ENZYMES AND CARBOHYDRATES

BIOCHEMISTRY LECTURE | CHEM 119

COFACTOR All non protein parts of a

OUTLINE conjugated enzyme
I. Enzymes
A. Classes of Enzyme HOLOENZYME Biochemically active part of the
B. Nomenclature of Enzymes conjugated enzyme
C. 6 Major Classes of Enzymes
D. Modes of Enzyme Action
COFACTORS
E. Enzyme Properties
F. Reaction Velocity - Can be divided in 2 parts
G. Energy Changes During Reaction SMALL ORGANIC INORGANIC ION
H. Michaelis-Menten Equation MOLECULES
I. Enzyme Inhibition
II. Carbohydrates Derived from dietary Derived from dietary
A. Classification of Carbohydrates vitamins minerals
1. Monosaccharides
2. Disaccharides Called co-enzymes or Nonmetallic ion cofactor:
3. Polysaccharides co-substrates Cl-
B. Carbohydrate Projection
C. Stereoisomers
D. Cyclic Formation of Carbohydrates SUBSTRATE
E. Monosaccharide Reactions - Reactant in an enzyme-catalyzed reaction
F. Biologically Important - Substance upon which the enzyme acts on
Polysaccharides ➢ Converted into product
G. Dietary Considerations
NOMENCLATURE OF ENZYMES
❖ SUFFIX -ASE
ENZYMES - Identifies as enzyme
- It is not another biomolecule but a protein EXAMPLES:
- Catalyst for biochemical reactions ➢ Urease
➢ True catalyst which makes the reaction ➢ Sucrase
faster ➢ Lipase
➢ Remains unchanged ❖ SUFFIX -IN
- Undergo all the reactions of proteins - Found in the names of digestive
➢ Includes denaturation enzymes
- There are thousands of enzymes in the human EXAMPLES:
body ➢ Trypsin
➢ Each reaction is accompanied with an ➢ Chymotrypsin
enzyme ➢ Pepsin
CLASSES OF ENZYME ❖ TYPE OF REACTION
❖ SIMPLE ENZYME ➢ OXIDASE: catalyzes oxidation reaction
- Protein only (amino acid chains) ➢ HYDROLASE: catalyzes hydrolysis
❖ CONJUGATED ENZYME reaction
- Nonprotein part + protein part ❖ IDENTITY OF SUBSTRATE
- The first name of an enzyme is the
substrate
EXAMPLE
➢ Glucose oxidase
➢ Pyruvate carboxylase
➢ Succinate dehydrogenase
❖ GENERAL NATURE OF SUBSTRATE
- From the name of substrate
APOENZYME Protein part of the conjugated EXAMPLE
enzyme ➢ Lipase
➢ Protease

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 SYSTEMATIC NOMENCLATURE OF ENZYMES
Oxidases Oxidation of substrate
- Developed by International Union of ➢ ↓ H atoms, ↑ O atoms
Biochemistry and Molecular Biology (IUBMB)
- Enzymes are subdivided into 6 molecular Reductases Reduction of substrate
classes ➢ ↓ O atoms, ↑ H atoms
- Gets more specific per number
EXAMPLE: Dehydrogenases Removal of 2 H atoms from
substrate introduces a
EC 2.7.3.2 double bond to the product,
SYMBOL MEANING H atoms being accepted by
coenzyme
EC Enzyme Comission

2 Molecular subdivision; 2
means transferases

7 Subclasses of the subdivision;

7 means
phosphorus-containing
groups TRANSFERASES

3 Category of the subclass; 3 SELECTED REACTION CATALYZED

means phosphotransferases SUBCLASSES
with nitrogenous group as
acceptor Transaminases Transfer an amino group
between substrates
2 The actual name of the
enzyme; Creatine Kinase Kinase Transfer of phosphate group
between substrates
6 MAJOR CLASSES OF ENZYMES
- The first number in the systematic
nomenclature of enzymes
CLASS REACTION CATALYZED

1 Oxidoreductases Oxidation-reductions

2 Transferases Functional group transfer HYDROLASES

reactions
SELECTED REACTION CATALYZED
3 Hydrolases Hydrolysis reactions SUBCLASSES

4 Lyases Reactions involving Lipase Hydrolysis of ester linkages

addition or removal of in lipids
groups from double
bonds Proteases Hydrolysis of amide linkages
in proteins
5 Isomerases Isomeration reactions
Nucleases Hydrolysis of
6 Ligases Reactions involving bond sugar-phosphate ester
formations coupled with bonds in nucleic acids
ATP hydrolysis
Carbohydrases Hydrolysis of glycosidic
bonds in carbohydrates
OXIDOREDUCTASES
Phosphatases Hydrolysis of
SELECTED REACTION CATALYZED phosphate-ester bonds
SUBCLASSES

