it happen very quickly. This enzyme is made up of four separate subunits that come together to form a single functioning enzyme.
What factors affect lactase?
Lactose concentration, sources of growth factors; temperature of incubation, and pH of the whey were the primary factors affecting lactase production. Increased levels of lactose in whey stimulated the yeast to produce higher levels of lactase activity per gram of dried yeast.
What is lactase enzyme used for?
LACTASE (LAK teys) is an enzyme that aids in the digestion of lactose. Lactose is in dairy foods like ice cream, cheese, and milk. This supplement is used to break down lactose and prevent bloating, diarrhea, and gas of lactose intolerance. The FDA has not approved this supplement for any medical use.
What is the role of lactase in the body?
The critical importance of lactase in a human nutritional setting stems from its role in allowing the breakdown of lactose into its constituent monosaccharide components, which can then be used to generate energy in the body. Lactase catalyzes the hydrolysis of the glycosidic bond in the disaccharide lactose, releasing galactose and glucose (Figure 2)5. These monosaccharides are then used primarily for the generation of adenosine triphosphate (ATP) via the citric acid cycle and oxidative phosphorylation6. During neonate and infant development, lactase is highly expressed in the human digestive system, breaking down lactose received from breast milk of which lactose is the primary carbohydrate component, and one of the key sources of nutrition during early years7. The medical importance of lactase is highlighted by congenital lactase deficiency (CLD), a rare autosomal recessive condition caused by mutations in the lactase gene (LCT) coding for the lactase enzyme8. New-born babies with CLD exhibit very little lactase activity, thus they cannot be fed on breast milk, any other type of milk, or formula containing lactose.
How much lactase is in a tablet?
Crush one lactase tablet, containing 200 mg of enzyme, to an even powder using a mortar and pestle.
What happens if you lose lactase?
Conversely, the loss of lactase expression can lead to lactose intolerance, also known as adult-type hypolactasia (ATH), resulting from an inability to break down lactose in the gut. ATH is characterized by a build up of lactose in the colon following ingestion of lactose containing food products. In the colon, the accumulated lactose is fermented by gut microbial fauna, releasing gasses including hydrogen, methane, and carbon dioxide. The production of these gases in individuals with lactase enzyme deficiencies promote abdominal bloating, increased flatulence, pain, nausea, and borborygmi (stomach rumbling)7. Increased levels of lactose in the digestive tract can also lead to loose stools.
How long does it take for lactase to react with a reaction B tube?
Add 10 µL of lactase extract to the reaction B tube, mix by vortexing and allow the reaction to proceed for 1 min at room temperature.
How long to vortex enzyme extraction?
Vortex for 1 min to maximize enzyme extraction.
Lab Report Assistant
This document is not meant to be a substitute for a formal laboratory report. The Lab Report Assistant is simply a summary of the experiment’s questions, diagrams if needed, and data tables that should be addressed in a formal lab report.
Questions
A. Explain why a glucose test strip may be used to determine the enzymatic activity of lactase. The glucose test strips may be used to determine the enzymatic activity of lactase. This is because lactase is an enzyme for digestion that is a catalyst for the breakdown of lactose.
How to determine enzyme specificity?
Enzyme specificity is achieved on the basis of its 3D structure, the type of amino acid sequence that makes its active site, type of substrate and most importantly the type of interactions (hydrophobic/hydrophilic etc) that are formed between enzyme’s active site and substrate molecule. The amino acid groups of the active site of enzyme may be of different type so it contributes in determining the specificity of enzyme. For example,
What is the relative specificity of enzymes?
Also termed as “Relative Specificity” of enzymes. Enzymes are specific for structurally related molecules. These structures share closely related bonding pattern. For example, the peptide bond, glycosidic bond and ester bond etc. Due to similar bonds present in these structures, the enzyme can bind and catalyze structurally related molecules.
What are enzymes?
Enzymes are the biological catalysts that speed up the chemical reactions in cells of living organisms. Enzymes are proteins having a 3D structure that needs to be maintained for an enzyme to remain functional. They lower thee activation energy of biochemical reaction in cells and thus speed up the rate of reaction. Activation energy of enzyme is the amount of energy required to initiate a reaction. With the help of enzymes, the substrates are converted into products that are utilized by the cell. For example, the digestive enzyme protease breaks down the large protein molecules into smaller digestible peptides.
Why can't amylase digest cellulose?
The amylase enzyme of human body cannot digest the cellulose because cellulose has β-1,4 glycosidic linkage and the enzyme can only break α-1,4 linkage of glycogen and starch. 6. Geometrical specificity.
How does specificity work?
How enzyme specificity works? 1 Some amino acid groups that give conformational changes to enzyme-substrate complex 2 Orientation groups that provide specific orientation for substrate attachment 3 Groups that provide affinity for developing intramolecular interactions between enzyme and substrate 4 Catalytic groups that create enough tension to provide bond breaking strength to enzymes
Which enzyme breaks the ester bond between fatty acids and starch?
In this case, the enzyme only considers the glycosidic bond not the substrate. Same is the case for lipase enzyme that breaks ester bond both in fatty acids and glycerol. The L and D forms of amino acids are structurally related to each other so they also have the ability to act as substrate for same enzyme.
Which enzyme breaks down macromolecular food particles into small digestible particles?
For example, the digestive enzymes break down the macromolecular food particle into small digestible particles. Trypsin enzyme catalyzes the breakdown of proteins. Amylase enzyme catalyzes carbohydrate digestion.
Purpose and Hypothesis
This lab measures the enzyme, in this case, lactase, specificity upon a certain substrate, which in this lab was lactose. After conducting the lab, enzyme action will have been recorded. Different factors will be closely examined for their effect on enzyme reactions, such as shape and denaturation.
Questions
This experiment called for the breaking down of lactose by lactase into glucose and galactase, so that usable ATP may use these molecules. This breakdown was displayed when the milk and enzyme solution later ended up with the presence of glucose in the solution after two minutes of initially not having this.
