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Enzymes
Enzymes
Enzymes
1. What are the effects on the function of proteins if its structure was affected by changes in pH,
temperature and other factors?
Enzymes work best within specific temperature and pH ranges, and sub-optimal conditions can cause
an enzyme to lose its ability to bind to a substrate.
Temperature: Raising temperature generally speeds up a reaction, and lowering temperature slows
down a reaction. However, extreme high temperatures can cause an enzyme to lose its shape
(denature) and stop working.
pH: Each enzyme has an optimum pH range. Changing the pH outside of this range will slow enzyme
activity. Extreme pH values can cause enzymes to denature.
Enzyme concentration: Increasing enzyme concentration will speed up the reaction, as long as there is
substrate available to bind to. Once all of the substrate is bound, the reaction will no longer speed up,
since there will be nothing for additional enzymes to bind to.
Substrate concentration: Increasing substrate concentration also increases the rate of reaction to a
certain point. Once all of the enzymes have bound, any substrate increase will have no effect on the rate
of reaction, as the available enzymes will be saturated and working at their maximum rate.
2. Why will a protein become functionally inactivated when it is denatured by temperature and other
denaturing factors? Explain in the molecular level emphasizing on the failure of interaction with other
proteins. Are there any mechanisms that a cell can still repair misfolded or denatured proteins?
Protein denaturation involves a change in the protein structure (generally an unfolding) with the loss
of activity. It has been described using the small protein, hen egg white lysozyme. Water is critical, not
only for the correct folding of proteins but also for the maintenance of this structure. Heat denaturation
and loss of biological activity have been linked to the breakup of the 2-D-spanning water network (see
above) around the protein (due to increased breakage of the hydrogen bonds with temperature), which
otherwise acts restrictively on protein vibrational dynamics. As proteins denature, their structures
initially become looser allowing them to take up more water with the water-exposed surface increasing
by up to 50% as might be expected from reversing protein folding. It is a cooperative process. The free
energy change on folding or unfolding is due to the combined effects of both protein folding/unfolding
and hydration changes.
3. It is not enough to observe color changes in determining enzyme activity or efficiency of enzymes,
why?
It is because to effectively determine enzyme activity there is a need to monitor the disappearance of
substrate or the appearance of product. Measuring the appearance of product is usually more accurate.
Since enzymes are proteins. It is also determined by measuring the amount of product formed, or
substrate consumed in a reaction in a given time. The functioning of the enzyme is determined by the
shape of the protein.
4. If 2 proteins have the same amino acid sequence, can they have different functions? Why or why not?
Yes, Amino acids play central roles both as building blocks of proteins and as intermediates in
metabolism. The 20 amino acids that are found within proteins convey a vast array of chemical
versatility. The precise amino acid content, and the sequence of those amino acids, of a specific protein,
is determined by the sequence of the bases in the gene that encodes that protein. The chemical
properties of the amino acids of proteins determine the biological activity of the protein. The chemical
properties of the amino acids of proteins determine the biological activity of the protein. Proteins not
only catalyze all (or most) of the reactions in living cells, they control virtually all cellular process. In
addition, proteins contain within their amino acid sequences the necessary information to determine
how that protein will fold into a three dimensional structure, and the stability of the resulting structure.
5. Will the enzymes in fruits and vegetables helpful in physiological and metabolic activities in our body?
Why or why not?
Yes, the enzymes in fruits and vegetables are very helpful in physiological and metabolic activities in
human body because it was proven that these fruit and vegetable enzymes boost the body immune
system, promote healthy digestion, and detoxify and revitalize the body cells which may help us in
preventing diseases. Example of fruit enzyme is the enzyme papain which can be found mainly in
papaya. Papain helps break down proteins into smaller units, called amino acids. The body uses the
amino acids for many basic functions. These enzymes are useful for treating bedsores, skin ulcers and
wounds from surgery according to the University of Maryland Medical Center. They may also promote
wound healing from burns. Another vegetable containing a very helpful enzyme in the human body is
the asparagus which contain the highest amount of glutathione peroxidase, an enzyme the body uses to
create antioxidants, which are used to combat cancer-causing agents.
Dinolardo, M.J. (2019, September 18) Are Fruits and Veggies Healthier Raw or Cooked? Retrieved
from:https://www-mnn-com.cdn.ampproject.org/v/s/www.mnn.com/food/healthy
eating/stories/amp/are-fruits-and-vegetables-healthier-raw-or
cooked?amp_js_v=a2&_gsa=1&usqp=mq331AQCKAE%3D#aoh=15703494368982&referre
=https%3A%2F%2Fwww.google.com&_tf=From%20%251%24s&share=https%3A%2F
2Fwww.mnn.com%2Ffood%2Fhealthy-eating%2Fstories%2Fare-fruits-and-vegetables-healthier
raw-or-cooked
Sweeney, E. (2019, August 7) Cooked vs. Raw: The Healthiest Way to Eat Fruits and Vegetables.
Retrieved from: https://www-huffpost
com.cdn.ampproject.org/v/s/www.huffpost.com/entry/cooked-raw-healthy-fruits
vegetables_l_5d39ecebe4b020cd99505bac/amp?amp_js_v=a2&_gsa=1&usqp=mq331AQC
AE%3D#aoh=15703494368982&referrer=https%3A%2F%2Fwww.google.com&_tf=From%
0%251%24s&share=https%3A%2F%2Fwww.huffpost.com%2Fentry%2Fcooked-raw-healthy
fruits-vegetables_l_5d39ecebe4b020cd99505bac
University of Arizona. (2013, September 3). The Chemistry of Amino Acids. Retrieved from
http://www.biology.arizona.edu/biochemistry/problem_sets/aa/aa.html