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    many thanks,

    if i was making such an investigation , what would i use?
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    sounds comlpicated
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    (Original post by sixthformer)
    many thanks,

    if i was making such an investigation , what would i use?
    Trypsin is a serine protease found in the digestive system of many vertebrates, where it hydrolyses proteins. Trypsin is produced in the pancreas.

    I'm thinking as it's an enzyme, it's most likely to be denatured at high temperatures, but if the temperature is at it's optimum then it would speed the rate of reaction, in this case hydrolysis and form a greater amount of product per unit time.

    If you want to carry out an experiment, I would suggest using the same volume of trypsin in a test tube along with the same sample of some type of protein (could be anything) making sure that it's the same size. Then placing these samples in different temperature water baths. Using some kind of indicator that would detect the hydrolysis of protien like using biuret reagent. If the protein was being hyrolysed then the mixture would stay blue to show no more protein is left, or if it's not being hydrolysed or at a slow rate it would turn from blue to lilac. You could use a stop watch to time how long it takes for the colour to change from lilac to blue. Record a table and compare the rate of reaction and see how temperature effects it. I'm thinking as temperature increases then the rate of reactin would also increase until an optimum temperature would show the rate of reaction at its maximum. Above this temperature the rate of reaction would drop due to denaturing of enzyme, and unable to carry out it's function of hydrolysis. Not sure if this experiment would work though, just a thought from my previous knowledge.

    Does that answer your question?
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    (Original post by loling909)
    Trypsin is a serine protease found in the digestive system of many vertebrates, where it hydrolyses proteins. Trypsin is produced in the pancreas.

    I'm thinking as it's an enzyme, it's most likely to be denatured at high temperatures, but if the temperature is at it's optimum then it would speed the rate of reaction, in this case hydrolysis and form a greater amount of product per unit time.

    If you want to carry out an experiment, I would suggest using the same volume of trypsin in a test tube along with the same sample of some type of protein (could be anything) making sure that it's the same size. Then placing these samples in different temperature water baths. Using some kind of indicator that would detect the hydrolysis of protien like using biuret reagent. If the protein was being hyrolysed then the mixture would stay blue to show no more protein is left, or if it's not being hydrolysed or at a slow rate it would turn from blue to lilac. You could use a stop watch to time how long it takes for the colour to change from lilac to blue. Record a table and compare the rate of reaction and see how temperature effects it. I'm thinking as temperature increases then the rate of reactin would also increase until an optimum temperature would show the rate of reaction at its maximum. Above this temperature the rate of reaction would drop due to denaturing of enzyme, and unable to carry out it's function of hydrolysis. Not sure if this experiment would work though, just a thought from my previous knowledge.

    Does that answer your question?
    thank you!!
 
 
 
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