1.
Role in nutrition and health
Dietary protein offers amino acids to support growth and specific demands as well as to
maintain the proteome's composition, structures, and functionality of the organism. Adult dietary
protein allowances for individuals and populations are derived from studies on nitrogen balance.
These are challenging to conceptualize, carry out, and understand, and the present allowances are
debatable. The true minimum protein intake necessary to maintain a healthy body composition
may not be captured in the majority of short-term (two-week) balance studies, and the
effectiveness of dietary protein utilization is noticeably understated. This is due to the adaptation
of the metabolic demand for amino acids to habitual protein intakes.
1.1 Role in nutrition
Protein, also known as protein, is a biological molecule, or macromolecule, consisting of
many amino acids linked together. Proteins perform a variety of functions within cells, including
catalytic metabolic reactions, DNA replication, response to stimuli, and transport of molecules
from one location to another. Once synthesized, proteins only exist for a certain period before
being degraded and regenerated by the cell's machinery through protein turnover. Other proteins
are involved in cell signaling, immune response, cell adhesion, and cell cycle. In animals, protein
is required in the diet to provide essential amino acids that cannot be synthesized. When digested,
it breaks down proteins for use in metabolism.
Protein is one of the important nutrients the body needs to supplement daily, helping
maintain life and improve health. Although it is important, you only need to supplement in the
right amount according to your needs. Supplementing too much can have a negative impact on
your health. As mentioned, the sequence of different amino acid chains will create different types
of proteins. In nature, there are more than 20 types of amino acids, including 9 essential types that
the human body must absorb from food sources. external product. Therefore, protein is an
important nutrient that the body needs to supplement daily but only exists for a certain period of
time. When the bonds between amino acids are destroyed, the protein is also degraded.
The roles of proteins in the body and life are very diverse, including cell structure structure,
body maintenance and development; participates in the transport of oxygen and nutrients; helping
protect the body; and providing the main daily amount of energy for the body because protein
accounts for about 10 - 15% of the basic diet, providing a large amount of energy for cells, for the
body to function and maintain life. In addition, protein also helps balance pH in the body to ensure
the circulatory system transports ions more easily. In addition to balancing pH, Protein also pulls
water from cells and blood vessels, helping to balance and regulate water in the body.
1.2 Role in health
Almost all chemical reactions in the body are catalyzed by proteins, which also control gene
expression, make up the majority of cellular structure, influence immunological function, and are a
major component of muscle. Individual amino acids, which make up proteins, act as
neurotransmitters, hormones, and physiological process modulators. Proteins are a part of
physiology in every way. Research has a lot of interest in the connections between dietary protein
and the body's protein metabolism. Additionally, research into how protein metabolism and needs
are affected by genetic, hormonal, physical, and viral processes as well as environmental pressures
is ongoing.
The role of protein in improving resistance is through its participation in providing amino
acids, which are the raw materials of antibodies and materials that protect, heal, and regenerate cell
tissue damage. Amino acids are also components of enzymes and hormones that play a decisive
role in the body's nutrient metabolism.
The amount of protein you should eat is 1-1.13 g/kg body weight/day. Vietnamese adults
should eat 60 - 70 g of protein per day. If converted into protein-rich foods, the total amount is
equivalent to about 300 to 400 g of lean fish and lean meat. Priority should be given to choosing
protein of animal origin, which has many essential amino acids that the body cannot synthesize on
its own. Protein-rich foods with high biological value that help strengthen the immune system
include eating fish, chicken, pork, beef, eggs, shrimp, crab, milk, soybeans...
2. Function, Quantity and Quality
2.1. Function
All biological tissues and muscles are built from proteins. The significance of proteins in
giving almost all bodily tissues structure is vital. Other "jobs" are assigned to certain proteins. In
other words, while they serve specific functions including serving as transporters, antibodies,
enzymes, and more, they are not structurally a part of the body. In addition, proteins also play a
variety of roles in cells. They function as enzymes that promote structural integrity, control how
substances flow through cell membranes, ward off sickness, and organize cell signaling pathways.
