Protein Digestion < begins at the stomach rather than proteins exposes their internal peptide bonds,

the mouth because the saliva does not contain any making them more susceptible to enzymatic
enzymes that affect proteins hydrolysis by enzymes like pepsin.
3. its acidity leads to the activation of pepsinogen,
Kasi in the mouth the saliva primarily targets
which is the inactive form of the digestive enzyme
carbohydrates, not proteins.
pepsin
The enzyme, salivary amylase, found in the mouth starts - Pepsinogen is the inactive precursor of the
the digestion of carbohydrates, and only has minimal enzyme pepsin. In the acidic environment of the
activity on proteins. In conclusion, the stomach, not the stomach (pH between 1.5 and 2.0), HCl activates
mouth, is the primary site for protein digestion pepsinogen by converting it into its active form,
pepsin. Once activated, pepsin plays a central
If you all can remember the Protein Denaturation and role in breaking down proteins into smaller,
Protein Hydrolysis more digestible fragments.
Protein Denaturation ← partial or complete So Kumbaga, amo nagkakamayada pepsinogen secretion
disorganization of proteins characteristic as a result to a due to the interaction of pepsinogen with hcl. Amo na
damage to its structure aactivate yung active form of pepsinogen which is
Protein Hydrolysis ← reverse of the formation of pepsin
peptide bond So yung pepsin naman, Pepsin effects the hydrolysis of
These processes both occur at the stomach approximately 10% of peptide bonds present in
proteins, producing a variety of polypeptides. = so amo
na ito na large polypeptides
Dietary Protein Intake: Small Intestine
- The process begins with the consumption of
dietary protein from food sources. - Now the partially digested food, now called
chyme, moves from the stomach to the small
(As it enters the mouth) Mouth intestine.
- Through mastication or what we call chewing - The pancreas then releases bicarbonate to
breaks down food into smaller particles. neutralize the acidic chyme, creating an optimal
However, as what I have said earlier the protein environment for enzymatic production such as
digestion does not occur in the mouth because trypsin, chymotrypsin, and carboxypeptidase.
the, enzyme, amylase, only prioritizes the - On the other hand, the Aminopeptidase is
digestion of carbohydrates produced by the small intestine
- However, all of these enzymes have the same
Stomach function which is hydrolyze or breakdown
peptide bonds of the large polypeptides into
- Thus, the partially chewed food (now called
smaller peptides and individual amino acids
bolus) enters the stomach. (where the protein
digestion takes place). Upon entering the Asya nagkamayda amino acids
stomach, it triggers the release of the hormone
gastrin. Gastrin's presence causes both Intestinal Lining
hydrochloric acid and pepsinogen secretion. - The lining of the small intestine contains tiny,
HCl's 3 Major Functions within the Stomach finger-like projections called villi and microvilli.
These structures significantly increase the
1. its antiseptic properties kills most bacteria surface area available for absorption. Amino
- The stomach is exposed to various ingested acids are absorbed into the bloodstream
microorganisms, including bacteria, viruses, and through the walls of the small intestine via
other pathogens. The highly acidic environment active transport
created by HCl helps to kill most of these
microorganisms, preventing them from causing Transport to the Bloodstream
infections or illnesses. - Once absorbed, amino acids are transported
- Also serves as the body’s defense mechanism, through the bloodstream to various cells and
protecting the digestive system tissues in the body. They are used for various
2. its denaturing action "unwinds" globular proteins, physiological processes, including the synthesis
making peptides more accessible to digestive of new proteins, energy production, and other
enzymes essential functions.
- Denaturation involves the disruption of non-
covalent bonds (such as hydrogen bonds and
hydrophobic interactions) This unfolding of
As you can observe in this table. It shows that In this reaction, the amino group from glutamate is
Nonessential Amino Acids require fewer reaction steps transferred to oxaloacetate, resulting in the
in their biosynthetic pathways than Essential Amino formation of aspartate
Acids
Then, aspartate is converted to asparagine. The
Nonessential Amino Acids: These amino acids have
Aspartate reacts with glutamine, and the amino
simpler biosynthetic pathways, requiring fewer steps for
group from glutamine is transferred to aspartate,
their synthesis.
producing asparagine
Essential Amino Acids: In contrast, essential amino acids
have more complex biosynthetic pathways, and the
human body cannot complete these pathways Tapos, The conversion of α-ketoglutarate to
efficiently, if at all
glutamate naman involves a process known as
kasi in order to obtain the essential amino acids, transamination. In this reaction, the amino group
humans are needed to consume food. Thus, this from ammonia is transferred to α-ketoglutarate,
requirement leads to multi-step reactions involved resulting in the formation of glutamate.
in the digestion of proteins.
Finally, in the production of proline and glutamine.
For proline biosynthesis, glutamate is converted to
pyrroline-5-carboxylate (P5C), which is then
Next, here in this diagram it shows the biosynthesis
reduced to proline. On the other hand, For
of the nonessential amino acids and the essential
glutamine biosynthesis, glutamate reacts with
amino acids
ammonia to form glutamine.
The starting materials for the biosynthesis of the 10
nonessential amino acids which are the glycolysis
and citric acid cycle Next let’s discuss the biosynthesis of the essential
amino acids.
First, let us discuss the glycolysis. So, in order to
obtain the amino acids, Cysteine, Glycine,. The conversion of phenylalanine to tyrosine is a
process known as hydroxylation and it involves the
The 3-phosphoglycerate is first converted to 3-
addition of a hydroxyl group to phenylalanine. The
phosphohydroxypyruvate, and then through a
enzyme responsible for this conversion is
series of reactions involving the transfer of an
phenylalanine hydroxylase. The enzyme
amino group, it is converted to phosphoserine.
phenylalanine hydroxylase catalyzes the addition of
Finally, phosphoserine is dephosphorylated to yield
a hydroxyl group (-OH) to the phenylalanine
serine.
molecule at the para position of the aromatic ring,
Then Serine naman is used as a precursor for the resulting in the formation of tyrosine.
biosynthesis of cysteine and glycine. Thus, the
production of cysteine and glycine
Phenylketonuria (PKU) is a genetic disorder that
occurs when there is a deficiency of the enzyme
Next, the conversion of pyruvate to alanine involves phenylalanine hydroxylase. This enzyme is
a process known as transamination. responsible for converting the amino acid
phenylalanine to tyrosine. In individuals with PKU,
Transamination is a biochemical process that
the lack of functional phenylalanine hydroxylase
involves the transfer of an amino group (NH2) from
leads to elevated blood levels. Then, Elevated levels
one molecule to another.
of phenylalanine and its byproducts can be toxic to
In this reaction, the amino group from glutamate is the developing brain. The central nervous system is
transferred to pyruvate, converting pyruvate into particularly vulnerable, and the accumulation of
alanine. these substances can lead to intellectual disability
and developmental delays. Specifically, it occurs
from infant – 6 yrs old. Sadly there is no cure for
So sa citric acid cycle naman, to obtain Asparagine this disease however there is treatment which is
newborn screening and strict dietary management
It first involves the The biosynthesis of aspartate
for preventing the neurological complications
from oxaloacetate which occurs through a
associated with PKU.
transamination reaction also.