LIPIDS
LIPIDS - are organic compounds of biologic origin
and in general:
1. Insoluble in water
2. Soluble in organic solvents such as ether,
acetone, chloroform and Carbon tetrachloride
3. Contain carbon, hydrogen, oxygen, and
sometimes nitrogen and phosphorous
4. In most cases, yield fatty acid and glycerol
Stru
cture of Fats and Oils /Triglycerides
Classification of Lipid based on
Biochemical Function
1. Energy storage lipid (triacyl glycerol)
2. Membrane lipid (phospholipid,
sphingoglycolipid, and cholesterol)
3. Emulsification lipid (bile acids)
4. Messenger lipid (steroid hormones, eicosanoid)
5. Protective coating lipid (biological wax)
Based upon whether or not saponification occurs
when a lipid is placed in basic aqueous solution,
lipids are divided into two categories:
1. Saponifiable lipid - are lipids that can be
converted into two or more molecules when
hydrolyzed. Examples: triacylglycerol,
phospholipids, sphingoglycolipids and
biological wax.
2. Non saponifiable lipid - cannot be broken
down into smaller units, since they do not react
with water. e.g. Cholesterol, steroid hormones,
bile acids, and eicosanoids.
____________________________________
FATTY ACID – product of fat hydrolysis
Classification of Fatty Acid
1. Saturated fatty acid - fatty acid containing
single bond. Examples: lauric acid, palmitic acid,
myristic acid and stearic acid
2. Unsaturated fatty acid - fatty acid that contains
double bond.
Unsaturated fatty acid made;
a. Monounsaturated - contains one double
bond; e.g. Palmitoleic acid and oleic
acid.
b. Polyunsaturated - contains two or more
double bond. e.g. linoleic acid, linolenic
acid, arachidonic acid.
Physical Properties of Fatty Acid
1. Short chain fatty acid is slightly soluble in water
2. Long chain fatty acid is generally insoluble in
water.
3. As carbon atom increases, melting point
increases.
4. Long chain fatty saturated fatty acid is solid at
room temperature.
5. Long chain unsaturated fatty acid is liquid at
room temperature
6. Increasing degree of unsaturation, decreases the
melting point.
TRIACYLGLYCEROL - is an energy storage
lipid formed by esterification of three fatty acids:
1. Simple triacylglycerol - triester formed from
esterification of glycerol with and three identical
fatty acid molecules; e.g. Glycerol tristearin
2. Mixed triacyl glycerol - triester formed from
the esterification of glycerol with more than one
kind of fatty acid; e.g. Oleo - palmito – stearin.
Saturated fats
- bad fats - can increase heart disease risk
Monounsaturated fats
- good fats - decrease both heart disease and breast
cancer risk
- Help reduce the stickiness of blood platelets and
also help prevent the formation of blood clots and
may also dissolve clots once they form.
Polyunsaturated fats - both good fats and bad fats
____________________________________
PHOSPHOLIPIDS
- are found in all cell membrane as bilayer and
responsible for the passage of various substance in
and out of the cell
- contains fatty acid, an alcohol, a nitrogen
compound and a phosphoric acid.
- Found in all tissues in the human body particularly
in brain, liver, spinal tissue, and cell membrane.
Responsible for passage of various substances into
and out of the cell.
Categories of Phospholipid
1. Phosphoglycerides
a. Phosphatidylcholine (lecithin)
- important in the metabolism of fat by the
liver and also source of phosphoric acid
which is needed or the formation of new
tissues.
b. Phosphatidylethanolmine (cephalins)
- important in blood clotting and also source
of phosphoric acid for the formation of new
tissues.
2. Phosphosphingosides
a. Sphingomyelins – present in large amount
in brain, liver and nerve tissues.
Accumulation of sphingomyelin results in
mental retardation and early death cause by
lack of enzyme sphingomyelinase.
Niemann-Pick disease - a disease of infancy or
early childhood due to the accumulation of
sphingomyelin in the brain, nerve and spleen.
____________________________________
GLYCOLIPIDS
- are called cerebroside, they found in large amount
in nerve tissues
- The structure is similar to sphingomyelin except
that they contain often galactose in place of choline
and phosphoric acid.