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 Synthetases Formation of new bond
between 2 substrates with
participation of ATP

Carboxylases Formation of new bond

between substrate and CO2
with participation of ATP
LYASES

SELECTED REACTION CATALYZED

SUBCLASSES

Dehydratases Removal of H2O from

substrate
ACTIVE SITE
Decarboxylases Removal of CO2 from -
Place where the substrate binds to the
substrate enzyme
Deaminases Removal of NH3 from - Some enzymes have more than 1
substrate active site
❖ ENZYME SUSBTRATE COMPLEX
Hydratases Addition of H2O to substrate - Intermediate reaction species formed
when substrate binds with the active
site

❖ FISCHER MECHANISM
ISOMERASES
- Known as the Lock and Key Model
SELECTED REACTION CATALYZED - Substrate is fixed in shape to the active
SUBCLASSES site before binding

Racemases Conversion of D to L isomer MODELS OF ENZYME ACTION

or vice versa
➢ Perfect match
Mutases Transfer of one functional
❖ KOSHLAND MECHANISM
group from one position to
another in the same - Known as the Induced-fit Model
molecule - The active site and substrate does not
match in shape before binding
- The active site adapts to the substrate
whilst binding
- More accepted explanation on how
enzymes bind
➢ There are enzymes who accept
more than 1 substrates
ENZYME PROPERTIES
❖ ACTIVE SITE
LIGASES
- An asymmetric pocket wherein
SELECTED REACTION CATALYZED biological reactions are catalyzed
SUBCLASSES - Contains amino acid side chains that
created 3-dimensional surface
complementary to the substrate
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❖ CATALYTIC EFFICIENCY ➢ Have a higher chance to bind
- Each enzyme molecule transforms with an active site
100-1000 substrate molecules into ❖ pH LEVEL
product each second - Most enzymes have optimal activity in
- 103-108 times faster than uncatalyzed the pH range of 7.0-7.5
reactions ➢ Neutral levels
➢ Due to the aqueous
● TURNOVER NUMBER environment of the cells
- Number of molecules an - The digestive enzymes are exempted
enzyme molecule could
ENZYME OPTIMUM pH
process per seconds when
saturated with the substrate Pepsin 2.0
- Equivalent to catalytic rate (kcat)
❖ SPECIFICITY Trypsin 8.0 (or around neutral pH)
- Enzymes are highly specific -
Once the enzyme passes the optimal
- Interacts with one or few substrates pH level, it will undergo the
- Catalyzes only one type of chemical denaturation process
reaction ➢ The side chains are protonated
❖ COFACTORS and deprotonated
- Non protein portion of an enzyme ❖ SUBSTRATE CONCENTRATION
needed for enzymic activity - The amount of substrate that the
❖ REGULATION enzyme binds
- Enzymes can be activated or inhabited - ↑ substrate concentration, ↑enzyme
so that the rate of production responds activity
to the need of the cell ➢ Higher substrate concentration,
❖ LOCATION WITHIN THE CELL faster enzyme activity
- Most of the enzymes are located and ➢ Constant enzyme concentration
- SUBSTRATE SATURATION: maximum
localized within specific organelles
rate of catalyzation when all active
within the cell sites are full
➢ Compartmentalized
REACTION VELOCITY
- Number of substrate molecules converted to
product per unit time
- Expressed as μmol of product formed per
minute
FACTORS AFFECTING REACTION VELOCITY
❖ TEMPERATURE
- Optimum temperature for human
enzymes is 37 degrees celsius
➢ Similar to the body
temperature
➢ As substrate concentration
- Increased body temperature leads to increases, all the active sites
decreased enzyme activity are fully booked
➢ Enzyme is prone to - TURNOVER NUMBER: number of
denaturation process as the substrate molecules converted under
temperature goes higher optimal conditions of temperature and
➢ Enzyme is still a protein pH
❖ ENZYME CONCENTRATION
- As temperature increases, reaction rate
- At constant enzyme concentration,
increases enzyme activity ↑ as enzyme
➢ Due to vibration of molecules, concentration ↑
enzymes have a higher chance ➢ Directly proportional
to have a collision with a ➢ The speed of reaction has no
substrate limit
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 ➢ When you increase the amount
of enzyme, the number of
active sites also increases
therefore increasing the amount
of substrates to be catalyzed
❖ COFACTORS
- Affects the proper functioning of the
enzymes
- May be part of the prosthetic group
- May act independently facilitating
enzyme reactions
❖ INHIBITORS
- “inhibit”
➢ Slows down or blocks totally
- Any substance that can diminish the
velocity of an enzyme-catalyzed
reaction
ENERGY CHANGES DURING REACTION
❖ FREE OF ENERGY ACTIVATION
- Energy difference between the
reactants and a high-energy
intermediate that occurs during the
formation of the product
➢ When reactants undergo a reaction, it
needs to cross over the middle part
(peak) before it becomes a product
➢ If the energy peak is low, then the
reactants will be converted into products
faster
➢ If the reactant peak is low and the
energy peak is significantly higher,
the reactants will not be converted into
products or there will be fewer
reactants converted
- ↓ free energy of activation, ↑ molecules
that have sufficient energy to pass
through transition state, ↑ rate of
reaction
MICHAELIS-MENTEN EQUATION
- Describes how reaction velocity varies with
substrate concentration
➢ V0 : initial velocity
➢ Vmax : highest maximum velocity
➢ S: substrate
➢ Km: Michaelis-Menten Equation
- Km= ½ Vmax
- Small Km: enzyme has high affinity for
substrate
- Large Km: enzyme has low affinity for
substrate
➢ [] : concentration in molarity
LINWEAVER-BURK PLOT
- double -reciprocal plot
- Used to calculate Km and Vmax
- Determine the mechanism of action of enzyme
inhibitors
- Inhibitor can be identified with the graph that
was used
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➢ Intercept on the y-axis: 1/Vmax
➢ Intercept on the x-axis: -1/Km
➢ X-axis: 1/[S]
➢ Y-axis:1/Vo
ENZYME INHIBITION
❖ ENZYME INHIBITOR
- Substance that slows down or stops
the normal catalytic function of an
enzyme by binding to it
➢ There is a structure that
attaches to the enzyme at
some point
❖ MODES OF INHIBITION
- Irreversible
- Reversible
➢ Competitive
➢ Noncompetitive
➢ Uncompetitive
MODES OF INHIBITION: IRREVERSIBLE
- Inactivates enzymes by forming a covalent
bond with the active site
➢ Covalent bonds share electrons
forming a very strong bond
- The structure is not similar to the enzyme’s
substrate
MODES OF INHIBITION: REVERSIBLE
- May or may not alter conformation of the
enzymes
- Alters enzyme activities
- It is not permanent
- Can be disrupted by the following factors
➢ Presence of excess substrates
➢ Presence of substrates with higher
affinity for the enzyme
MODES OF INHIBITION: REVERSIBLE COMPETITIVE
- the competitive inhibitor will bind to the active
site of the enzyme
- Leading to the formation of enzyme inhibitor
complex
- There is no product
- A competitive inhibitor has a part that is
identical to the substrate
➢ This ensures that the active site will
bind to the inhibitor since it has the
same part as the substrate
➢ The inhibitor will not just bind anywhere
else
- The inhibitor will compete against the
substrate for the active site of the enzyme
MODES OF INHIBITION: REVERSIBLE
NONCOMPETITIVE
- The substrate is free to bind with the active site
- The inhibitor will not fight with the substrate for
a place in the active site
➢ It will bind to locations other than the
active site
- Produces the enzyme substrate inhibitor
complex
- The inhibitor can bind even if there is an
existing substrate already
- Will not produce a product
- The shape of the active site will change as the
inhibitor binds with the enzyme
➢ Causing the substrate not being able to
fit in the active site
➢ Producing no product or no catalytic
process
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 - Suffix -ose denotes that a compound is a
carbohydrate
CLASSIFICATION OF CARBOHYDRATES

