MC 2
• Enzymes are specific to their
COVERAGE (LEC AND
LAB):
1. Enzymes
2. Vitamins
3. Carbohydrates
4. Lipids
ENZYMES (LEC)
Enzymes as Biological Catalysts
Enzymes
• proteins that increase the rate of
reaction by lowering the energy of
activation (which is the energy
needed for a reaction to take place;
convert reactants to product)
• They catalyze nearly all the
chemical reactions taking place in
the cells of the body.
• Enzymes have unique three-
dimensional shapes that fit the
shapes of reactants (substrates)
• Biochemical reaction because
enzymes see in biological cells
(examples: cellular respiration,
digestion, metabolic processes)
Enzyme Structure
• They have a globular shape
• A complex 3-D structure
(Example: Human pancreatic
amylase- secreted by the pancreas
and specific for the digestion of
amylase in starch which is
substrate)
Properties of enzyme
1. Tertiary
2. Has specificity (shape of enzyme
must fit the shape of the substrate;
every enzyme has its own substrate
to catalyze
3. Globular Shape
Substrate
• The substrate of an enzyme are the
reactants that are activated by the
enzyme
substrates
• The specificity is determined by
the active site
Naming Enzymes
• The name of an enzyme identifies
the reacting substance
- usually ends in –ase
• For example:
sucrase – sucrose
maltase – maltose
lipases – lipids
amylase – amylose
Proteins – Proteases
• Describes the function of
enzyme/reactions catalyzed
• For example:
oxidases – oxidation
reductases – reduction
oxido reductases – redox
decarboxylases – removal of CO2
Dehydrases – dehydration
• Common names are used, end with
-in
• For example:
Pepsin and Trypsin which
catalyze the digestion of protein
Rennin
Chymotrypsin
• Some names describe both the
substrate and the function
• For example:
Alcohol dehydrogenase – catalyze
the dehydrogenation and oxidation
of an alcohol like ethanol
(substrate).
Dehydrogenation – removal of 2
hydrogen atoms from the substrate
Oxidation - removal of 2 hydrogen atoms
and addition of oxygen
Reduction – addition of 2 hydrogen atoms
and removal of oxygen
Classification of Enzymes
Enzymes are classified according to the
type of reaction they catalyze:
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Class Reactions bonding, salt-bridges, hydrophobic
catalyzed interactions, etc.
Oxidoreductases Oxidation- • Products are released when the
sssssssssssssssssssssss reduction reaction is complete (they no
Transferases Transfer groups of longer fit well in the active site)
XXXXXXXXXXXXX atoms Enzyme Specificity
Hydrolases Hydrolysis • Enzymes have varying degrees of
Lyases Add atoms/remove specificity for substrates
atoms to/from a double • Enzymes may recognize and
aljasd,anDANJNDDNXbond catalyze:
Isomerases Rearrange atoms - a single substrate
Ligases Use ATP to - a group of similar substrates
ssssssssssssssssssssssss combine molecules - a particular type of bond
Oxidoreductases, Transferases and
Hydrolases

Note: Glucose and fructose are group

specificity because it’s hexoses and have 6
carbon atoms.
Hexoses – monosaccharides
containing 6 carbon atoms.
Linkage Specificity Examples:
Peptidases (Chymotrypsin) – for
Lyases, Isomerases and Ligases
splitting peptide bond
Lipases – splitting ester bond
Glycosidase – splitting glycosidic
bond and carbohydrates
Lock-and-Key Model
• In the lock-and-key model of
enzyme action:
- the active site has a rigid shape
- only substrates with the matching
shape can fit
- the substrate is a key that fits the
lock of the active site
• This is an older model, however,
and does not work for all enzymes
Active Site
Induced Fit Model
• The active site is a region within
• In the induced-fit model of enzyme
an enzyme that fits the shape of
action:
substrate molecules
- the active site is flexible, not
• Amino acid side-chains align to
rigid
bind the substrate through H-

