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Amylase is an enzyme and, like most enzymes, it will denature when exposed to high temperatures. Denature means to lose its shape and an enzyme such as amylase is dependent on its shape to perform its function.

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12y ago
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5mo ago

To test if catalase can catalyze starch, you would mix catalase with starch and observe if there is any breakdown of starch into simpler products like glucose. You can also use a test reagent like Lugol's iodine to detect the presence of starch before and after the catalase reaction as a qualitative test. Finally, you can measure the amount of glucose produced using a glucose detection assay as a quantitative test for catalase activity on starch.

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11y ago

Catalase can only break down hydrogen peroxide. Therefore, it cannot break down starch because starch is a polymer of glucose and it is not a substrate of catalase.

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Q: How would you test to see if catalase could catalyze starch?
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The effect of catalase on non living things?

Catalase is an enzyme that is involved in breaking down hydrogen peroxide into water and oxygen. Since non-living things do not have biological processes or metabolic pathways, catalase would have no effect on them. It requires a living system to function and cannot catalyze reactions in non-living objects.


What enzyme catalyzes the digestion of starch?

Lactase catalyzes the breakdown of lactose. It would probably not catalyze the breakdown of starch because enzymes are SPECIFIC and are typically named for the substrate that it acts on. Amylase is the enzyme that catalyzes the breakdown of starch. (Named so because in plants, starch is stored in the amyloplasts)


Why is the shape of H2O2 important to the enzyme catalase?

The shape of H2O2 is important because enzymes like catalase have specific active sites where the substrate (H2O2) binds and reacts. The shape of H2O2 must fit into the active site of catalase for the enzyme to catalyze the decomposition of H2O2 effectively. If the shape of H2O2 does not match the active site, the enzyme may not work properly.


Reaction of Bacillus Megaterium in a catalase test?

Bacillus megaterium is catalase-positive, meaning it produces the enzyme catalase which breaks down hydrogen peroxide into water and oxygen. In a catalase test, if Bacillus megaterium is added to hydrogen peroxide, you would observe the formation of bubbles or effervescence due to the release of oxygen gas. This is a positive catalase test result for Bacillus megaterium.


What would happen if your body didn't have the enzyme catalase?

we would die


What are some example sentences for the word catalyze?

The new policy served to catalyze a wave of innovation within the company. The presence of a mentor can catalyze a student's academic success. The introduction of renewable energy incentives helped to catalyze the shift towards sustainable practices.


Would you expect Clostridium to produce catalase?

No, Clostridium are generally catalase-negative bacteria. They lack catalase enzyme which catalyzes the breakdown of hydrogen peroxide into water and oxygen.


Do catalase reactions occer at 100 degrees?

No, catalase enzymes are denatured at high temperatures, such as 100 degrees Celsius. Denaturation causes the enzyme to lose its shape and function, which would prevent catalase reactions from occurring effectively at such high temperatures.


Is there catalase in boiled liver?

Not if you boiled it well. Liver does contain catalase, but boiling permanently denatures most proteins. Whatever catalase was in the liver before boiling will probably be denatured and non-functional after boiling.


Which type of protein hepls to catalyze biochemical reactions?

That would be an enzyme.


How would the results of the starch hydrolysis change if glucose was added to the medium?

Adding glucose to the starch hydrolysis medium would provide an additional readily available source of energy for the organisms present. This could potentially increase the growth rate and metabolism of those organisms, leading to a faster breakdown of starch into glucose. As a result, the rate of starch hydrolysis may be accelerated in the presence of glucose.


What would the reaction rate do if another substance that binds to the active site of catalase was added?

If another substance binds to the active site of catalase, it could potentially inhibit or slow down the enzyme's activity. This could decrease the rate of reaction catalyzed by catalase, as the binding of the other substance may interfere with the enzyme's ability to bind with its substrate and convert it to products.