Gauchers’ Disease
- the accumulation of glycolipid in the brain can
cause mental retardation at the age of three.
Juvenile and adult form of this disease are
characterized by the enlarged spleen and kidneys.
hemorrhaging, mild anemia and fragile bones.
____________________________________
EICOSANOIDS - biologically active compounds
derived from arachidonic acid. They are extremely
potent compound with a variety of actions.
1. Prostaglandin - They are derived from
arachidonic acid which is formed from the
nutritionally essential fatty acid linolenic acid.
 It has been isolated from most mammalian
tissues, including male and female reproductive
system, liver, kidneys, pancreas, heart, lungs,
brain, and intestine. The richest source of
prostaglandin is the human seminal fluid.
Prostaglandin have a wide range of physiological
effect:
a. Involved in the body’s defense against all forms
of change including those induced by chemical,
mechanical, physiologic and pathologic stimuli.
b. Prostaglandin are involved in the cellular level
in regulating body function, including gastric
acid secretion, contraction and relaxation of
smooth muscle, inflammation and vascular
permeability, body temperature and blood
platelet aggregation.
2. Prostacyclin - a potent inhibitor of platelet
aggregation and is a powerful vasodilator.
3. Thromboxane - have an effect opposite to that
of prostacyclin. They are potent aggregators of
blood platelet and have a profound contractive
effect on a variety of smooth muscles.
Both prostacyclin and thromboxane exert their
influence by regulating the production of Camp,
with the thromboxane acts as inhibitor and
prostacyclin as stimulator
4. Leukotriene - found in leukocytes (white blood
cells). Various inflammatory and
hypersensitivity (allergy) responses are
associated with elevated levels of leukotrienes.
STEROIDS - high molecular mass tetracyclic
compound with one or more (-OH) group. The most
common sterol is cholesterol which are found in
animal fat. Found in animal tissues in the brain and
nerve tissues in the bloodstream and in gallstone.
Cholesterol - found in all animal tissues,
particularly in the brain and nerve tissue in
the blood stream and in gallstone. It aids in
the absorption of fatty acid from small
intestine.
Atherosclerosis - form of arteriosclerosis,
result from the deposition of excess lipids,
primarily triglyceride and cholesterol from
the blood stream
The normal cholesterol level in human is 200 -
220 mg/Dl, with slightly higher levels being normal
for normal individuals.
Other Steroids:
1. Bile salts - oxidation product of cholesterol. It is
a primary component of bile. It helps in the
digestion of fats in our body and also helps to
absorb fat soluble vitamins like A, D, E and K
2. Sex hormone
3. Hormone of the adrenal cortex
4. Ergosterol - when exposed to ultraviolet
radiation one of the product formed is calciferol
(vitamin D2)
Steroid Hormone
- hormone that is the derivative of cholesterol
1. Sex hormone
2. Adrenocorticoid hormone
Sex hormone
1. Estrogen - female sex hormone
2. Androgen male sex hormone
3. Progestin - the pregnancy hormone
Adrenocorticoid Hormone
1. Mineralocorticoid Hormone – control the
balance of Na+ and K+ in cells and body fluids
2. Glucocorticoid Hormone – control glucose
metabolism and counteract inflammation
WAX – is a compound produced by the reaction of
a fatty acid with high molecular mass alcohol.
Water insoluble and nonreactive, hence waxes make
excellent protective coatings
Examples:
1. Beeswax - honeycomb of bee
2. Spermaceti - sperm whale
3. Carnauba - carnauba palm
4. Lanolin - Wool
5. Chinese wax - in the cuticle leaves
6. Cholesterol palmitate - In blood plasma
Physiological Importance of Wax: 1. Iodine number - the number of grams of
1. It serves as a protective agent on the surface of iodine taken up by 100 grams of fat
plants and animals. 2. Saponification number - represents the number
2. It protects fruits from excessive loss of moisture of alkali (KOH) required to neutralize the fatty
acid contained in one gram of fat.