2|O N G R AY N E
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- the shapes of the enzyme, active
site, and substrate adjust to maximize the
fit, which improves catalysis
- there is a greater range of
substrate specificity
• This model is more consistent with
a wider range of enzymes
Enzyme Catalyzed Reactions
• When a substrate (S) fits properly
in an active site, an enzyme-
substrate (ES) complex is formed:
E + S  ES
• Within the active site of the ES
complex, the reaction occurs to
convert substrate to product (P):
ES  E + P
• The products are then released,
allowing another substrate
molecule to bind the enzyme
- this cycle can be repeated
millions (or even more) times per minute
• The overall reaction for the
conversion of substrate to product
can be written as follows:
E + S  ES  E + P
Example of an Enzyme Catalyzed
Reaction
The reaction for the sucrase catalyzed
hydrolysis of sucrose to glucose and
fructose can be written as follows:
E + S  ES  E + P1 + P2
where E = sucrase, S = sucrose, P1 =
glucose and P2 = fructose
Isomers – molecules with same number
and kinds of atoms but different
arrangement of atoms
Epimerase – convert D-isomer to L-
isomer
Isoenzyme
- Isoenzymes are different forms
of an enzyme that catalyze the one type/
same reaction in different tissues in the
body.
- they have slight variations in the
amino acid sequences of the subunits of
their quaternary structure
- For example, lactate
dehydrogenase (LDH), which
catalyze dehydrogenation of
lactate to pyruvate, consists of five
isoenzymes which differ in the AA
sequencing in their subunits.
H Subunit – Heart M Subunit-Muscle
Tetramer – 4 subunits
Damaged tissues release LDH into
bloodstream. The presence of any form of
LDH in the blood will indicate which
tissue of our body is affected.
Cofactors
• An additional non-protein
molecule that is needed by some
enzymes to help the reaction
• Tightly bound cofactors are called
prosthetic groups
• Cofactors that are bound and
released easily are called
coenzymes (ex. ADP)
• The inorganic metallic ions such as
Na+, Fe+3 and Mg2+ are called
activators
• Many vitamins are coenzymes
APOENZYME (inactive enzyme,
protein)
- catalyze reaction if there is a cofactor
Apoenzyme + Cofactor = Holoenzyme
(Active Enzyme, Conjugated)
Diagnostic Enzymes
• The levels of diagnostic enzymes
in the blood can be used to
determine the amount of damage
in specific tissues
3|O N G R AY N E
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Enzyme Activity -how fast enzyme
catalyze reaction
Factors Affecting Enzyme Activity:
1. Temperature
2. pH
3. Enzyme Concentration
4. Substrate Concentration
5. Inhibitors
Temperature and Enzyme Activity
• Enzymes are most active at an
optimum temperature (usually
37°C in humans)
• They show little activity at low
temperatures
Activity is lost at high temperatures as
denaturation occurs.
• Beyond the optimum temperature,
the enzyme is deactivated until it
lost its activity due to denaturation
pH and Enzyme Activity
• Enzymes are most active at
optimum pH
• Amino acids with acidic or basic
side-chains have the proper
charges when the pH is optimum
• Activity is lost at low or high pH
as tertiary structure is disrupted
Optimum pH for Selected Enzymes
• Most enzymes of the body have an
optimum pH of about 7.4
• However, in certain organs,
enzymes operate at lower and
higher optimum pH values
• Pepsin in the stomach is most
active in an acidic medium
because of HCI present in stomach
(stomach is also acidic).
• Hyperacidity – too much acid in
the body
Enzyme Concentration and Reaction
Rate
• The rate of reaction increases as
enzyme concentration increases (at
constant substrate concentration)
• At higher enzyme concentrations,
more enzymes are available to
4|O N G R AY N E
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catalyze the reaction (more
reactions at once)
• There is a linear relationship
between reaction rate and enzyme
concentration (at constant substrate
concentration)
Substrate Concentration and Reaction
Rate
• The rate of reaction increases as
substrate concentration increases
(at constant enzyme concentration)
• Maximum activity occurs when
the enzyme is saturated (when all
enzymes are binding substrate)
• The relationship between reaction
rate and substrate concentration is
exponential, and asymptotes
(levels off) when the enzyme is
saturated
Enzyme Inhibitors
• Inhibitors (I) are molecules that
cause a loss of enzyme activity
• They prevent substrates from
fitting into the active site of the
enzyme:
E + S  ES  E + P
E + I  EI  no P formed
Reversible Inhibitors (Competitive
Inhibition)
• A reversible inhibitor goes on and
off, allowing the enzyme to regain
activity when the inhibitor leaves
• A competitive inhibitor is
reversible and has a structure like
the substrate
- it competes with the substrate for
the active site
- its effect is reversed by
increasing substrate concentration
Example of a Competitive Inhibitor
Malonate is a competitive inhibitor of
succinate dehydrogenase
- it has a structure that is similar to
succinate
- inhibition can be reversed by
adding succinate
Reversible Inhibitors (Noncompetitive
Inhibition)
• A noncompetitive inhibitor has a
structure that is different than that
of the substrate
- it binds to an allosteric site
rather than to the active site.
- it distorts the shape of the
enzyme, which alters the shape of the
5|O N G R AY N E
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active site and prevents the binding of the b) Classification of enzyme: Oxidase;
substrate Oxidoreductase
• The effect can not be reversed by c) Substrate: Succinate
adding more substrate, but d) Product: Fumarate
lowering the concentration of e) E.S Complex: Succinate dehydrogenase
inhibitor makes enzyme regain its – Succinate Complex
activity. 4) Aspartase
Irreversible Inhibitors a) reaction: addition of a group to a double
• Inactivates enzymes by forming bond
strong covalent bond to AA side b) Classification of enzyme: Lyases
chain in the active site c) Substrate: Fumarate
• Addition of excess substrate does d) Product: Aspartate
not reverse the inhibition process e) E.S Complex: Aspartase – Fumarate
• Enzyme is permanently Complex
deactivated
• An irreversible inhibitor destroys ENZYMES (LAB)
enzyme activity, usually by Objective:
bonding with side-chain groups in To determine the effects of temperature,
the active site enzyme concentration and pH on the
• The activity of enzyme cannot be activity of catalase and salivary amylase
regained because the inhibitor
form covalent bonds with AA and Enzy Sour Substr Reaction Equati
active site of the enzyme me ce ate Catalyzed on
• Substrate bonds with the Active 1) Pota H2O2 Decompo H2O2
Site of the enzyme by means of Catal to stion of (catala
hydrogen, hydrophobic ase hydrogen se)
peroxide H2O
interactions of ionic bond.
+ O2
Uncompetitive Inhibitor
2) Sali Starch Hydrolysi Starch
• Inhibitors that fit into the enzyme- Saliv va s of (amyl
substrate complex. ary starch ase)
ACTIVITY: Amyl maltos
1) Phosphoglyceromutase ase e
a) reaction: rearrangement of (mout
atoms/Isomerization h)
b) Classification of enzyme: Isomerase glucos
c) Substrate: 3-Phosphoglycerate e
d) Product: 2-Phosphoglycerate (stoma
ch
e) E.S complex: Phospogylceromutase – 3-
Phospoglycerate Complex The activity of catalase was measured from
2) Urease the time it took for the filter paper (w/
a) reaction: Hydrolysis catalase) to rise on the surface of the
b) Classification of enzyme: Hydrolase H2O2. The fastest filter paper rises, the
c) Substrate: Urea most active is the catalase.
d) Product: Ammonia Oxygen – pushes paper upward
e) E.S Complex: Urease – Urea Complex The activity of the amylase was measured
3) Succinate dehydrogenase from the time it took for the dark color to
a) reaction: Dehydration, oxidation fade-light brown when the heated mixture

6|O N G R AY N E
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of saliva, starch solution, HCI, or Data:
H2O/NaOH and NaCI solution is treated 4 ml catalase 5s = 1/5 = 0.2
with iodine. 3 ml catalase 10s = 1/10 = 0.1
- Denaturation happens when in high 2 ml catalase 15s = 1/15 = 0.06
temperature. 1 ml catalase 20s = 1/20 = 0.05
Procedure 2. 0 0
Effect of temperature on Catalase Interpretation: As enzyme increases
Activity (substrate conc. is constant) the activity
(controlled variable: amount of substrate, increases
enzyme Type of Graph: Linear
manipulated variable: temperature Procedure 4.
dependent variable: time) Effect of pH
Observation Time it took for (controlled variable: temperature, amount
the filter paper to of saliva, starch solution, etc)
rise dependent: time for the fading of dark
0°C 50 secs color)
(reciprocal: a) Saliva + starch solution + dil HCI
1/50) = 0.02
(acidic) + NaCl solution
10°C 40 secs (1/40) =
0.025
b) Saliva + starch solution + H2O
20°C 30 secs (1/30) = (neutral) + NaCl solution
0.03 c) Saliva + starch solution + dil NaOH
30°C 20 secs (1/20) = (basic) + NaCl Solution
0.05 where:
40°C (close to opt. 10 secs Saliva (Source in Amylase)
temperature, but (maximum Starch Solution (Substrate)
deactivation/slow activity) (1/10) = Dil. HCl, H2O, and Dil. NaOH (to
down of activity of 0.10 manipulate pH)
enzyme occurs) NaCl Solution (activator (cofactor))
50°C (deactivation 15 secs (1/15) = Type of graph: Parabola
occurs) 0.06 Note:
60°C 0
- When people got sick, enzyme
(Denaturation/loss of
activity)
deactivated and when it got higher,
Interpretation: As temperature increases, enzyme denatures, until you got vomit.
the activity of enzyme increases until it - Milk is not advisable to drink when
reaches the opt temp. Beyond the opt temp. you have ulcer because people have too
the activity shows down until it lost its much acid when they have ulcer.
activity
Type of Graph: Parabola VITAMINS (LEC)
Procedure 3. Vitamins
Effect of Enzyme Concentration on Definition
Catalase Activity - organic substances, essential in
(controlled variable: temperature, amount the diet in small amounts that are
of substrate
involved in fundamental functions
manipulated variable: amount of catalase)
of the body.

