Name: Jay Lure G.

Baguio
Section: BPED 1-A
Subject: Physiology of Exercise and Physical Activity (BPED 52)
Professor: Sir Gregorio C. Ramos Jr.

Assignment: UNIT 3 ASSESSMENT TASK

Kindly answer the questions below and Send your Outputs to our BPED 52 google
Classroom within ten (10) days.

1. Name the German scientist who made a chance observation that Droved Louis
Pasteur was wrong. Explain and illustrate the issue.
In 1897, the German chemist, Eduard Buchner (1860—1917), demonstrated that
fermentation can be brought about using lifeless chemicals rather than living yeast. He
established that biochemical reactions are possible outside living cells. His discovery
led to him receiving the 1907 Nobel Prize in Chemistry. He made a chance observation
that proved Pasteur wrong. His discovery revolutionized the study of physiologic
systems and represented the beginning of the modern science of biochemistry.
Searching for therapeutic uses for protein, he concocted a thick paste of freshly grown
yeast and sand in a large mortar and pressed out the yeast cell juice. The gummy liquid
proved unstable and could not be preserved by techniques available at that time. One of
the laboratory assistants suggested adding a large amount of sugar to the mixture—his
wife used this technique to preserve fruit.
To everyone’s surprise, what seemed like a silly solution worked; the nonliving juice
from the yeast cells converted the sugar to carbon dioxide and alcohol (directly
contradicting Pasteur’s prevailing theorem). The epoch finding about non-cellular
fermentation earned Professor Buchner the 1907 Nobel Prize in chemistry.
2. Why is ATP’s function is amazing?
Adenosine Triphosphate is an especially important organic molecule found in all
living organisms. It consists of adenosine (the sugar ribose with the organic base
adenine) and three phosphate groups. The potential energy stored in the covalent bond
between the second and third phosphate groups is important to living organisms
because it provides the energy used in nearly all of the chemical reactions within cells.
ATP is often called the energy currency of cells because it is capable of both storing
and providing energy.
The function of ATP is amazing because in the variety of processes it powers in
all living cells. This ubiquitous compound is found in microorganisms, plants, and
animals ranging from nematodes to cockroaches and humans. Surprisingly, wherever
ATP is found, it is always in the same structure, regardless of the organism's
complexity.
ATP functions are amazingly use in several cellular processes. Some important
functions of ATP in the cell are briefly discussed below:
Active Transport
ATP plays a critical role in the transport of macromolecules such as proteins and
lipids into and out of the cell. The hydrolysis of ATP provides the required energy for
active transport mechanisms to carry such molecules across a concentration gradient.
Transport of molecules into the cell is called endocytosis whilst transport out of the cell
is known as exocytosis.
Cell Signaling
ATP has key functions both in intracellular and extracellular signaling. It is easily
recognized by purinergic receptors in mammalian tissues – its release from synapses
and axons activates purinergic receptors that modulate calcium and cyclic AMP levels
inside the cell.
In the central nervous system, adenosine modulates neural development, the
control of immune systems, and of neuron/glial signaling. ATP is also involved in signal
transduction – its phosphate groups are used up by kinases in phosphate transfer
reactions which activate a cascade of protein kinase reactions.
Structural Maintenance
ATP plays a very important role in preserving the structure of the cell by helping
the assembly of the cytoskeletal elements. It also supplies energy to the flagella and
chromosomes to maintain their appropriate functioning.
Muscle contraction
ATP is critical for the contraction of muscles; it binds to myosin to provide energy
and facilitate its binding to actin to form a cross-bridge. ADP and phosphate are then
released and a new ATP molecule binds to myosin. This breaks the cross-bridge
between myosin and actin filaments, thereby releasing myosin for the next contraction.