3. Reichert-Meissl Number - This is the amount
Fats - triacylglycerol that is solid at room of 0.1N alkali required to neutralize the volatile
temperature. fatty acids distilled from one gram of fat.
4. Acetyl number - represent the number of mg of
Oils - triacylglycerol that is liquid at room KOH necessary to neutralize the acetic acid
temperature liberated from the hydrolysis of one gram of
acetylated fat.
5. Polenske number - the number of mg KOH
FATS OILS required to neutralize the insoluble fatty acid
from 5 grams of fat.
Triglycerides made up of one
Similarities glycerol molecule and three
fatty acid molecules Essential Fatty Acid - fatty acid needed for
complete nutrition of the human body from dietary
Unsaturated /
Saturated / no sources, because it cannot be synthesized within the
one or more
C=C bonds body.
C=C bonds
1. Linoleic acid
Saturated 2. Linolenic acid
Unsaturated Linoleic acid is the primary member of the omega-
Differences chains packed
chains packed 6- fatty acid and linolenic acid is the primary
closely
less closely member of omega-3 fatty acid. These two acids are
together
needed for proper membrane structure and also
Solids at room Liquids at serve as a starting material for the production of
temp room temp several biochemically active important long chain
omegas-6 and omega-acids.

Importance of Essential Fatty Acids

Uses of Fat
1. Fat serve as the reserve supply of food energy
for the body
2. Fat is stored in adipose tissue and serve as
protector of the vital organs.
3. Fat in the outer layer of the body acts as heat
insulators
4. Fat acts as electrical insulator and allow rapid
propagation of nerve impulses.
5. Fats are constituents of lipoprotein, which are
found in the cell membrane, and in the
mitochondria and also serve as a means of
transporting lipids in the blood stream
Identification of Fat
1. Needed for proper membrane structure.
2. Serve as starting materials for the production of
several biochemically important longer-chain
omega-6 and omega -3 acids
Linoleic acid is the starting material for the
biosynthesis of arachidonic acid
Arachidonic acid is the major starting material for
Eicosanoid - substances that helps regulate blood
pressure, clotting and several other important body
functions.
Linolenic acid - is the starting material for the
biosynthesis of two additional omega-3 –fatty acids.
1. Eicosanopentanoic acid
 2. Docosahexamoic acid
These two acids are important constituents of the
communication membrane of the brain and are
necessary for normal brain development. They are
also active in the retina of the eye.
Omega-3 fatty acid - unsaturated fatty acid
with its endmost double bond three carbon atoms
away from the methyl end.
Omega-6 fatty acid - unsaturated fatty acid
with its endmost double bond six carbon atoms
away from the methyl end
Chemical Reactions of Triacylglycerol
1. Hydrolysis- triacylglycerol or fat reacts with
water to produce fatty acid and glycerol
2. Rancidity – fats develops an unpleasant odor
and taste when allowed to stand at room
temperature.
3. Hydrogenation – the addition of hydrogen to
double bond. Example vegetable can be
converted to fat by the addition of hydrogen in
the presence of catalysts in the process known
as hydrogenation.
4. Saponification – heating of fat with strong base
such as sodium chloride to produce glycerol and
salts of fatty acid (soap)
MIDTERM LAB 1: Qualitative Test for Lipids
1. Solubility Test
- the preliminary test which detects the presence
of all lipids
- lipids are readily miscible in non-polar
solvents like chloroform, partially soluble in a
polar solvent like ethanol and immiscible in a
polar solvent like water.
PROTEINS
PROTEINS - are compounds of high molecular
mass consisting largely of chains of alpha amino
acids united by peptide bonds. It is a component of
all living cells and is synthesized by the cell to
affect growth. Upon hydrolysis proteins will be
broken down into its basic building blocks, the
amino acids
Functions of Protein
2. Translucent Spot Test
- a preliminary test for the lipids which can be
detected by the appearance of a translucent and
greasy spot. The lipid will form a greasy spot as
they are having a greasy texture that will
penetrate into the filter paper.