7|O N G R AY N E
 MC 2
- act as a coenzyme
Classification
- lipid-soluble vitamin
Common features
﹡Nonpolar (hydrophobic)
﹡Poorly soluble in water but soluble
in fat and fat solvents
. can be extracted from the source by
using solvent extraction using fat as the
solvent.
. Can be stored in the body so a
regular supply is not needed
. Can accumulate to toxic levels if
large amount is ingested.
. Fairly stable at normal cooking
temperature
Classification
- water-soluble vitamin
Common features:
﹡water soluble, polar (hydrophilic)
. Extracted from the source using water
as solvent
. Cannot be stored in the body so
regular supply is needed
. Excess amount is excreted in urine
. Unstable to heat and light (medicine
that it’s water-soluble is in foil)
Classifications:
Vit B complexes, Vit C, folic acid
Lipid-Soluble Vitamins
Vitamin A (Retinol)
natural form of vitamins (form of
vitamins contained in fruits and
vegetables and other foods, not going
inside the body):
A1（retinol）
A2（3-dehydro-retinol ）
﹡active form (bioavailable and ready
for absorption):
retinol、retinal、retinoic acid
﹡pro-vitamin A (precursor of
vitamins, substance that can be
converted into vitamins): β-carotene
(seen in yellow fruits and vegetables;
Vit A1 and A2)
﹡storage : liver
How is β-carotene converted to
Vitamin A?
Biochemical function
＊Photographic substances in visual
cell
＊participating in the synthesis of
glycoprotein and maintaining
differentiation of epithelial cells
(Vit A is good for eyes and healthy
skin)
Deficiency
night blindness, dry eyes dry skin
Vitamin D (Calciferol)
types：VitD2（Ergocalciferol）
VitD3（Cholecalciferol ）
﹡pro-VitD2：Ergosterol
Pro-VitD3： 7-hydro-cholesterol
Ergosterol→VitD2
cholesterol→7-hydro
cholesterol→VitD3
What makes the early morning
sunlight help in activating Vit D?
8|O N G R AY N E
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Vitamin K
Natural form：K1、K2(2-methyl-1-4-
naphthoquinone)
Artificial synthesis ：K3、K4
biochemical function
Maintaining the normal levels of
Ergosterol VitD2 coagulation factor (responsible for
(UV light) blood clotting when there is bleeding)
Biochemical function deficiency : hemorrhagic disease
• Targeting on intestinal (continuous bleeding)
mucous,kidney and renal
tubular， Water-Soluble Vitamins
• Promoting absorbance of Vitamin B1 (thiamine )
calcium and phosphorous ﹡vitamin B1: thiamine
• Being beneficial to formation ﹡active form :Thiamine
and calcification of new bone pyrophosphate (TPP) (they have
Deficiency Brittleness and hydroxyl group so water soluble)
children—— rickets deformation of Biochemical function
adults——osteomalaciabones ﹡ With effects in the nerve
conduction，inhibiting the
Vitamin E (Tocopherol） cholinesterase (an enzyme that
types：Tocopherol , Tocotrienols catalyzes hydrolysis of acetylcholine)
﹡easy to be oxidized; protector of activity.
other substances Acetylcholine – substances that is
Free radicals – substances in our body responsible for nerve
which when oxidized will cause illness impulses/transmission of nerve
like cancer, premature aging. impulses
biochemical function (If acetylcholine catalyzes, we can feel
anti-oxidation numbness because cholinesterase
Vitamin E: antioxidant hydrolyses it resulting of not enough
ROO·  RH  ROOH  acetylcholine)
R· Vitamin B1: inhibitor of cholinesterase
（Peroxide free radical) deficiency
(polyunsaturated fatty acids) beriberi (damage or inflammation of
(organic peroxide) (organic free the nerve resulting to muscle weakness,
radical） difficulty in maintaining balance,
R·  O2  ROO· difficulty in walking resulting to heart
ROO·+Vit E-OHROOHVit E-O· failure)
Maintaining reproduction peripheral Neuritis (damage of
Promoting metabolism of Hb peripheral nerves resulting to muscle
(Hemoglobin) weakness, muscle cramps, tingling
Deficiency: sterility sensation and pain)

9|O N G R AY N E
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Vitamin B2 (riboflavin)
﹡vitamin B2: riboflavin
﹡ active form : flavin
mononucleotide (FMN)
flavin adenine
dinucleotide (FAD):
biochemical function ：
FMN and FAD are the prosthetic
group of
oxidoreductases with function of
transmitting hydrogen
deficiency：
cheilosis – sore and cracking of the lips
glossitis – inflammation of tongue
scrotitis – inflammation of scrotum
Vitamin B3 (nicotin acid, nicotinamide)
vitamin B3:
niacin
nicotinic acid
nicotinamide
Active form:
Nicotinamide adenine dinucleotide
(NAD+)
Nicotinamide adenine dinucleotide
phosphate (NADP+)
biochemical function
﹡NAD+ and NADP+: coenzyme of
dehydrogenases（Malate
dehydrogenase, lactate
dehydrogenase), transfer of hydrogen
deficiency
pellagra – skin inflammation (affect
digestive system resulting to diarrhea)
Vitamin B6 (pyridine derivatives)
vitamin B6: pyridoxine
pyridoxal
pyridoxamine
active form : Pyridoxal-Phosphate
pyridoxamine-Phosphate
biochemical function
Pyridoxal-Phosphate
Coenzyme of amino acid
aminotransferase, decarboxyIase,
and - amino-- levulinate synthase
（ALA synthase）
Deficiency:
peripheral neuropathy
Vitamin B5 (pantothenic acid)
﹡pantothenic acid
﹡active form : CoA
4-phosphopantetheinyl : acyl
carrier protein (ACP)
biochemical function
﹡CoA and 4-phosphopantetheinyl are
coenzyme of acyl transferase
，transfer of acyl
Deficiency: fatigue, insomnia, nausea,
diarrhea
Vitamin B7 (Biotin)
Biotin: co-enzyme of
carboxylase（pyruvate
carboxylase）
Deficiency: Dermatitis (eczema),
enteritis (inflammation of small
intestine)
Vitamin B9 (Folic Acid)
﹡folic acid: Pteroylglutamic acid
﹡active form: tetrahydrofolate (FH4)
(THF)
biochemical function ：
FH4 : co-enzyme of transferase of
one carbon unit
deficiency : Megaloblastic anemia
(type of anemia that enlarge red blood
cells or RBCs)
clinical application: Antitumor drug
Fact about Folic Acid: It is not a
vitamin, but its function is like a
vitamin
Vitamin B12 (cobalamine)
vitamin B12: coholamine
active form: coholamine
10 | O N G R A Y N E
 MC 2
5- Dichloromethane H2O
deoxyadenosylcobalamin CH2Cl2 (fat (polar
Biochemical function ：methyl solvent) solvent)
transfer 1. Soluble Insoluble
Deficiency：Megaloblastic anemia , Vit
nerve disease , High blood level of A
homocysteine 2. Insoluble soluble
Vitamin C (ascorbic acid) Vit
C6H8O6 (Molecular Formula) – B
shows the number and kind of atoms. 3. Insoluble Soluble
Ascorbic Acid (analyte) + I2 (titrant) Vit
Structural formula – shows the C
arrangement or bonding of atoms. 4. Soluble Insoluble
biochemical function：redox Vit
reaction, anti-oxidant, D
hydroxylation , synthesis of collagen 5. Soluble Insoluble
protein ， Vit
deficiency：scurvy – swelling and E
bleeding of gums 6. Insoluble Soluble
α-Lipoic acid Folic
- Anti-oxidant even if it’s not a Acid
vitamin, can be coenzymes. (B9)
Biochemical function
cooperating with TPP to participate CH2Cl2 – non-polar organic solvent
oxidative decarboxylation of pyruvic that can dissolve non-polar solutes.
acid 、α–keto acid; coenzyme of lipoic Vitamin B, C, and folic acid are
acid acetyl transferase for transfer of soluble in H2O because of the
acetyl group. presence of hydrophilic group
Deficiencies: neurometabolic disease (hydroxyl groups (-OH)) that form
such as seizures hydrogen bonds with H2O
Vitamin A,D,E are soluble in
dichloromethane because of their
VITAMINS (LAB) hydrophobic group. (long hydrocarbon
Properties of Vitamins: chain)
1) Solubility – physical property Procedure 2.
2) Chemical Property of Vit. C – Standardization of iodine by
Readily be oxidized Titration with Vitamin C
Objectives: Titration – quantitative method of
1) Determine the solubility of determining the concentration of an
several vitamin samples unknown analyte by adding a specific
2) Analyze the Vit. C content of volume of a titrant with a known
heated and unheated fruit juice concentration.
Solubility of Vitamins

