Why catalase does not break down starch?
I don't know what you are talking about. There is only one difference between enzymes and catalyst that enzymes are biological catalyst, which speeds up the reaction without itself being changed. The enzyme used to break down starch into glucose is amylase. catalase breaks down hydrogen peroxide into water and oxygen,
To what substance will the enzyme catalase react more, h2o2, water, or starch solution?
Not entirely. Catalase is the enzyme that hydrolyzes H2O2 (peroxide) and should not react with H2O. It also should not react with starch. So, your results with starch are suspect. Either the starch is contaminated, or the catalase may be contaminated.
Effect of sugar on catalase/enzyme activity?
Nothing would change that reaction because it does not involve sugar. Catalase is a very general name for any enzymes that perform catalytic reactions, or breaking down of other molecules. The reaction with hydrogen peroxide is specifically performed by peroxidase, an enzyme with the structure to break down H2O2 molecules. Sugars, no matter what kinds, play no role in this reaction and so would have no effect on this reaction. Here it is: 2 H2O2 + peroxidase= 2 H2O + O2 It is the release of the oxygen gas formed in this reaction that makes the peroxide 'fizz'. Notice, this reaction has no carbohydrates involved. There are no carbon atoms involved at all, in fact, so it is not even an organic reaction much less a biochemical one. It happens in animal tissues, but it is a neutralizing reaction because H2O2 is a poison and must be broken down to harmless byproducts. Remember, an enzyme is structured to fit on its substrate molecule exactly, and peroxidase fits on peroxide molecules to break those bonds. It does not fit on carbohydrates.
What is the optinum pH of the enzyme, catalase?
Wikipedia
What is the relationship between pH and enzyme activity?
All enzymes have an optimum pH... that is the pH at which they work the fastest. However, as pH increases or drops from this optimum, the bonds that keep the enzyme in their shape break. Thus, the enzyme changes shape. Ergo, the active site changes shape and the substrate no longer fits. The enzyme is said to be denatured.Extremely high or low pH values generally result in complete loss of activity for most enzymes. pH is also a factor in the stability of enzymes. As with activity, for each enzyme there is also a region of pH optimal stability.The optimum pH value will vary greatly from one enzyme to another, as the following Table shows:Enzyme pH OptimumLipase (pancreas) 8.0Lipase (stomach) 4.0 - 5.0Lipase (castor oil) 4.7Pepsin 1.5 - 1.6Trypsin 7.8 - 8.7Urease 7.0Invertase 4.5Maltase 6.1 - 6.8Amylase (pancreas) 6.7 - 7.0Amylase (malt) 4.6 - 5.2Catalase 7.0To illustrate the relationship between enzymes and pH, consider the case of amylase, an enzyme that aids in digestion. The optimum pH for amylase is achieved in the stomach, which is where the enzyme begins to break down carbohydrates. The pH of saliva inside the mouth is higher than the optimum pH, so amylase is not activated while chewing. The same holds true for the small intestine — the pH is similar to saliva. The main factor is pH because it has a direct effect on when the enzyme becomes active and inactive throughout the digestive system.
How does pH affect the activity of catalase?
Catalase, as most enzimes, has an optimal pH to achieve its maximum activity (in this case, 7.0). If you change the pH of the medium either way, you will observe a decline in its activity.
Which enzyme breaks the cellular wall of bacteria?
Lysozyme or Muramidase or Glycoside hydrolase is the enzyme discovered by Alexander Fleming is responsible for breaking down bacterial cell wall.This enzyme leads to the breakdown of peptidoglycan layer of bacterial cell wall.It is mostly found in-1 Milk2Tears3Mucus4saliva5SweatAnd many other fluids..Hope it helps…
Effect of substrate concentration on reaction rate of enzyme catalase?
Well, in general if you're interested in substrate concentration effects, then you need to vary your substrate concentration (your dependent variable) while keeping your catalase concentration constant. You can do this by dilution of stock solution(s) containing your substrate (hydrogen peroxide, I'm guessing), and reacting each with a constant concentration of catalase. You need something to measure the rate of reaction - this part has probably been explained to you since you can do it different ways. You need to make sure you vary your substrate (peroxide) concentrations enough to get the flat top and bottom portions of the sigmoid reaction rate curve, and enough data points to get the slope of the middle part. Your research should give you some good starting points.
How amylase and pancreatin speed up hydrolysis of starch?
Pancreatin is a mixture of the enzymes of pancreatic juice, and contains amylase. The amylase is an enzyme and as such lowers the activation energy of the reaction and speeds it up. Amylase works by hydrolysing the glycosidic bonds betwen the alpha glucose units in starch.