3. Acrolein test
- used to detect the presence of glycerol and fat
- the reaction between glycerol and potassium
hydrogen sulphate results in the formation of
“Acrolein” that is characterized physically by
the release of the pungent smell.
4. Hubl’s Test
- used to know the degree of unsaturation of the
given samples.
- When reacting with Hubl's reagent, oils
resulting to a violet color of iodine is
unsaturated and if the color persists then the
given fat or oil is saturated.
Linseed oil – unsaturated
Cotton seed oil - saturated
5. Salkowski’s Test
- used to detect cholesterol in a solution. It is an
important test used to detect cholesterol
depending on the colors (distinct and clear
colors) that yield from the reaction of
cholesterol with concentrated sulfuric acid.
6. Libermann-Buchard’s Test
- also called acetic anhydride test
- used for the detection of cholesterol. The
formation of a green or green-blue color after a
few minutes is positive.
1. Protein function in the body in building new
cell, maintenance of existing cells, and
replacement of old cells.
2. Proteins are important type of compound in the
body.
3. Valuable source of energy in the body.
4. Protein are involved in catalysis of biochemical
reactions
5. Protein are involved in the transfer of oxygen.
6. Protein s are component of hair, and nails as
well as connecting and supporting tissue.
7. Proteins are also involved in the transmission of
hereditary characteristics.
AMINO ACIDS
- are organic compounds that contains an amine and
carbonyl functional group, along with side chain
specific for each amino acid. The key element of an
amino acids is carbon, hydrogen, oxygen and
nitrogen. There are 20 known amino acids one is
not optically active, glycine.
- building blocks for protein
Nonoptically Active Cysteine – unique
Amino Acid amino acid due to the
presence of sulfuhydyl
group
Zwitterion Form of Amino Acid
Amphoteric Nature of Amino Acid
Amino acids contain carbonyl (COOH) group
which is acidic, and the amino (–NH2) group. In
solution, the carbonyl group can donate hydrogen
ion to the amino group, forming a dipolar ion called
the zwitterions.
Amino acids can react to both acid and base
Amino acids are amphoteric compounds; they can
react with either acids or bases. When an amino
acid is places in basic solution, it forms a negative
charged ion that will migrate towards a positive
electrode. In an acid solution, the amino acid forms
a positively charged ion that will be attracted to
negatively charged electrode
Isoelectric point
- the pH at which the number of cations and
anions are equal.
- certain pH amino acids will not migrate toward
either the positive or negative electrode. A t this
pH, amino acid will be neutral, then there will
be equal number of positive and negative ions.
- At pH above isoelectric point, protein has more
negative than positive charge. At pH, below
isoelectric point, protein has more positive and
negative charges.
ESSENTIAL AMINO ACID - amino acid needed
for complete nutrition of the human body but cannot
be synthesized in the body. It includes; Arginine,
histidine, isoleucine, valine, leucine, lysine,
methionine, phenylalanine, threonine and
tryptophan.
NONESSENTIAL AMINO ACIDS - amino acids
that our body can synthesize. Examples: alanine,
arginine, asparagine, aspartic acid, cysteine,
glutamic acid, glutamine, glycine, proline, and
tyrosine.
Classification of Amino Acid
1. Neutral Polar Amino acids – Their molecule
have the same number of amino and carboxyl
group. And they are capable of forming
hydrogen bonding and therefore interact with
water (hydrophilic)
Examples: serine, threonine, tyrosine,
asparagine, and glutamine
2. Neutral nonpolar amino acids – their
molecules have the same number of amino and
carbonyl group. They interact poorly with water
(hydrophobic)
 Examples: Glycine, Alanine, Valine, B. B-pleated sheet – contains parallel strand of
Leucine, Isoleucine, Phenylalanine, polypeptide held together by hydrogen bond.
tryptophan, methionine, cysteine, proline. Example: Silk
3. Acidic amino acid - their molecules have more
carbonyl group than amino group, such as,
glutamic acid and aspartic acid
4. Basic amino acid - their molecule has more
amino group such as lysine, arginine, and
histidine.