11 | O N G R A Y N E
 MC 2
Quantitative – amount in mass and Function
volume. 1) Vit B1 Inhibitor of enzyme
Analyte – substance/solution whose 2) Vit B2 Prosthetic group of
concentration is unknown. Substance oxidoreductases
whose concentration is to be 3) Vit B3 Coenzyme of
determined. Vitamin C is the analyte dehydrogenase
(Erlenmeyer flask) 4) Vit B5 Coenzyme of
Titrant – solution with a known transferase
concentration known as standard 5) Vit B6 Coenzyme of
solution. Iodine solution is the titrant transferase
(Biuret) Coenzyme of
Standardization – a process by which decarboxylase
the concentration of a certain solution Coenzyme of
is being established in order for it to synthase
have an accurate and precise one. 6) Vit B7 Coenzyme of
Starch solution – indicator carboxylase
Indicator – detect the endpoint of 7) Vit B9 Coenzyme of
titration transferase
Endpoint – point in titration which is 8) Vit B12 Coenzyme of
shown by the change in color of the transferase
indicator. It indicates that the reaction
is already complete (can observe/ blue Enzyme being Reaction catalyzed
or gray color) helped by by the enzyme
Reaction: coenzyme
Cholinesterase Hydrolysis of
acetylcholine
NADH Removal of
dehydrogenase hydrogen from
Equivalence point – point at which the NADH
vit. C and iodine will react completely Malate Removal of
(titrant, analyte. We don’t see this. The Dehydrogenase hydrogen from
endpoint will see). Lactate malate or from
Effect of Heat on Vit C. content of Dehydrogenase lactate
Calamansi Juice Acyl transferase Transfer of acyl
It destroyed because heat causes the group
oxidation of some vit. C and breaking - AA amino - Transfer of amino
down of vit. C into smaller molecules. transferase group from Amino
Conclusion: Concentration of Vitamin - AA Acid
C in the heated and unheated calamansi decarboxylase - Removal of
juice were determined by titration with - ALA Synthase COOH of Amino
iodine solution. Acid
Vit. B Complex Biochemical - Synthesis of

12 | O N G R A Y N E
 MC 2
alpha-amino
levulenic acid
Pyruvate Addition of
carboxylase carboxyl group to
pyruvate
Methyl Transfer of one
transferase carbon unit
Methyl Transfer of methyl
transferase group
CARBOHYDRATES (LEC)
Carbohydrates
- are the most abundant class of
organic compounds found in
living organisms.
- They originate as products of
photosynthesis, an endothermic
reductive condensation of
carbon dioxide requiring light
energy and the pigment
chlorophyll.
n H2O + Energy  CnH2nOn
+ n O2
- The formulas of many
carbohydrates can be written as
carbon hydrates, Cn(H2O)n,
hence their name.
- The carbohydrates are a major
source of metabolic energy,
both for plants and for animals
that depend on plants for food.
- Aside from the sugars and
starches that meet this vital
nutritional role, carbohydrates
also serve as a structural
material (cellulose), a
component of the energy
transport compound ATP,
recognition sites on cell
surfaces, and one of three
essential components of DNA
and RNA.
- Carbohydrates are called
saccharides or, if they are
relatively small, sugars.
Functions:
1) major source of metabolic energy
(ATP)
2) Has nutritional role
3) serve as structural material, ex.
Cellulose, chitin, peptidoglycan
4) component of ATP
5) recognition sites on cell surfaces
(Glycoprotein)
6) Component of DNA and RNA
A- Simple Sugars
• Contain the elements carbon,
hydrogen, and oxygen.
• The name carbohydrate literally
means water compounds of
carbon.
• The general formula for simple
sugars is Cn(H2O)n.
• This class of compounds is
better described as Polyhydroxy
aldehydes and ketones.
• The simplest carbohydrates are
glyceraldehyde and
dihydroxyacetone.
Aldehydes – a class of organic
compounds containing an aldehyde
group (can be seen in C-1 and the
structure is CHO)
13 | O N G R A Y N E
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Examples: formaldehyde – formalin
(when dissecting, HCHO)
Acetaldehyde – cinnamon
(CH3CHO)
Ketones – organic compounds
containing ketone group. (can be seen
in C-2 and structure is -CO)
Examples: Acetone (CH3COCH3)
Diethyl Ketone
(CH3CH2COCH2CH3)
Note: Carbohydrates can be classified
as aldehyde or ketone.
Example: Glucose and fructose
(C6H12O6)
A - Methods of Classification:
Several methods are used to classify
carbohydrates.
1-One method of classification is
based on whether the carbohydrate
can be broken down into smaller
units.
• Monosaccharides
cannot be broken down into smaller
units by hydrolysis. Sometimes it is
called simple sugars.
Examples: fructose, glucose,
acetaldehyde, ribose, deoxyribose,
galactose
• Disaccharides
can be broken down (hydrolyzed) into
two monosaccharide units.
Examples: Sucrose – hydrolyzed to
glucose and fructose
Maltose – hydrolyzed into 2
glucose units
Example: Raffinose – hydrolyzed will
form 1 glucose, 1 galactose, 1 fructose
• Polysaccharides
composed of 7 or more
monosaccharide units.
Examples: Starch, cellulose, and
glycogen are made up of many glucose
units.
2-Another method is based on the
number of carbons found in a simple
sugar.
• If it has 3 carbons it is called a
triose.
• If it has 4 carbons it is called a
tetrose.
• If it has 5 carbons it is called a
pentose.
• If it has 6 carbons it is called a
hexose.
3-Another method uses the kind of
carbonyl group.
A- Aldose:
A monosaccharide with an aldehyde
group.
have aldehyde grp in C-1
B- Ketose
A monosaccharide with a ketone group.
CH 2OH

