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    Bio Essay 8

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    Dana Soko
    An enzyme is a protein that catalyzes chemical reactions through its unique three-dimensional structure. It has an active site that binds to specific substrate molecules and lowers their activation energy, speeding up reactions without being used up itself. Enzyme structure allows for specificity, binding only certain substrates through induced fit. An experiment could investigate how temperature affects enzyme activity by measuring reaction rates of an enzyme-substrate pair like catalase and hydrogen peroxide at increasing temperatures using a colorimeter. Results could show higher reaction rates, and lighter product colors, at lower temperatures before the enzyme denatures from excess heat disrupting its structure.

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    Bio Essay 8

    Uploaded by

    Dana Soko
    11K views1 page
    An enzyme is a protein that catalyzes chemical reactions through its unique three-dimensional structure. It has an active site that binds to specific substrate molecules and lowers their activation energy, speeding up reactions without being used up itself. Enzyme structure allows for specificity, binding only certain substrates through induced fit. An experiment could investigate how temperature affects enzyme activity by measuring reaction rates of an enzyme-substrate pair like catalase and hydrogen peroxide at increasing temperatures using a colorimeter. Results could show higher reaction rates, and lighter product colors, at lower temperatures before the enzyme denatures from excess heat disrupting its structure.

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    An enzyme is a protein that catalyzes chemical reactions through its unique three-dimensional structure. It has an active site that binds to specific substrate molecules and lowers their activation energy, speeding up reactions without being used up itself. Enzyme structure allows for specificity, binding only certain substrates through induced fit. An experiment could investigate how temperature affects enzyme activity by measuring reaction rates of an enzyme-substrate pair like catalase and hydrogen peroxide at increasing temperatures using a colorimeter. Results could show higher reaction rates, and lighter product colors, at lower temperatures before the enzyme denatures from excess heat disrupting its structure.

    Copyright:

    Attribution Non-Commercial (BY-NC)
    Download as DOCX, PDF, TXT or read online from Scribd
    Download as docx, pdf, or txt
    11K views1 page

    Bio Essay 8

    Uploaded by

    Dana Soko
    An enzyme is a protein that catalyzes chemical reactions through its unique three-dimensional structure. It has an active site that binds to specific substrate molecules and lowers their activation energy, speeding up reactions without being used up itself. Enzyme structure allows for specificity, binding only certain substrates through induced fit. An experiment could investigate how temperature affects enzyme activity by measuring reaction rates of an enzyme-substrate pair like catalase and hydrogen peroxide at increasing temperatures using a colorimeter. Results could show higher reaction rates, and lighter product colors, at lower temperatures before the enzyme denatures from excess heat disrupting its structure.

    Copyright:

    Attribution Non-Commercial (BY-NC)
    Download as DOCX, PDF, TXT or read online from Scribd
    Download as docx, pdf, or txt
    of 1

    Dana Sokolowski

    Triveline, Period 3

    8. (1994) Enzymes are biological catalysts.


    a. Relate the chemical structure of an enzyme to its specificity and catalytic activity.
    b. Design a quantitative experiment to investigate the influence of pH or temperature on the activity
    of an enzyme.
    c. Describe what information concerning the structure of an enzyme could be inferred from your
    experiment.

    An enzyme is a catalytic protein. A 3D shape made up of three levels of structure: primary,


    secondary, and tertiary structure. With a unique sequence of amino acids in the primary structure, it
    defines the protein’s unique traits. The center of the enzyme is called the active site. The amino acids
    contain R groups which catalyze the conversion of substrate to product. Substrate is held in the enzyme’s
    active site by weak hydrogen and ionic bonds. By catalyzing the substrate, it speeds up the reaction by
    lowering the activation energy, thus causing the product to leave the active site and allow the enzyme to
    repeat the process with more substrate.
    It only requires small amounts of enzyme to catalyze and since an enzyme is never used up in a
    reaction, it can function over and over again. Also, enzymes may function in forward and reverse
    reactions but it depends on the amount of products and reactants in the enzymatic reaction.
    The structure of an enzyme also allows it to have specificity. Since proteins have a specific
    makeup of amino acids in their primary level of structure, they are unique and thus, only catalyze with the
    substrate unique to their function. In other words, only one kind of substrate works with a certain type of
    enzyme. It is a lock and key concept. However, since substrate does not fit perfectly in an enzyme, the
    enzyme change its shape slightly in order to accommodate the substrate through a process called induced
    fit.
    To investigate the influence of temperature on the activity of an enzyme, I would use catachol as
    my enzyme and catacholase as my substrate. First I must set up my experimental and control groups. My
    experimental group would manipulate temperature, the variable we are testing at increments of about ten
    degrees Celsius beginning at zero degrees up until 30 degrees as well as an extreme temperature such as
    80 degrees. However, I must control the amount of enzyme and substrate used in order to eliminate
    volume as a potential confounding variable. My dependent variable would be the amount of time it takes
    the enzyme to react with the substrate which we measure with the colorimeter. I would also need to set up
    a negative control which would measure the absorbency rate of the enzyme without the substrate and vice
    versa. The positive control group I keep the enzyme at room temperature and then mix it with the
    substrate. To measure the rate of reaction I use the colorimeter to detect the absorbency. Once the timer
    on the computer levels out then we record the time in the appropriate temperature increment and take out
    the cuvet. The darker the color of the product, the higher the absorbency rate. Lastly, it is essential to
    replicate the experiment in as many trials as possible.

    It can be inferred from the data that if kinetic energy increases as temperature increases, and we
    measure the rate of enzyme reaction as we increase its temperature, then the rate of the reaction should
    increase as kinetic energy increases. Thus, causing the color of the product to decrease in intensity as we
    increase its temperature. At a certain temperature, however, the enzyme will become denatured and its
    product will be clear and colorless. This means that the enzyme can no longer react with the substrate
    because its shape has been changed; as a result of an excess in heat, the hydrogen and ionic bonds that
    kept the enzyme stable became disrupted.

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