3. Tertiary Structure of Protein – refers to the

folding and bending of the coil into specific
layers of fibers;
Tertiary structure of proteins is stabilized by:
PROTEIN STRUCTURE
a. Salt bridges
1. Primary Structure – refers to the number and - Protein fold so that positively charged
sequence of amino acid. Each of the very large side chains are often located adjacent to
number pf peptide and protein molecules in negatively charged side chains. The salt
biological organism have different sequence of bridge or ionic bond between the
amino acids and that allows the protein to carry charged functional groups helps stabilize
its function. the tertiary structure.
b. Hydrogen bond
2. Secondary Structure of Protein - refers to the - Folding is also stabilized by hydrogen
recurring arrangement of the amino acid chain. bonds that form between the polar
A. Alpha helix – occurs when amino acids hydrogen of one amino acid and a lone
forms a coil or spiral. The coils consist of pair of electrons on another.
loops of amino acid held hydrogen bond c. Disulfide bond
between the H and NH2 of one amino acid - Some proteins are cross-linked with
and the O of carbon C=O of the acid part of covalent bonds. The most common is a
another amino acid. Examples; hair, wool. disulfide bond between the sulfur atoms
of two cysteines. These (covalent bond)
are most common in extracellular
proteins.
d. Hydrophobic bond
- Soluble globular proteins fold so that
hydrophobic side chains are mostly
sequestered in the core of the protein.
The removal of the non-polar groups
from water (i.e. the hydrophobic effect)
 is the primary force stabilizing tertiary
structure.
4. Quartertiary structure- The highest level of
protein organization which applies to protein
with more than one poly peptide chain. It
determines how the different subunits of the
protein fit an organized whole. Examples:
Hemoglobin
MIDTERM LAB 2: Qualitative Test for Proteins
1. Biuret Test
- It is positive for all the compounds that contain
ENZYMES
Enzymes - are protein that acts as biological
catalyst that regulate the rate at which chemical
reactions provide energy in living organism without
itself being altered in the process.
In general enzymes are precipitated by
protein precipitant, like concentrated alcohol,
ammonium sulfate and trichloroacetic acid. In
solution they are colloidal in nature and are non-
dialyzable.
Biological Importance of Enzyme
more than one peptide bond like proteins,
proteoses, peptones, polypeptides, etc.
- A purplish violet color indicates a positive test.
2. Ninhydrin Test
- a test for amino acids and proteins with a free -
NH2 group. When such an -NH2 group reacts
with ninhydrin, a purple-blue complex is
formed.
3. Xanthproteic Test:
- uses a nitration reaction to determine the
presence of proteins in a solution.
- a change in color indicates a positive test.
4. Millon’s Test
- used to detect the presence of soluble proteins.
- A reddish-brown coloration or precipitate
indicates the presence of tyrosine residue which
occur in nearly all proteins.
5. Sakaguchi Test
- a chemical test used for detecting the presence
of arginine in proteins.
- A red colored complex indicates a positive
test.
6. Hopkins-Cole Test
- a chemical test used for detecting the presence
of tryptophan in proteins.
- A purple ring appears between the two layers
if the test is positive for tryptophan.
7. Sulfur Reaction or Lead Acetate Test
- This test is specific for sulphur containing
amino acids.
- The sulfur-containing amino acid such as
cysteine, cysteine, and methionine reacts
with lead acetate under alkaline conditions to
form a brown precipitate.
1. Enzymes are responsible for the different
reactions in living matter.
2. Speeds up the rate of chemical reactions to help
support life.
3. Help perform very important task like building
muscles, destroying toxins and breaking down
food particles during digestion.
 4. Rennin (the milk curding enzyme)

Classification of Enzyme
1. Oxidoreductases – enzyme that catalyze
oxidation; reduction reaction between two
substrates.