Lactose - hydrolyzed to C O
HO C H
glucose and galactose H C OH
• Oligosaccharides H C OH
can be broken into three to six CH 2OH

monosaccharide units.
fructose have ketone grp in C-2

14 | O N G R A Y N E
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Usually combine the carbonyl
classification and the number
classification together.

Isomerism – a property of simple

B- Stereoconfigurations of simple sugars/monosaccharides which they
sugars. can exist in different forms. These
Carbohydrates contain many forms have same number and kinds of
stereocenters. atoms but with different arrangement of
1- If the OH group is found on the atoms.
right side of the carbon chain, the Types of isomers
sugar is designated as a D sugar. 1) Structural and Constitutional
2- If the OH group is found on the left Isomers
- have same molecular formula but
side of the chain of carbons, the sugar
different structural formula.
is designated as an L sugar.
Examples: Glucose (Aldose) and
H O H O Fructose (ketone) – both have same
C C
molecular formula. (they have diff.
H C OH HO C H
CH2OH CH2OH
structural formula because they have
diff. functional grp)
D-glyceraldehyde L-glyceraldehyde
a) Functional Isomers – have diff.
D-aldotriose L-aldotriose
functional group but same molecular
B- Stereoconfigurations of simple formula.
sugars. Examples: glucose and fructose,
CHO
H C OH glyceraldehyde and
CH 2OH

CHO
D-glyceraldehyde
CHO
dihydroxyacetone (C3H6O3)
H
H
C OH
C OH
HO C H
H C OH
b) Chain/Skeletal Isomer
CH 2OH CH 2OH CH3CH2CH2CH2CH3 (n-pentane,
D-erythrose
straight/linear chain)
D-threose
CHO CHO CHO CHO
HO C H H C OH
CH3CHCH2CH3 (Isopentane,
H C OH HO C H
H C OH H C OH HO C H HO C H
H C OH H C OH
branched)
H C OH H C OH
CH 2OH CH 2OH CH 2OH CH 2OH
D-arabinose D-ribose D-lyxose D-xylose

CHO CHO CHO CHO

CHO CHO CHO CHO

CH3 MF – C5H12
HO C H H C OH HO C H H C OH
HO C H H C OH HO C H H C OH
HO C H HO C H H C OH H C OH
HO C H HO C H H C OH H C OH

c) Position Isomers – differ in the

HO C H HO C H HO C H HO C H
H C OH H C OH H C OH H C OH
H C OH H C OH H C OH H C OH
H C OH H C OH H C OH H C OH
CH 2OH
D-mannose
CH 2OH
D-glucose
CH 2OH
D-altrose
CH 2OH

D-allose
CH 2OH

D-tallose
CH 2OH CH 2OH CH 2OH
position functional groups
D-galactose D-idose
CH3CH2CH2CH2OH (n-butyl alcohol)
D-gulose

CH3CHCH2CH3

15 | O N G R A Y N E
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Hemiacetal – if the anomeric carbon
OH (2-butyl alcohol) C-1 on the aldehyde group of aldoses.
2) Stereoisomers Hemiketal – if the anomeric carbon is
- have the same MF but with different C-2 on the ketone group of ketoses.
structural dimensions (configuration Cyclic Structures: (also known as
of C atoms). Haworth Projection Formula)
a) Enantiomers – mirror images of Five membered sugar rings are
each other (also known as optical known as furanose rings.
isomers) H
C
O
HO CH2 HO CH2
Penultimate C – 2nd to the last carbon H C OH O H O OH

H C OH H H + H H
Examples: D-glucose and L-glucose H C OH H OH H H

D sugars – if the hydroxyl grp of 2nd CH2OH OH OH OH OH

to the last C atom is oriented to the D-ribose -D-ribofuranose -D-ribofuranose

right side of that C. • Six membered sugar rings are

L-sugars – if the hydroxyl grp of 2nd known as pyranose rings.
H O
to the last C atom is oriented to the C
HO CH 2 HO CH 2
H C OH
left side of that C. HO C H
H OH
OH H +
H O OH
OH H
Stereocenters – an atom with three or H C OH
HO OH HO H
H C OH
more attachments in which the CH 2OH
H OH H OH

-D-glucopyranose
interchanging of two of these D-glucose -D-glucopyranose

attachment lead to another Carbohydrate Anomers:

stereoisomer.
Chiral carbon – carbon atom with 4
different groups.
2n(number of chiral carbon)- formula used to
determine the number of isomers for
each sample sugar
Example: glucose can form 16
isomers
erythrose have 4 isomers
xylulose have 4 isomers
b) Diastereomers – not-mirror image
of a simple sugar.
Examples: D-glucose and D-altrose
D-arabinose and D-ribose
D-xylulose and D-ribulose
c) Epimers – diff in configuration of
only one carbon atom.
Example: D mannose is the C-2
epimer of D-glucose
d) Anomers – diff in configuration of
C-1 in a cyclic structure.
• Formation of either of the cyclic
forms has created a new
stereocenter.
• These stereoisomeric ring forms
of carbohydrates are called
Anomers.
• Anomers:
are carbohydrates that differ by the
stereo-configuration of the carbon
involved in ring formation.
• The greek letters α and β are
used to describe the
configuration about the ring
forming carbon.
• The α anomer always has the
OH group oriented in a
downward fashion on the
anomeric carbon of a D-sugar.
• The β anomer always has the
OH group oriented in an
upward fashion on the
anomeric carbon of a D-sugar.