Enzymes
Some proteins have an enzyme role. Enzymes are proteins that catalyze chemical processes.
A chemical reaction needs a site, and an enzyme's role is to reduce the energy and time required
for that reaction to occur (Figure 2.1). Enzymes are sometimes referred to as catalysts for this
reason. Cells undergo more than 100 chemical reactions each second on average, the majority of
which call for enzymes. Over a thousand different enzyme systems are only found in the liver.
Similar to how a lock can only be opened with a specific key, an enzyme is specific and will only
use certain substrates (or chemicals in Figure 2.1) that fit into its active site. An exclusive enzyme
is necessary for almost all chemical reactions. Fortunately, an enzyme can act as a catalyst
repeatedly even though it finally breaks down and is recreated. Enzymes are involved in every
biological process, including the digestion of food in the stomach and small intestine, the
conversion of food into cellular-useable molecules, and the synthesis of all macromolecules,
including protein.
Figure 2.1.1: Enzymes are proteins. An enzyme’s job is to provide a site for substances to chemically react
and form a product and decrease the amount of energy and time it takes for this to happen.
Hormones
Hormone production is carried out by proteins. Chemical messengers known as hormones
are created in one area of the body and then delivered via the blood to another. The hormone sends
a message to start a certain cellular process or reaction when it reaches the target tissue or portion
of the body. For instance, your blood glucose levels increase following a meal. The pancreas
releases the hormone insulin in reaction to the elevated blood sugar. Insulin informs the body's
cells that glucose is there and instructs them to take it up from the blood and either store it or use it
to create energy or macromolecules. Since hormones are primarily responsible for turning
enzymes on and off, some proteins can even control the behavior of other proteins. Many
hormones are generated from proteins, albeit not all of them are. The hormones glucagon,
melatonin, and thyroid hormone are more examples of hormones derived from proteins.
Fluid and Electrolyte Balance
A healthy protein intake permits the body's fundamental biological functions to maintain the
status quo in a dynamic environment. Maintaining the body's water distribution is referred to as
fluid balance. An excessive amount of blood water can quickly enter a tissue, causing swelling and
possibly even cell death. Always, water moves from a high-concentration area to a low-
concentration area. As a result, water gravitates toward regions that contain more other solutes,
including proteins and glucose, it. Proteins have a strong fluid-attracting property, thus they
circulate continually in the blood at high concentrations to maintain the balance of water between
the blood and cells. Protein intake deficiencies can lead to edema or swelling. Albumin is the most
prevalent protein in the blood. The presence of albumin in the blood causes the blood's protein
concentration to resemble that of cells. Toto maintain the status quo, fluid exchange between the
blood and cells is therefore not excessive but rather is kept to a minimum. The cell membrane
contains transport proteins that aid in preserving the right balance of electrolytes (such as sodium
and potassium) both inside and outside the cell.
Acid – Base (pH) Balance
In order to keep the blood's pH (a measure of how acidic or basic a substance is) in the right
range, protein is also necessary. From 0 (highly acidic) to 14 (strongly basic/alkaline), the pH scale
runs the gamut. Blood pH is kept in the somewhat basic range of 7.35 to 7.45. When the blood
becomes excessively acidic (a condition known as acidosis), it indicates that the blood's hydrogen
(H+) content is too high. Alkalosis, a condition in which the blood becomes overly basic or
alkaline, indicates that the blood's amount of H+ is inadequate. Body processes can be impacted by
even a small pH variation in the blood. Two examples of this include:
- When proteins are exposed to acids or bases the proteins change shape and stop functioning
as intended. This process of proteins uncoiling and losing their shape and function is known
as denaturation. Denaturation of proteins also occurs with exposure to heat, heavy metals,
alcohol, and other damaging substances.
- Acidic blood (from ketoacidosis) can lead to coma and/or death in extreme cases.