Nomenclature of enzymes: The enzyme that catalyze oxidation reactions in
A. Upon the substrate they act upon: The suffix the body are important because these reactions
“ase” is added to the name of the substrate acted are responsible for the production of energy.
upon. Examples; Many of these enzymes are present in
1. Amylase acts on starch mitochondria.
2. Maltase acts on maltose Examples: Oxidases, reductase, hydroxylase,
3. Cellulase acts on cellulose transelectronases, dehydrogenases
4. Lipase acts on lipid
5. Urease acts on urea 2. Transferases – enzymes that catalyzes the
transfer of functional group between two
B. Upon the reaction enhanced: The suffix “ase” is substrate
also added to the type of chemical reaction Examples: transaminases, transmethylases,
activated; Examples: transamidases, transpeptidases,
1. Oxidase for oxidation trasncarboxylases, transulfatases
2. Hydrolase for hydrolysis
3. Transaminase for transfer of amino group 3. Hydrolases – enzyme that catalyze hydrolysis
(transamination) reaction of carbohydrates, esters and proteins
4. Decarboxylase for removal of CO2 Examples:
(Decarboxylation) a. Carbohydrases – enzyme that catalyze the
5. Hydrase or dehydrase for reversible addition hydrolysis of carbohydrates
or removal of water  Maltase – for hydrolysis of maltose to
C. Enzyme whose names do not indicate the glucose, occurs in the intestinal juice
substance acted on or reaction enhanced.  Ptyalin or salivary amylase, for hydrolysis
1. Pepsin (gastric juice) of starch and dextrin and maltose
2. Ptyalin (in saliva)
3. Trypsin (in pancreatic juice)
  Sucrase - for hydrolysis of sucrose to
fructose and glucose: occurs in intestinal
juice.
 Lactase - for hydrolysis of lactose to
glucose and galactose: occurs in intestinal
juice.
 Amylopsin or pancreatic amylase – for the
hydrolysis of starch to dextrin and
maltose; pancreatic amylase occurs in the
pancreatic juice.
b. Esterases – enzyme that catalyze the
hydrolysis of esters into acids and alcohols
 Gastric lipase for the hydrolysis of fats to
fatty acids and glycerol
 Steapsin and pancreatic lipase for the
hydrolysis of fats to fatty acids and
glycerol
 Phosphatase for the hydrolysis of
phosphoric acid esters to phosphoric acid
c. Proteases are enzyme that catalyze the
hydrolysis of protein to derived protein and
amino acids.
These are teo types: proteinases and
peptidases
 Proteinases for the hydrolysis of proteins to
peptides
o Pepsin - found in gastric juice for the
hydrolysis of protein to polypeptide
o Trypsin found in pancreatic juice, for the
hydrolysis of protein to polypeptides
o Chymotrypsin found in pancreatic juice
for the hydrolysis of protein to
polypeptides.
 Peptidases - for the hydrolysis of
polypeptide to amino acids
o Aminopeptidases – from intestinal juice
o Carboxypeptidase from pancreatic juice
o Nucleases – are enzyme that catalyze the
hydrolysis of nucleic acids;
Examples: ribonuclease and
deoxyribonuclease
4. Lyases - are enzyme that catalyze the removal
of groups from substrate by means other than
hydrolysis, usually the formation of double
bonds
Example is fumarase; which catalyze the change
of fumaric acid to L- maleic acid in the Kreb
Cycle.
e.g. Deaminases, desulfuhydrases, dehydrases,
decarboxylase
5. Isomerases - enzyme that catalyze the
interconversion of cis-trans isomer/ or catalyze
intramolecular rearrangement.
Example is alanine racemase which catalyzes
the conversion of D-alanine to L-alanine which
is the form the body can use. Other examples
are epimerase and mutase
6. Ligases or Synthases - enzyme that catalyzes
the coupling of two compounds with the
breaking of pyrophosphate bond. Example is
the enzyme that catalyze the formation of
Malonyl CoA during lipogenesis. Examples are
carboxylase and synthetase.
Terminologies in Enzyme Chemistry
1. Substrate substance acted upon by an enzyme
Example: Starch is the substrate of amylase
2. Zymogen (proenzyme) – inactive form of an
enzyme
Pepsin - active form
Pepsinogen – inactive form
3. Activators – substances that convert the
proenzyme or zymogen (inactive form) into
active enzyme. Activators maybe inorganic
substance or organic in nature. Organic
activators are called kinases.