16 | O N G R A Y N E
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Important Carbohydrates • Composed of two D-glucose
* Monosaccharides sugars joined by an α-1,4
composed of three to seven carbon linkage.
atoms. CH 2OH CH 2OH
1- Glucose H O H H O OH
H H
• The most abundant hexose in OH H OH H
our diet. OH O H
• The building block of complex H OH H OH
carbohydrates. 2. Lactose - milk sugar.
• Component of the • Found in milk and milk
disaccharides: sucrose, maltose products.
and lactose. • Composed of one galactose
• Found in the polysaccharides: and one glucose unit joined by
starch, cellulose and glycogen. a β-1,4 linkage.
CHO
H C OH
CH 2OH CH2OH CH2OH
H O
HO C H H
H,OH
OH O H O OH
OH H
H C OH H H
H C OH OH O
H OH OH H OH H
CH 2OH
H H
2. Galactose H OH H OH
• Found in the disaccharide,
lactose. 3. Sucrose - table sugar.
• Found in the cellular • Product of sugar cane and
membranes of the brain and sugar beets.
nervous system. • Composed of one glucose and
• Galactose is the C-4 epimer of one fructose unit.
glucose. • Linkage is at both anomeric
CHO
carbons.
CH 2OH
H C OH CH2OH
HO O
HO C H H H O H CH2OH H
OH H H,OH O
HO C H H
H OH H H OH
H C OH
H OH O
CH 2OH OH CH2OH
H OH OH H
3. Fructose
• Sweetest of the carbohydrates. * Polysaccharides
• Component of the disaccharide composed of many (more than 10)
sucrose. monosaccharide
• Fructose is a keto sugar. 1- Cellulose:
• Major structural material of
* Disaccharides plant cells.
composed of 2 monosaccharide units • Consists of many glucose units
1. Maltose - malt sugar. joined by β-1,4 linkages.
• Used in cereals, candies and the 2. Starch:
brewing of beverages.

17 | O N G R A Y N E
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• Storage form of glucose found carbohydrate to undergo easy
in rice wheat, potatoes, grains oxidation.
and cereals. • If the sugar gets oxidized it
• Consists of many glucose units causes reduction.
joined by α-1,4 linkages. • Thus the name “reducing
• Maltose is the disaccharide sugar”.
starting material.
QUALITATIVE TESTS FOR
CARBOHYDRATES
Exp. 1 Molisch Test
• It is the general test for all
carbohydrates.
• Monosaccharides give a rapid
positive test. Disaccharides and
polysaccharides react slower.
• The Molisch reagent dehydrates
pentoses to form furfural.
3. Glycogen: • dehydrates hexoses to form 5-
• Animal starch. Storage form hydroxymethyl furfural.
of glucose found in the liver and • The furfurals further react with
muscle of animals. -naphthol present in the test
• Contains many highly branched reagent to produce a purple
glucose units. product.
• Joined by α-1,4 linkages and
branched by α-1,6 linkages.

4. Dextrin:
• Mixture of branched and un-
branched soluble
polysaccharides produced by
partial hydrolysis of starch by
acids or amylases.
Reducing sugars
Any sugar that contains either:
1- A free aldehyde group.
2- An α-hydroxy ketone group. ■ Method:
3- A hemiacetal linkage • 1ml test solution + 2 drops of α-
• The presence of any of these naphthol
groups allows the • mix well

18 | O N G R A Y N E
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• add conc. H2SO4 down the side
of the tube to form the ring at
the interface of the two layers.
- ve +ve
Exp. 2 Fehling's Test
• This test is used to differentiate
between reducing and non
reducing sugars.
• A reducing sugar reacts with
Fehling's reagent in alkaline
medium to form an orange to
red precipitate.
• Fehling's reagent is commonly
used for reducing sugars but is
known to be not specific for
aldehydes.
• Positive result is detected by
reduction of the deep blue
solution of cupric (II) to a red
precipitate of insoluble cuprous
oxide (Cu2O).
• Positive result is detected by
reduction of the deep blue
solution of cupric (II) to a red
precipitate of insoluble cuprous
oxide (Cu2O).
• The sucrose does not react with
Fehling's reagent. Sucrose is a
disaccharide of glucose and
fructose. Most disaccharides are
reducing sugars (e.g. lactose
and maltose)
• Sucrose is non-reducing sugar
because the anomeric carbon of
glucose is involved in the
glucose- fructose bond and
hence is not free to form the
aldehyde in solution.
Fehling's Reagent: 2solutions are
required:
*Fehling's “A"
uses 7 g CuSO4.5H2O dissolved in
distilled water
containing 2 drops of dilute sulfuric
acid.
*Fehling's "B"
uses 35g of potassium tartrate and 12g
of NaOH in 100 ml of distilled water.
■ Method:
• 1ml test solution +
1ml Fehling's reagent
• heat the mixture in BWB
(5min)
• Reddish brown ppt
19 | O N G R A Y N E
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Exp. 3 Benedict's Test
• This test is used also to
differentiate between reducing
and non reducing sugars.
• It works on the same principle
but Benedict is more stable than
Fehling's reagent.
• Benedict's reagent contains blue
copper(II) sulfate (CuSO4) ·
5H2O which is reduced to red
copper(I) oxide by aldehydes,
thus oxidizing the aldehydes to
carboxylic acids.
• The copper oxide is insoluble in
water and so precipitates. The
colour of the final solution
ranges from green to brick red
depending on how many of the
copper (II) ions are present.
■ Method:
• 1ml test solution +
1ml Benedict's reagent
• heat the mixture in BWB
(5min)
• Reddish brown ppt
Exp. 4 Barfoed’s Test
• It is a test used to differentiate
between monosaccharides and
disaccharides. This reaction will
detect reducing
monosaccharides in the
presence of disaccharides. This
reagent uses copper ions to
detect reducing sugars in an
acidic solution. Barfoed's
reagent is copper acetate in
dilute acetic acid (pH 4.6)
• Reducing monosaccharides are
oxidized by the copper ions in a
weak acidic medium to form a
carboxylic acid and a reddish
ppt of Cu2O (cuprous oxide).
• Reducing disaccharides (lactose
but not sucrose) undergo the
same reaction but at slower rate.
■ Method:
• 1 ml of the solution to be tested
+ 2 ml of freshly prepared
Barfoed's reagent.
• Place test tubes into a boiling
water bath and heat for 2
minutes.
• Remove the tubes from the bath
and allow to cool.
• Formation of a green, red, or
yellow precipitate is a positive
test for reducing
monosaccharides.
• Do not heat the tubes longer
than 3 minutes, as a positive test
can be obtained with
disaccharides if they are heated
long enough.
Exp. 5 Seliwanoff Test
• The test reagent dehydrates
ketohexoses to form 5-
hydroxymethylfurfural.
• 5-hydroxymethylfurfural
further reacts with resorcinol
present in the test reagent to
20 | O N G R A Y N E
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produce a red product within
two minutes.
• Aldohexoses react to form the
same product, but do so more
slowly.
■ Method:
• 1/2 ml of a sample + 2ml of
Seliwanoff's reagent (a solution
of resorcinol and HCl) is added.
• The solution is then heated in a
boiling water bath for two
minutes.
• A positive test is indicated by
the formation of a red
product.
• In case of sucrose, avoid over-
boiling because sucrose may be
hydrolyzed to its component
(glucose and fructose) and gives
false positive result.
-ve +ve
Exp. 6 Hydrolysis Test
• Sucrose is the only non-
reducing sugar so it does not
reduce the alkaline Cu solutions
(Fehling and Benedict). Sucrose
must first be hydrolyzed to its
component and then test for.
■ Method:
• 6 ml of 1% sucrose in a test
tube + 2 drops of concentrated
hydrochloric acid (HCl).
• Heat the tube in a boiling water
bath for 15 minutes.
• Then test for Fehling, Benedict
and all the previous tests.
Exp. 7 Iodine Test
(Test for Polysaccharides)
1- Starch:
• 1/2 mL of the fresh starch
solution + 1 drop of the iodine
solution.
• A dark blue color indicates a
positive test for starch.
• If the yellow color of the iodine
reagent simply becomes diluted,
no starch is present.
• Record the observation as
positive (blue) or negative
(yellow).
2- Dextrin:
• 1/2 mL of the fresh dextrin
solution + 1 drop of the iodine
solution.
• A violet color indicates a
positive test for dextrin.
• If the yellow color of the iodine
reagent simply becomes diluted,
no dextrin is present.
• Record the observation as
positive (violet) or negative
(yellow).
CARBOHYDRATES (LAB)
IDENTIFICATION TESTS FOR
CARBOHYDRATES
Sample Carbohydrates
21 | O N G R A Y N E
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Glucose Monosaccharide/ react with the furfural to form the red
Hexose/Aldose/ colored solution.
Aldohexose Procedure 3: Bial’s Test
Lactose Disaccharide - specific test for pentoses
Positive result: blue-green color,
- consists of
No sample gave + result.
galactose and Bial’s reagent: orcinol + conc HCl
glucose Principle: Pentoses are dehydrated by
Starch Polysaccharide conc. HCl to form furfural. Orcinol will
- consists of react with furfural to form the blue green
many glucose solution.
units Note: These 3 have furfural formation
Fructose Monosaccharide/ Reducing Test for sugars:
Hexose/Ketone/  Benedict’s
Ketohexose  Barfoed’s
 Tollen’s
Sucrose Disaccharide Reducing sugar – have free aldehyde and
- glucose and ketone group or those with hemiacetal
fructose linkage.
Galactose Monosaccharide/ Note:
Hexose/Aldose/ All monosaccharides are reducing agent.
Aldohexose All polysaccharides such as starch are
non-reducing.
Procedure 1: Molisch’s Test Sucrose, a disaccharide is non-reducing.
- general test for carbohydrates Procedure 4: Benedict’s Test
- specific for reducing sugars
Positive result: Violet ring in between
Positive result: Brick-red ppt
two layers Sample w/ positive reagent: glucose,
All samples have positive results. lactose, fructose, galactose
Molisch reagent: alpha-napthol Benedict’s reagent: CuSO4(Cupric sulfate
(aromatic alcohol) + conc. H2SO4 pentadehyde) * 5 H2O + Na carbonate +
Principle: Carbohydrates are Na citrate
dehydrated by conc H2SO4 to form Principle: Benedict’s reagent is an
FURFURAL. The alpha-napthol will react oxidizing agent.
with furfural forming violet ring.
Procedure 2: Seliwanoff’s Test Reducing sugar + CuSO4 (oxidizing agent)
- distinguishing that between aldoses + Carboxylic Acid + Cu2O (brick
ketoses red)
only ketoses gave (+) result.
Positive result: red colored solution Reaction: REDOX
Samples: fructose, sucrose when heated Reducing sugar and Carboxylic Acid:
further so that it hydrolyzed to fructose and oxidation
glucose. CuSO4 and Cu2O: reduction
Seliwanoff’s reagent: resorcinol + conc.
HCl Procedure 5: Barfoed’s Test
Principle: Ketoses are dehydrated by conc. - test that distinguishes reducing
HCl to form furfural. Then, resorcinol will monosaccharide from red disaccharide.