The body has a number of processes that keep the blood pH within a healthy range to avoid
problems. When the blood becomes overly basic, certain proteins function as buffers and release
hydrogen (H+) into the blood. If the blood becomes overly acidic, proteins can also absorb
hydrogen from the blood. Proteins keep the pH of the blood within a normal range by releasing
and absorbing hydrogen as needed.
Transport
In the transfer of nutrients, proteins are also important. Large molecules are typically not able to
get through a cell's membrane. The cell membrane has a large number of transport proteins that
help the cell take in the necessary chemicals and nutrients. Some of these proteins function as
channels, enabling certain chemicals to enter and exit cells. Others serve as one-way taxis and
need power to run.
Figure 2.1.2: Carrier proteins and channel proteins
(A) A carrier protein alternates between two conformations, so that the solute-binding site is sequentially
accessible on one side of the bilayer and then on the other. (B) In contrast, a channel protein forms a water-
filled pore across the bilayer through which specific solutes can diffuse.
Antibodies
Our immune system is built to go after and eliminate alien objects. The immune system
creates antibodies to fight off invaders when they attack the body. Antibodies are specialized
proteins that can identify an antigen, which is a distinctive chemical found in dangerous bacteria
and viruses. The antigen is destroyed when antibodies bind to it. Additionally, antibodies stimulate
other immune system components to locate and eliminate unwelcome invaders.
Figure 2.1.3: Antibodies are proteins that surround and attack foreign substances by attaching to
antigens on the surface of the foreign substance. Each antibody binds to a specific antigen; an
interaction similar to a lock and key
Wound Healing, Tissue Regeneration, and Nerve Function
Inflammation, proliferation, and remodeling are the three stages of the wound healing
process, all of which require proteins. For instance, if you suffer a minor cut, your skin will swell
up and get red. Bradykinin and other proteins widen blood vessels at the site of injury to start the
healing process. In order to halt the bleeding, a clot is formed by platelets being held together by
another protein called fibrin. Then, during the proliferation phase, cells enter the damaged tissue to
repair it by putting new collagen (protein) fibers in place. The collagen fibers aid in bringing the
edges of the wound together. More collagen is deposited during the remodeling phase, creating a
scar. Only 80% of normal, unharmed tissue is functional, including scar tissue. If a diet is
insufficient in protein, the process of wound healing is markedly slowed.
While the body goes through a distinct process known as tissue regeneration that occurs
continuously, wound healing only occurs when an injury is suffered. An precise structural and
functional replica of the old tissue is produced during tissue regeneration. In the end, fresh,
completely functional tissue takes the place of the old tissue. Cells are continuously destroyed,
fixed, and replaced. The amino acids are recycled into new proteins when the proteins in the cells
are broken down. Some cells (such as heart-muscle cells and nerve cells) do not renew at any
noteworthy numbers, whilst others (such as skin, hair, nail, and intestinal cells) do so at a relatively
high pace. When cells divide to form new tissue, numerous different proteins, including enzymes,
transport proteins, hormones, and collagen, are needed. Every three to five days, the intestine's
lining cells regenerate. Diets low in protein hinder tissue repair, which leads to a host of health
issues, such as poor nutrition digestion and absorption.
Neurotransmitters, such as epinephrine, which carry messages from one nerve cell to
another, can be created from amino acid
Energy Source
Proteins include amino acids that can be broken down and converted into energy. Protein
does not provide much of the energy needed in healthy individuals. If a person's diet is deficient in
both lipids and carbs, their body will turn to amino acids to provide energy. Proteins are removed
from the blood and body tissues (such as muscle) when they are required for energy. Deamination
is necessary for converting proteins into energy. The amine group is taken off of the amino acid
during deamination, and the nitrogen is then delivered to the kidney for excretion. Energy is
produced by metabolism of the remaining elements. It's critical to consume enough fat and
carbohydrates to prevent our bodily tissues from being broken down for energy. It's also critical to
remember that extra protein cannot be stored by the body. If you consume too much protein, you'll
excrete nitrogen; the other parts will either be used as energy or turned into fat for later use.