3. What is enzyme? Demonstrate its functions and unique property?

Enzymes are a type of protein found within a cell and a biological molecules
(typically proteins) that create chemical reactions in the body and significantly speed up
the rate of virtually all of the chemical reactions that take place within cells to help
support life. They are vital for life and serve a wide range of important functions in the
body, such as aiding in building muscle, destroying toxins, and breaking down food
particles during digestion and metabolism. An enzyme’s shape is tied to its function.
Heat, disease, or harsh chemical conditions can damage enzymes and change their
shape. When this happens, an enzyme doesn’t work anymore. This affects the body
processes the enzyme helped support.
Some enzymes help break large molecules into smaller pieces that are more easily
absorbed by the body. Other enzymes help bind two molecules together to produce a
new molecule. Enzymes are highly selective catalysts, meaning that each enzyme only
speeds up a specific reaction. The molecules that an enzyme works with are called
substrates. The substrates bind to a region on the enzyme called the active site.

There are two theories explaining the enzyme-substrate interaction.

In the lock-and-key model, the active site of an enzyme is precisely shaped to hold
specific substrates. In the induced-fit model, the active site and substrate don’t fit
perfectly together; instead, they both alter their shape to connect.
Whatever the case, the reactions that occur accelerate greatly — over a millionfold —
once the substrates bind to the active site of the enzyme. The chemical reactions result
in a new product or molecule that then separates from the enzyme, which goes on to
catalyze other reactions.
The suffix “-ase” is used to signify an enzyme. In enzyme naming, an enzyme is
denoted by adding -ase to the end of the name of the substrate on which the enzyme
acts. It is also used to identify a particular class of enzymes that catalyze a specific type
of reaction.
Below, find some examples of words ending in -ase, along with a breakdown of different
root words in their name and their definition.
Examples:
Acetylcholinesterase (acetyl-cholin-ester-ase): This nervous system enzyme, also
present in muscle tissue and red blood cells, catalyzes the hydrolysis of the
neurotransmitter acetylcholine. It functions to inhibit the stimulation of muscle fibers.
Amylase (amyl-ase): Amylase is a digestive enzyme that catalyzes the decomposition
of starch into sugar. It is produced in salivary glands and the pancreas.
Carboxylase (carboxyl-ase): This class of enzymes catalyze the release of carbon
dioxide from certain organic acids.
Collagenase (collagen-ase): Collagenases are enzymes that degrade collagen. They
function in wound repair and are used to treat some connective tissue diseases.
Dehydrogenase (de-hydrogen-ase): Dehydrogenase enzymes promote the removal
and transfer of hydrogen from one biological molecule to another. Alcohol
dehydrogenase, found abundantly in the liver, catalyzes the oxidation of alcohol to aid in
alcohol detoxification.
Deoxyribonuclease (de-oxy-ribo-nucle-ase): This enzyme degrades DNA by catalyzing
the breaking of phosphodiester bonds in the sugar-phosphate backbone of DNA. It is
involved in the destruction of DNA that occurs during apoptosis (programmed cell
death).
Endonuclease (endo-nucle-ase): This enzyme breaks bonds within nucleotide chains
of DNA and RNA molecules. Bacteria use endonucleases to cleave DNA from invading
viruses.
Histaminase (histamin-ase): Found in the digestive system, this enzyme catalyzes the
removal of the amino group from histamine. Histamine is released during an allergic
reaction and promotes an inflammatory response. Histaminase inactivates histamine
and is used in the treatment of allergies.
Hydrolase (hydro-lase): This class of enzymes catalyzes the hydrolysis of a compound.
In hydrolysis, water is used to break chemical bonds and split compounds into other
compounds. Examples of hydrolases include lipases, esterases, and proteases.
Isomerase (isomer-ase): This class of enzymes catalyzes reactions that structurally
rearrange the atoms in a molecule changing it from one isomer to another.
Lactase (lact-ase): Lactase is an enzyme that catalyzes the hydrolysis of lactose to
glucose and galactose. This enzyme is found in high concentrations in the liver,
kidneys, and mucous lining of the intestines.
Ligase (lig-ase): Ligase is a type of enzyme that catalyzes the joining together of
molecules. For example, DNA ligase joins DNA fragments together during DNA
replication.
Lipase (lip-ase): Lipase enzymes break down fats and lipids. An important digestive
enzyme, lipase converts triglycerides into fatty acids and glycerol. Lipase is produced
mainly in the pancreas, mouth, and stomach.
Maltase (malt-ase): This enzyme converts the disaccharide maltose to glucose. It is
produced in the intestines and used in the digestion of carbohydrates.
Nuclease (nucle-ase): This group of enzymes catalyzes the hydrolysis of bonds
between nucleotide bases in nucleic acids. Nucleases split DNA and RNA molecules
and are important for DNA replication and repair.
Peptidase (peptid-ase): Also called protease, peptidase enzymes break peptide bonds
in proteins, thereby forming amino acids. Peptidases function in the digestive system,
immune system, and blood circulatory system.
Phospholipase (phospho-lip-ase): The conversion of phospholipids to fatty acids by the
addition of water is catalyzed by a group of enzymes called phospholipases. These
enzymes play an important role in cell signaling, digestion, and cell membrane function.
Polymerase (polymer-ase): Polymerase is a group of enzymes that builds polymers of
nucleic acids. These enzymes make copies of DNA and RNA molecules, which is
required for cell division and protein synthesis.
Ribonuclease (ribo-nucle-ase): This class of enzymes catalyzes the break down of
RNA molecules. Ribonucleases inhibit protein synthesis, promote apoptosis, and
protect against RNA viruses.
Sucrase (sucr-ase): This group of enzymes catalyzes the decomposition of sucrose to
glucose and fructose. Sucrase is produced in the small intestine and aids in the
digestion of sugar. Yeasts also produce sucrase.
Transcriptase (transcript-ase): Transcriptase enzymes catalyze DNA transcription by
producing RNA from a DNA template. Some viruses (retroviruses) have the enzyme
reverse transcriptase, which makes DNA from an RNA template.
Transferase (transfer-ase): This class of enzymes aids in the transfer of a chemical
group, such as an amino group, from one molecule to another. Kinases are examples of
transferase enzymes that transfer phosphate groups during phosphorylation.