22 | O N G R A Y N E
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Reducing monosaccharide – readily gives • Named from the Greek word lipos,
positive result which means “fat.”
Reducing disaccharide – slowly gives • Fatty acids are building blocks,
positive result. monomers of polymeric lipids and
Positive result – brick red ppt non-polymeric lipids.
Glucose, galactose, fructose give positive • There are lipids that do not contain
result readily fatty acids.
Lactose gives positive result slowly. Physical property
Barfoed reagent – oxidizing agent  All lipids are insoluble in water but
consisting of cupric acetate and acetic acid. soluble in organic solvents (non-
polar solvents) like ether, benzene,
Reducing monosaccharide + (CH3COO)2 dichloromethane, etc.
Cu Carboxylic acid + cuprous acid  Non-polar
(Cu2O) (brick red) Functions
• For long-term energy storage
Reducing monosaccharide and Carboxylic (reserved energy)
acid: oxidation • For protection (ex. Visceral fats –
(CH3COO)2 Cu and cuprous acid (Cu2O): envelops and protect internal
reduction organs. Waxes and cutin/cuticle –
found in the leaves to protect the
Procedure 6: Tollen’s Test plants from too much loss of H2O)
- test that distinguishes reducing aldoses • Insulation (ex. Adipose fats-
from reducing ketoses. found beneath skin that regulates
Reducing aldoses only give a positive body temperature)
result. • Lubrication (ex. Synovial fluid in
Positive result: Silver mirror ppt our joints are made up of lipids)
Tollen’s reagent: oxidizing agent • Precursors for some hormones
consisting of ammoniacal silver nitrate (Steroidal hormones such as sex
solution. hormones)
• Key component of cell
Reducing Aldoses + AgNO3 redox membrane (ex. Phospholipid)
carboxylic acid + Ag (silver) Types of Lipids
Lipids with fatty acids
Reducing Aldoses and carboxylic acid:  Prostaglandins
oxidation  Waxes
AgNO3 and Ag (silver): reduction  Fats and oils(triglycerides)
 Phospholipids
Procedure 7: Iodine Test
 Sphingolipids
- test for starch.
 Glycosphingolipids
LIPIDS (LEC)  Cooking oil
 Butter
Lipids are  Margarine
• Biomolecules that contain fatty Lipids without fatty acids
acids  Steroids
• Soluble in organic solvents but not  Sex hormones
in water. Structures of Lipids

