ENZYMES EXAMPLES OF ENZYMES IN THE DIGESTIVE SYSTEM
 proteins which speed up a reaction, called
CATALYSTS
 vital to the regulation of the metabolic
processes of the cell
 enzymes often end in -ase
TYPES OF ENZYMES
ACCORDING TO THE REACTIONS
THEY CATALYZE
1. Oxidoreductases
 bring about oxidation and reduction reactions
 electrons in the form of hydride ions or
hydrogen atoms are transferred
2. Transferases
 responsible for transferring function groups
from one molecule to another
 some transferases also transfer phosphate
groups between ATP and other compounds
3. Hydrolases
 catalyze reactions that involve the process of
hydrolysis and break single bonds by adding
water
 some function as digestive enzymes because
they break the peptide bonds in proteins
4. Lyases
 catalyze reactions where functional groups are
added to break double bonds in molecules or
where double bonds are formed by the
removal of functional groups
5. Isomerases
 catalyze the reactions where a function group
is moved to another position within the same
molecule such that the resulting molecule is
actually an isomer of the earlier molecule
6. Ligases
 perform a function that is opposite to that of
the hydrolases
 form bonds by removal of the water
component
IUB Classification Of Enzymes
 Lipase (breaks down lipids)
 Amylase (breaks down starch)
 Protease (breaks down proteins)
MODELS OF ENZYMES
1. Lock and Key Model (1894)
 suggested by Emil Fischer
 suggests that the enzyme and the substrate
possess specific complementary geometric
shapes that fit exactly into one another
2. Induced Fit Model (1958)
 suggested by Daniel Koshland
 suggests that the active site continues to
change until the substrate is completely bound
to the active site of the enzyme
ACTIVE SITE
 specifically shaped area where items called
the SUBSTRATE can bind
 changes shape to bind to the substrate
perfectly in a process called INDUCED FIT
 can either build up or break down the
substrates that bind to it
a) The enzyme and the substrate are
in the same area. Some situations
have more than one substrate
molecule that the enzyme will
change.
b) The enzyme grabs on to the
substrate at a special area called
the active site. The combination is
called the ENZYME/SUBSTRATE
COMPLEX.
c) A process called catalysis happens.
Catalysis is when the substrate is
changed. It could be broken down
or combined with another
molecule to make something new.
It will break or build chemical
bonds. This is called the
ENZYME/PRODUCT COMPLEX.
d) The enzymes release the product.
When the enzyme lets go, it
returns to its original shape. It is
then ready to work on another
molecule of substrate.
 FACTORS AFFECTING EZYME ACTIVITY
1. Temperature
 higher temperature generally makes for higher
rates of reaction
 increasing or decreasing the temperature
outside of a tolerable slows reaction
 very high temperatures (for animal enzymes,
above 40°C or 104°F) may cause an enzyme
to DENATURE, losing its shape and activity
 optimum temperature level is usually the
normal temperature of the body (37°C)
Note that normal body temperature can range from
36.1°C to 37.2°C.
 below 37°C (SUB-OPTIMAL)
 37°C (OPTIMAL)
 50-60°C (ENZYME DENATURES)
2. pH Level
 active site amino acid residues often have
acidic or basic properties that are important for
catalysis
 changes in pH can
affect these
residues and make
it hard for
substrates to bind
 low pH is acidic
while high pH is
basic (alkaline)
 enzymes work best
in a fairly narrow pH
range
 if the environment
surrounding an
enzyme becomes too acidic or too basic, the
enzyme’s shape and function will suffer
3. Inhibitors
 presence of certain substances that inhibit the
action of a particular enzyme
 Occurs when inhibiting substances attaches
itself to the active site thereby preventing the
substrate attachment, slowing down the
process
4. Concentration of enzymes and substrates
 rate of reaction increases with increasing
substrate concentration up to a point, beyond
which any further increase in substrate
concentration produces no significant change
in reaction rate
SOURCES OF ENZYMES
1. Animal-based enzymes
 “Law of Similars” hypothesizes that although
the source of animal-based enzymes we
consume does not originate from a human
body, it is thought to be similar enough for the
human body to recognize and utilize
 majority of animal byproducts we consume are
processed, destroying natural enzymes
 function exclusively within a limited pH level
range and become unstable in a low pH
(acidic) level
2. Plant-based enzymes
 fruits and vegetables are commonly consumed
in their raw, natural form
 effective over a broad scope of pH levels
(between 3.0 and 9.0)
 well-suited for supporting comprehensive
digestive health
 four important enzymes often found in plants
are protease, amylase, lipase and cellulose
 fruits and vegetables are an ideal source for