2.2. Quality
Protein quality is related to the capacity of dietary protein to provide nitrogen and dietary
essential (or indispensable) amino acids (EAA) to achieve nitrogen balance and support body
composition and functions1. A food's protein quality can be assessed by measuring its nitrogen
content, amino acid content, or protein directly. This is known as protein concentration or density.
Through metabolic tests that monitor nitrogen balance, one can determine the protein quality that
is suitable for human consumption. Protein efficiency ratio (PER), which measures a protein's
capacity to sustain growth in young rats, and net protein utilization (NPU), which measures a
protein's capacity to retain nitrogen, are two biological assays that have been used in laboratories
to evaluate the quality of food proteins. Protein quality can be evaluated using chemical scores,
which compare the amount of each of the nine essential amino acids (EAA) in the test protein to
the amount of that EAA in the amino acid scoring reference pattern. The computation is adjusted
by the protein digestibility-corrected amino acid score (PDCAAS) for ileal or fecal proteins or by
the digestibility of ileal amino acids for the digestible indispensable amino acid score (DIAAS).
Protein quality is important since there are variations in protein quality among dietary sources, and
some food processing and storage methods can also have an impact. The highest protein
concentrations in vegetables are found in pulses, which range from 20% to 25% dry weight in
most raw beans and peas to about 36% dry weight in soy beans. Cereal seeds have a protein
content of 15-20% dry weight. Animal products are high in protein (30–70% dry weight). Animal
products have 100% true protein or amino acid digestibility and a well-balanced amino acid
composition, both of which are characteristics of foods of animal origin. The digestibility of
proteins in natural vegetable diets ranges from 70 to 85%, and almost all vegetable foods contain
one or more limiting amino acids.
1
Daniel Tomé (2023), Protein quality and sources, Encyclopedia of Human Nutrition (Fourth Edition), Elsevier, Pages 559 –
567, https://doi.org/10.1016/B978-0-12-821848-8.00028-7
2.3. Quantity
The United States National Health and Nutrition Examination survey (NHANES) (2009-
2010) suggests protein intake ranges from 14 to 16 percent of energy intake. Summing across age
(n=23,876 adults ≥19 years) and gender groups using NHANES data from 2001-2010, Pasiakos et
al reported deciles of usual protein intake ranged from a median of 0.68 to 1.51 g/kg body weight,
and that most Americans consume at least the recommended dietary allowance (RDA) for the
protein of 0.8 g/kg body weight/day. However, fewer overweight and obese individuals met the
RDA for protein, and analyses were not stratified by age, so it remains unclear what percentage of
older, overweight individuals are meeting the RDA for protein.
Moreover, there has long been discussion regarding whether the daily requirement for
protein, which is 0.8 g/kg body weight, rises with age. Recent reviews by international expert
committees and other researchers have shown that older adults in particular need to consume
enough protein for a number of reasons. 1) Anabolic resistance, or the decreased sensitivity of
muscle to amino acids from dietary sources due to factors like decreased uptake by muscle,
reduced signaling for protein synthesis, and decreased digestive capacity; 2) Inflammatory
conditions that cause increased metabolism of dietary protein (i.e. heart failure) and/or 3)
Prolonged muscle inactivity (i.e. due to injury or bed rest) may increase muscle protein
breakdown.
Sufficient consumption of protein from food is crucial, particularly for elderly individuals,
as it is believed to be essential for maintaining fat-free mass (FFM). It has been determined that
low FFM is a separate risk factor for both mortality and functional impairment. FFM is frequently
used as a stand-in for skeletal muscle mass in large-scale research. But if connective tissue grows
as a result of aging or obesity, FFM—which is a heterogeneous compartment that includes organ
mass and portions of connective tissue—may stay stable in a person with decreased skeletal
muscle mass. Researchers have scaled fat mass (FM) and its inverse, fat free mass (FFM) to height
squared in order to account for body size. This has resulted in the creation of two indexes:
FM/height2 (FMI) and FFM/height2 (FFMI). Consequently, body mass index (BMI) would be
equal to the sum of the FFM and FMI. However, excess adiposity is not taken into account when
utilizing height as a scale for body size in overweight and obese people. FFM expressed as a
percentage of total body mass has been one alternative parameterization used to account for body
size.