23 | O N G R A Y N E
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 For example caprylic acid with 8
carbon atoms.
CH3—(CH2)6—COOH
CH3—CH2—CH2—CH2—CH2—CH2—
CH2—COOH
Saturated and Unsaturated Fatty Acids
Saturated fatty acids – contains all carbon
atoms are singly bonded (can get heart
disease)
Ex. Pork fat consist of stearic acid (solid)
Palmitic acid contained in coconut oil
- C–C bonds
 Molecules that fit closely together
in a regular pattern.
Fatty Acids  Strong attractions between fatty
 Long-chain carboxylic acids acid chains.
(RCOOH)  High melting points that make
 Insoluble in water them solids at room temperature
 Typically 12-18 carbon atoms
(even number)
 Some contain double bonds
Carboxylic Acid – group of organic
compounds containing the carboxyl group
which written as -COOH (functional grp)
General Formula of carboxylic acid:
R-COOH
R – hydrocarbon chain
COOH – functional group
Examples of -COOH
Acetic acid - CH3COOH
Butyric acid – CH3CH2CH2COOH
Example of fatty acid
CH3(CH2)12COOH (Condensed Structural
Formula) (myristic acid have 14 carbon
atoms)
Note: Unsaturated fatty acids – One or more
 if less carbon, it’s carboxylic acid, carbon-carbon double bond (C=C)
if more carbon, it is called fatty - most beneficial to our health because it
acid. has more vegetable oil.
 COOH will always be the Carbon Monounsaturated – one double bond
1 Polyunsaturated – two or more carbon-
Fatty Acid Formulas carbon double bond.
 The formulas for fatty acids are • Nonlinear chains do not allow
written as molecules to pack closely
 Condensed formulas. • Few interactions between chains
 Line-bond formulas. • Low melting points

24 | O N G R A Y N E
 MC 2
• Liquids at room temperature
• Have “kinks” in the fatty acid
chains.
Note: Palmitoleic acid can get more oil in
coconut oil than palmitic.
For saturated, the longer the hydrocarbon
chain (greater number of C atoms) the
higher is the melting point because more
bonds must be broken before it finally
melts
Omega 3 and 6 – good for health
Notation:
Oleic acid – 18:1( 9), Monounsaturated
Linoleic Acid – 18:2( 9,12),
Polyunsaturated, Omega 6
Linolenic acid – 18:3 ( 9,12,15),
Polyunsaturated, Omega 3
Arachidonic acid – 20:4 ( 5,8,11,14),
Polyunsaturated, Omega 6
Saturated:
Palmitic Acid – 16:0
Capric Acid – 10:0
Palmitic – 16 carbons all singly bonded
(saturated) (62 degrees)
Palmitoleic – 16 carbons, 1 double bond in
C-9 (monounsaturated) (0 degrees)
Saturated Fatty Acid
- Closely packed together, more attraction,
higher melting point than unsaturated fatty
acid with same number of C-atom because
their molecules are closely packed
together. Making their intermolecular force
of attraction stronger.
Unsaturated Fatty Acid
- molecules are loosely packed together
making the force of attraction weaker. This
is due to kinks (bent) in the double bond.
The greater the number of double bonds,
the lower the mpt.
- the more the kinks, the more will loosely
packed. Ex. Linoleic Acid
- exhibit as -trans isomerism.
Geometric isomers – cis and trans
configuration.
Cis-Oleic
Trans-Oleic
Classification of Lipids
I. Lipids with fatty acids
a) Triglyceride – also known as
triacylglycerol or fats and oils.
- consists of 1 glycerol
(polar) molecule and 3 fatty acids (non-
polar).
Ex. Cooking oil, coconut oil, butter, lard,
margarine and animal fats.
25 | O N G R A Y N E
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Esterification – a reaction between an
alcohol and a carboxylic acid forming an
ester and H2O.
Ester bond – bond links glycerol to fatty
acid.
Simple Triglyceride – composed of
glycerol and 3 similar fatty acids.
Ex. Trimyristin and glyceryltrimyristate.
Mixed Triglyceride – composed of
glycerol and different fatty acid.
Reactions of Triglyceride
1) Hydrogenation (1 bond) – It is
unsaturated fatty acid that will turn into
fatty acid.
- addition of hydrogen
gas to the unsaturated fatty acid of a
triglyceride where the double bond of the
unsaturated fatty acid is connected to
single bond. It creates in the presence of
nickel or Platinum catalyst. For every
double bond, 1 hydrogen molecule must
react.
2) Hydrolysis (double bond) – splitting of
ester bond by adding water.
- produce
glycerol and 3 fatty acids. For every ester
bond to be splitted, 1 H2O molecule must
be added
Triglyceride + H20 glycerol + 3FA
3) Saponification (double bond) – soap
making process.
- splitting
of ester bond in triglyceride by adding
strong base like NaOH/KOH. It is called
ALKALI HYDROLYSIS.
The products in saponification are glycerol
and 3 salts of fatty acids (SOAP)
b) Glycerophospholipids/
Phosphoglyceride/ Phospholipids
 The most abundant lipids in cell
membranes.
 Composed of glycerol, two fatty
acids, phosphate and an amino
alcohol.
Amino Alcohol – contains amino group.
Example: lecithin – found in egg yolk,
wheat germ, and yeast
Cephalin – found in brain and
nerve tissue
Lecithin – example of phospholipid
containing 2 palmitic acid, 1 glycerol,
phosphate and choline (amino alcohol)
(they are the composition).
PO4 group, amino alcohol + glycerol –
polar end of lecithin
Fatty acid (palmitic acid) – non polar
end.
Lecithin has ester bonds that connect the
fatty acid to glycerol.
Amide linkages – bond that connects the
amino alcohol to the PO4 group.
Note: The difference between lecithin and
cephalin is the amino alcohol content.
Amino Alcohol Content of phospholipid:
1) Choline – contained in lecithin
2) Ethanolamine and Serine – both
contained in cephalin.
Note: Phosphate group became acidic
because of phosphoric acid.
All phospholipid have ester bond.
c) Sphingolipids/Phosphosphingolipid
- only 1 fatty acid.
- Are similar to phospholipids.
- Contain sphingosine (a long-chain amino
alcohol), a fatty acid, phosphate, and a
small amino alcohol.
- Have polar and nonpolar regions.
Types of Sphingolipids
26 | O N G R A Y N E
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 Ceramide – found in skin - contains 20 C atoms and a five membered
Function: oily consistency in skin ring
 Sphingomyelin – found in myelin - enhance our immune system,
sheath inflammatory response
 Glycosphingolipid – contains
sugar instead of PO4 and amino
alcohol.

Sphingosine is a long-chain unsaturated

amino alcohol.
Steroids: Cholesterol, Bile Salts, and
Steroid Hormones

Steroid Nucleus
A steroid nucleus consists of:
 3 cyclohexane rings.
 1 cyclopentane ring.
 No fatty acids.

Types:
Cholesterol
• Is the most abundant steroid in
the body.
• Has methyl CH3- groups, alkyl
chain, and -OH attached to the
steroid nucleus.
• Have OH (gives polar), have
methyl grp (gives non-polar/long
hydrocarbon chain)
Bile salts/acid
Steroid hormones
Note: All lipids without fatty acids have
steroid nucleus
Triglyceride – most abundant lipid in our
body
Phospholipid – most abundant cell
membrane.

d) Waxes
Fatty Acid long-chain alcohol

e) Prostaglandin
- derivative of arachidonic acid

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