enzymes
3. Fungal enzymes
 critical in the production and preparation of
many food products
 commonly produced from a fungal source
called Aspergillus
 can contain a variety of enzymes, such as
protease, amylase, lipase, cellulase and
tilactase
 acid stable and can survive within the pH
range of the stomach
 suitable for a vegetarian diet, unlike animal-
source enzymes
EXAMPLES OF NATURALLY DIGESTIVE ENZYMES
1. Pineapple
 contain a group of digestive enzymes called
bromelain
 these enzymes are proteases, which break
down protein into its building blocks, including
amino acids
2. Mango
 contain the digestive enzymes amylases, which
are a group of enzymes that break down carbs
from starch (a complex carb) into sugars like
glucose and maltose
 amylase enzymes in mangoes become more
active as the fruit ripens
3. Other examples
 Papaya
 Honey
 Ginger
 Miso
ENZYME DEFICIENCIES
1. Mucopolysaccharidoses (MPS)
 group of inherited diseases in which a
defective or missing enzyme causes complex
sugar molecules to accumulate in cells
 progressive damage is done to the heart,
bones, joints, respiratory system and central
 nervous system
 signs and symptoms develop with age as more
cells become damaged
 divided into three broad groups based on
severity of symptoms—Hurler, Hurler-Scheie,
and Scheie (in decreasing order of severity)
2. Lysosomal Storage Diseases (LSD)
 group of approximately fifty inherited disorders
that occur when a missing enzyme results in
the body’s inability to recycle cellular waste
 severity of the disorder depends on the type
and amount of cellular debris that
accumulates, but almost all disorders are
progressive
 affected individuals often have intellectual and
developmental disabilities, cloudy corneas,
short stature, stiff joints, incontinence, speech
and hearing impairment, chronic runny nose,
hernia, heart disease, hyperactivity,
depression, pain and a dramatically shortened
life span
3. Nieman-Pick Disease (NPD)
 Nieman-Pick Disease refers to a group of
inherited metabolic disorders known as lipid
storage disorders
 patients diagnosed with these disorders lack a
critical enzyme necessary to metabolize fatty
substances in the body called lipids
 as result, harmful quantities of lipids
accumulate in the spleen, liver, lungs, bone
marrow and brain
 Symptoms may include lack of muscle
coordination, brain degeneration, learning
problems, loss of muscle tone, etc
CHEMICAL NATURE OF ENZYMES
 all known enzymes are proteins
 have high molecular weight compounds made
up principally of chains of amino acids linked
together by peptide bonds
 enzymes can be denatured and precipitated
with salts, solvents and other regents
 have molecular weights ranging from 10,000
to 2,000,000
 many enzymes require the presence of other
of compounds called COFACTORS and
COENZYMES
COFACTORS + COENZYMES
 may bind to the active site which help the
enzymes build up or break down substrates
into products
 cofactors are typically metal ions (ex. iron),
while coenzymes are organic molecules (ex.
vitamins)
COENZYMES
 many are called vitamin-derived coenzymes
formed form the vitamins that are part of our
diet
 Act as agents for transferring different groups
such as electrons or molecules during reactions
TYPES OF COENZYMES
1. NAD/NADP
 nicotinamide adenine dinucleotide (NAD) and
nicotinamide adenine dinucleotide phosphate
(NADP) are derivatives of the B-vitamin,
nicotinic acid
2. Flavin Mononucleotide (FMN) and Flavin
Adenine Dinucleotide (FAD)
 commonly called flavoproteins
 hydrogen transferring coenzymes associated
with hydrogenases
 contain the B-vitamin, riboflavin
 more tightly bound to the apoenzyme, and
cannot be separated by dialysis
3. Coenzyme A (CoA)
 has a complex structure consisting of an
adenosine triphosphate, a pantothenic acid
which is a B-vitamin and cysteamine
 involved in the transfer of acyl-groups
 one of the most important CoA derivatives is
the sulfhydryl
 (-SH) group of cysteamine moiety of this
coenzyme forming a thioester with the
carboxyl
 (-COOH) group of the acyl-compound to
produce acetyl-CoA
 thioester bond is energy-rich and can easily
transfer the acetyl- group to an acceptor
RDA OF LIPASE
 500 lipase units/kg per meal initially (up to the
maximum dose) for adults
 dose should not exceed 2,500 lipase units/kg
per meal, 10,000 lipase units/kg per day, or
4,000 lipase units/g of fat ingested per day
 1,000 lipase units/kg per meal initially (up to
the maximum dose) for children older than 12
months but younger than 4 years
 dose should not exceed 2,500 lipase units/kg
per meal, 10,000 lipase units/kg per day, or
4,000 lipase units/g of fat per day
 500 lipase units/kg per meal initially (up to the
maximum dose) for children older than 4 years
 dose should not exceed 2,500 lipase units/kg
per meal, 10,000 lipase units/kg per day or
4,000 lipase units/g of fat per day