CATEGORY DESCRIPTION

MONOSACCHARIDE Has a single polyhydroxy

aldehyde or polyhydroxy
ketone

OLIGOSACCHARIDE 2-10 monosaccharide

MODES OF INHIBITION: REVERSIBLE
units covalently bonded
UNCOMPETITIVE to each other

POLYSACCHARIDE Several thousand

- The catalytic process will be the same until the
formation of enzyme substrate complex
- The inhibitor will bind to the enzyme substrate
complex
➢ Leading to the formation of the enzyme
inhibitor complex
- It will only attach when the substrate bind to the
active site
monosacchraide units
- Counted according to the number of
saccharides
- Sugar is a general designation for either a
monosaccharide or a disaccharide
MONOSACCHARIDE
- Carbohydrate that cannot be hydrolyzed to
simpler compounds
- Basic unit that comprises the carbohydrates
EXAMPLES:
➢ White
➢ Crystalline solid
➢ All that are sweet tasting
➢ Polar compounds with high melting
points
➢ Water soluble
➢ Insoluble in organic solvents
- Classified according to
➢ Based on functional group
➢ Based on number of carbon atoms

CARBOHYDRATES
- Hydrate of carbon
➢ water
- Molecular formula of carbohydrates CLASSIFICATION: FUNCTIONAL GROUPS
➢ CnH2nOn
➢ Cn(H2O)n ALDOSE KETOSE
- Refers to the following:
Contains an aldehyde Contains a ketone group
➢ Polyhydroxy aldehydes
group
➔ There is an OH
➢ Polyhydroxy ketones
➢ Compounds that can be hydrolyzed to # OF BONDS PER ELEMENT
them
➔ HYDROLYZED: broken down ELEMENT # OF BOND
into a simpler compound