Given the uncertainty about protein intakes among older adults, particularly among
overweight and obese adults, the purpose of this analysis was to examine the associations between
meeting the RDA for protein intake (>0.8 grams per kilogram body weight per day) and body
composition measures among a multi-ethnic urban population of older adults. Due to differences in
methodology of measuring body composition, several measures relating to FFM and FM were
examined.
3. Deficiency
The term ‘protein deficiency’ represents a state of relative or absolute deficiency of body
proteins or one or more of the essential amino acids. ‘Protein turnover’ reflects the balance of
protein degradation and resynthesis. When there is more breakdown than synthesis, lean tissues are
burned; conversely, when there is more synthesis than breakdown, lean tissues are built. There is
variation in the quantitative relationship between the concentrations of circulating amino acids and
their rate of catabolism in both people and diets. The rate of amino acid catabolism increases or
decreases overall depending on the continuous high or low protein consumption; this rate is
partially independent of the amounts of amino acids in the blood. While a diet lacking in protein is
the primary cause of protein shortage, the condition can also frequently arise in a range of
pathologic situations. A thorough assessment of the underlying illness is essential for the
nutritional treatment of protein insufficiency, with balanced energy-protein and micronutrient
supplementation serving as the cornerstone of the regimen.
Protein shortage is typically coupled with energy insufficiency, specifically fat and
carbohydrate deficiencies, or protein-energy malnutrition (PEM). PEM can cause a variety of
clinical symptoms in both humans and animals that are undernourished. In terms of function, the
body is divided into two differently regulated protein compartments: the visceral compartment,
which is represented by protein storage in the visceral organs, mainly the liver, and the somatic
component, which is represented by proteins in the skeletal muscles. Energy (calories from carbs
and fats) is the main limiting factor when the somatic component is mostly affected, and the
disease is called marasmus. Kwashiorkor is the disease syndrome that results when the visceral
component is mostly impacted and PEM is the main limiting dietary factor. This condition has
more concerning implications because it depletes both the visceral and somatic protein supplies.
This causes internal organ atrophy in addition to muscle atrophy. In addition to generalized
wasting, serous atrophy of visceral and peripheral fat stores, anemia, abnormal bone growth,
endocrine atrophy, cerebral atrophy, bone marrow hypoplasia, fatty liver, thymic and lymphoid
depletion, intercurrent infections, and skin lesions, plasma protein concentrations decrease in
kwashiorkor. In domestic and laboratory animals generalized edema may not be evident, but
serous atrophy of fat, visceral organ atrophy, anemia, poor hair coat, and predisposition to
infectious disease are prominent features of protein (PEM) and/or protein/carbohydrate
malnutrition. Adverse changes attributable to PEM can be subtle and difficult to assess in a
qualitative fashion histologically. Changes such as atrophy of fat can be discerned as an increase in
myxomatous tissue with high ground substance in places where mature adipose tissue normally
would be found, but other changes, such as atrophy of adipose cells within organs, can be more
difficult, and sometimes impossible without ancillary techniques such as organ to body weight
ratios and morphometry.
On the other hand, moderate protein restriction without malnourishment has an additional
effect linked to the mitigation or control of long-term illnesses like chronic kidney disease. Since
both generally occur together, it can be challenging to distinguish between the reduction of protein
intake and overall calorie restriction (DR). In terms of cancer, DR (which typically includes caloric
restriction as well) can lower the incidence and/or vulnerability to cancer in the majority of tested
species, whether it is induced or spontaneous. Reduced consumption of protein and energy has
generally prevented or postponed the development of both chemically and spontaneously induced
tumors as well as transplantable tumors. The evidence for protein restriction as a major means of
preventing cancer is far from unequivocal, and the complicated interactions among protein,
carbohydrate, and fat intake and therefore overall caloric or energy restriction leading to
prevention of cancer have yet to be resolved.
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