4. Holoenzyme - the combination of apoenzyme
and coenzyme
5. Antienzyme – substances that inhibit enzyme
activity
6. Apoenzyme – protein part of the enzyme
7. Coenzyme – non-protein part of the enzyme

Mechanism of Enzyme Action
1. Lock and key model - the substrate must fit in
with the active site in order for the reaction to
occur
2. Induced fit model – the active site must change
its conformation in order to accommodate the
incoming substrate.
Characteristic of Enzyme Action
1. High degree of Specificity – this means that an
enzyme will act only on a particular substance
or closely related substance.
Examples; Proteoses can act only on proteins
but not on fats
Classification of Specificity
A. Absolute specificity – when the enzyme
acts on one and only one substrate
Examples:
Arginase on arginine and urease on urea
B. Relative specificity – when an enzyme can
act on more than one substrate of related
structure but at different intensities.
Example:
Pancreatic lipase can hydrolyze fats with
greater rapidity but with simple esters at a
slower rate.
C. Stereochemical specificity – when an
enzyme can act on only a substance of
specific configuration.
Example: maltase can on alpha glucosidase
but not on beta glucosidase
Factors that affects Enzyme Action
A. Concentration of the substrate
B. Concentration of enzyme
C. Effect of pH
D. Effect of temperature
E. Time
F. Radiation
Activators and Inhibitors
Activators - inorganic substance that tend to
increase the activity of an enzyme
Inhibitor – is any substance that will make an
enzyme less active or render it inactive.
 1. Competitive Inhibitor – inhibitor that temperatures, the enzyme is denaturated.
compete with the substrate in binding with Therefore, more time will be taken by an
active site enzyme to digest the starch at lower and higher
2. Non-competitive Inhibitor – inhibitor that temperature.
does not compete with the substrate in binding  At 37 °C, the enzyme is most active, hence,
with the active site. takes less time to digest the starch.
 The optimum pH for the enzymatic activity of
MIDTERM LAB 4: Action of Salivary Amylase on salivary amylase ranges from 6 to 7. Above
Starch and below this range, the reaction rate reduces
Results noted: as enzymes get denaturated.
It takes less time to reach achromic point at 37°C,  Salivary amylase is most active at pH 6.8.
as the enzyme is maximum active at this Moreover, the pH 5 is acidic and pH 8 is
temperature, while at higher and lower temperatures alkaline therefore salivary amylase did not act
more time is taken to reach the achromic point. in these tubes whereas the enzyme acted in the
tube with ph 6.8 and digested the starch.
Conclusions:
 At the optimum temperature, the amylase will
break down starch very quickly.
 At low temperatures, the amylase will break
starch down slowly due to reduced kinetic
energy.
 At high temperatures, the amylase will break
starch down slowly or not at all due to
denaturation of the enzyme's active site.
 All enzymes are proteinaceous in nature.
Wherein at lower temperatures, the enzyme
salivary amylase is deactivated and at higher
Vitamins – is an organic compound, essential in small amounts for proper functioning of the
human body, that must be obtained from dietary sources because the body cannot synthesize
it.

CLASSIFICATION
1. Water soluble vitamins - C, P, B
2. Fat Soluble vitamins - A, D, E, K

WATER SOLUBLE VITAMINS

1. Vitamin C - known as ascorbic acid
2. Vitamin P - Capillary-fragility factor
3. B- COMPLEX VITAMINS ARE
a. Thiamin (Vitamin B1)
b. Riboflavin (Vitamin B2)
c. Niacin (nicotinic acid, nicotinamide, vitamin B3)
d. Pantothenic acid (vitamin B5)
e. Vitamin B6 (Pyridoxine, Pyridoxal, Pyridoxamine)
f. Biotin (Vitamin B7)
g. Folate (folic acid, vitamin B9)
h. Vitamin B12 (Cobalamin)

FAT SOLUBLE VITAMINS

1. Vitamin E or Tocopherol - natural antioxidant
2. Vitamin D – Antirachitic vitamins
3. Vitamin A – Antixeropthalmic factor
4. Vitamin K – Antihemorrhagic factor