4. What happen when excess protein is taken by an individual?

High-protein diets, which have seen a recent resurgence since diets like Atkins
and the Zone gained popularity in the 1990s. Diets such as the Caveman or Paleo diet
can vary in terms of macronutrient ratios, but are typically high in protein. While the
standard ketogenic (or “keto”) diet emphasizes fat, it can also be high in protein. Even
mostly or entirely plant-based diets can be high in protein. Protein is an essential part of
a healthy diet. It helps to build and repair muscle, organs, and bones. High-protein diets
have also been shown to be helpful with reducing fat, losing weight, increasing satiety,
or a feeling of fullness, and retaining muscle.
However, high-protein diets have also been associated with several risks that are
important to be aware of and understand. Nutritional experts don’t advocate
consumption to exceed the recommended daily amount.
When calculating how much total protein you currently eat or should eat, factor in
protein from your diet (e.g., food and drink sources). You should also factor in
supplements, if the supplements you use contain substantial amounts of protein, such
as protein powder.
Risks of eating too much protein
 Consuming high amounts of any nutrient for a long period of time typically comes
with risks, as can be the case with protein. Overconsumption may lead to an increased
risk of certain health complications, according to research.
There are potential benefits to a high-protein diet for otherwise healthy people.
However, it’s important to understand the health concerns related to excess protein in
the body, especially if you follow an excessively high-protein diet for an extended
period.
a. Weight gain- High-protein diets may tout weight loss, but this type of weight loss
may only be short-term. Excess protein consumed is usually stored as fat, while the
surplus of amino acids is excreted. This can lead to weight gain over time, especially if
you consume too many calories while trying to increase your protein intake. A 2016
study found that weight gain was significantly associated with diets where protein
replaced carbohydrates, but not when it replaced fat.
b. Bad breath- Eating large amounts of protein can lead to bad breath, especially if you
restrict your carbohydrate intake. Brushing and flossing won’t get rid of the smell. You
can double your water intake, brush your teeth more often, and chew gum to counter
some of this effect.
c. Constipation- High-protein diets that restrict carbohydrates are typically low in fiber.
Increasing your water and fiber intake can help prevent constipation. Tracking your
bowel movements may be helpful.
d. Diarrhea- Eating too much dairy or processed food, coupled with a lack of fiber, can
cause diarrhea. This is especially true if you’re lactose-intolerant or consume protein
sources such as fried meat, fish, and poultry. Eat heart-healthy proteins instead. To
avoid diarrhea, drink plenty of water, avoid caffeinated beverages, limit fried foods and
excess fat consumption, and increase your fiber intake.
e. Dehydration
Your body flushes out excess nitrogen with fluids and water. This can leave you
dehydrated even though you may not feel more thirsty than usual. A 2006 study
concluded that consuming more protein had a minimal impact on hydration. This risk or
effect can be minimized by increasing your water intake, especially if you’re an active
person. Regardless of protein consumption, it’s always important to drink plenty of water
throughout the day.
f. Kidney damage- Excess protein can cause damage in people with preexisting kidney
disease. This is because of the excess nitrogen found in the amino acids that make up
proteins. Damaged kidneys have to work harder to get rid of the extra nitrogen and
waste products of protein metabolism.
g. Increased cancer risk- Certain high-protein diets that are particularly high in red
meat-based protein are linked to an increased risk of various health issues, including
cancer. Eating more red and/or processed meat is associated with colorectal, breast,
and prostate cancer. Conversely, eating protein from other sources has been
associated with a decreased risk of cancer. Scientists believe this could be due, in part,
to hormones, carcinogenic compounds, and fats found in meat.
h. Heart disease- Eating lots of red meat and full-fat dairy foods as part of a high-
protein diet may lead to heart disease. This could be related to higher intakes of
saturated fat and cholesterol. According to a 2010 study, eating large amounts of red
meat and high-fat dairy was shown to increase the risk of coronary heart disease in
women. Eating poultry, fish, and nuts lowered the risk. A 2018 study also showed that
long-term consumption of red meat can increase trimethylamine N-oxide (TMAO), a gut-
generated chemical that is linked to heart disease. Findings also showed that reducing
or eliminating dietary red meat reversed the effects.
i. Calcium loss- Diets that are high in protein and meat may cause calcium loss. This is
sometimes associated with osteoporosis and poor bone health. A 2013 review of
studies found an association between high levels of protein consumption and poor bone
health. However, another 2013 review found that the effect of protein on bone health is
inconclusive. Further research is needed to expand and conclude upon these findings.
What’s normal?
The ideal amount of daily protein that you should consume varies depending on a
number of factors, including age, gender, activity, health, total diet and other variables.
However, in most cases, the recommended daily amount of protein for adults can be
calculated based on your body weight. For most adults with minimal physical activity,
experts recommend consuming a minimum daily average of 0.8 grams of protein per
kilogram (kg) of body weight. If you exercise primarily with weights or body weight for
more than one hour most days of the week, you may do well eating up to 1.2 to 1.7
grams per kg of body weight each day. However, some people, including elite athletes,
may be able to eat as much as 3.5 g per kg of body weight without any side effects. In
general, experts also believe that most healthy adults can tolerate eating 2 g of protein
per kg of body weight per day over the long term. While others believe that otherwise
healthy adults can safely consume even higher levels of protein regardless of activity
level, this hasn’t been extensively studied over the long term.
5. Solve and come up with the estimated daily protein needs of persons with the
following Conditions:

ESTIMATING INDIVIDUAL PROTEIN REQUIREMENTS

Let’s say for instance a person who weighs 65 kg.
5.1 Fever, fracture, infection
For a person with Fever, fracture, infection who weighs 65 kg, the protein
requirement equals 97.5 g.
1.5 g•kgʌ-1 X 65 kg = 97.5 g

5.2 Protein depleted

The same person with a chronic infection or in a protein-depleted state would
require an upper-range estimate of 130 g of protein daily.
2.0 g•kgʌ-1 X 65 kg = 130 g

5.3 Extensive burns

The same person with an Extensive burns state would require an upper-range
estimate of 195 g of protein daily.
3.0 g•kgʌ-1 X 65 kg = 195 g

5.4 Intensive training

The same person with an intensive training would require an upper-range estimate
of 52 g of protein daily.
0.8 g•kgʌ-1 X 65 kg = 52 g