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 Carbon 4

Oxygen 2

Hydrogen 1

CLASSIFICATION: # OF CARBON ATOMS

# NAME EXAMPLE - The farthest chiral carbon from the functional

group will be used to determine the enantiomer
3 Triose Glyceraldehyde
➢ If it is on the right, it is a d-enantiomer
4 Tetrose Eryhtrose ➢ If it is on the left, it is an l-enantiomer
CARBOHYDRATE PROJECTION
5 Pentose Ribose ❖ FISCHER PROJECTION
- Not enclosed in one polygon
6 Hexose Glucose ➢ Open-chain
- Used when the structure of the
7 Heptose Sedoheptulose
carbohydrate is in an open chain
- The most carbon that will be formed in a
carbohydrate will only be until 7 and the least is
3.
➢ Due to the metabolic pathway of
carbohydrates
CHIRALITY
- A chiral molecule is a molecule whose images
are not superimposable ❖ HAWORTH PROJECTION
➢ There is a difference between the - Used in carbohydrates that are in ring
images form
- For a carbon to be considered chiral, it should ➢ Cyclic carbohydrates
have: - Used in an enclosed figure
➢ 4 attached atoms or groups of atoms
➢ The 4 atoms should be different from
one another

4NUMBERING
- The most oxidized end of the molecule
has the lowest number
➢ Double-bond
- They exist in two forms that are referred to as
enantiomers
➢ Mirror image of one another
➢ D/L enantiomers
➢ The d-enantiomers dominate here in
carbohydrates

❖ D AND L MONOSACCHARIDES

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 - In drawing the other enantiomer, it
should be looked at as if it is a mirror
image
➢ Mirror image but not
superimposable
- The first carbon and the last carbon
will remain the same
- Glucose and all the other naturally
occurring sugars are d-enantiomers
STEREOISOMERS
- Same molecular formula
➢ Same number of carbon, hydrogen,
and oxygen atoms
❖ ENANTIOMERS
- The consequence of a chiral carbon
➢ The carbohydrate exists in two
forms
- Mirror images of each other
- They are nonsuperimposable
- There is an imaginary mirror in front
of the two structures
❖ DIASTEREOMERS
- The structures are not mirror images
of each other
- Even if there is one molecule that did
not correspond to the other, it is already
considered a diastereomer
❖ EPIMERS
- 2 sugars that differ in configuration
around 1 specific carbon atom
- Not mirror images
- Almost the same structures but differ in
one carbon chain
➢ The positions of the hydrogen
and hydroxyl group are flipped
horizontally
The hydroxyl group is
above
❖ ANOMER
- Hemiacetal or hemiketals which differ
only in configuration at C1
➢ C1 is the asymmetric center or
the anomeric carbon
➢ HEMIACETAL- from an
aldehyde
➢ HEMIKETAL- from a ketone
- Its asymmetry is a consequence of
mutarotation
➢ The hydroxyl group will have a
different location
➔ Up, down, equator
CYCLIC FORMATION OF CARBOHYDRATE
- All OH groups to the right of the formula will
appear in the bottom of the ring
- Left OH groups will appear above the ring
- The rotation of the formula will be
counterclockwise
- The last oxygen will bind to the first carbon
and the hydrogen will bind to the oxygen of the
first carbon
➢ The double bond between carbon and
oxygen will disappear
- The hydroxyl may stay below or up
α-stereoisomer β-stereoisomer
The hydroxyl group is
below
- Cyclization is the formation of a new
streogenic center at the anomeric carbon
➢ 2 different isomers are formed
➔ Alpha and beta
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 MONOSACCHARIDE REACTIONS
❖ OXIDATION
- Increased number of oxygen atoms
- Formation of double bonds from single
bonds
- Known as sugar acids
➢ Due to the carboxylic acid
- Product depends on the point of oxidation

SITE AGENT PRODUCT

HAWORTH PROJECTION
C-1 Tollens Aldonic Acid
D form L form

CH2OH is positioned CH2OH is positioned

above the ring below the ring
**a positive indicator (reducing sugar) is the
formation of a Ag byproduct

C-1 Benedict’s Aldonic Acid

or Fehlings

**a positive indicator (reducing sugar) is the

formation of a brick-red precipitate (copper
oxide)

- The D and L form is determined by the C-6 Enzyme Alduronic Acid

position of CH2OH on the highest-numbered
ring on the atom
➢ 6th carbon
α form β form

CH2OH and -OH (carbon CH2OH and -OH (carbon

1) are on opposite sides 1) are on same side C-1 & Nitric Acid Aldaric Acid
C-6 (HNO3)

❖ REDUCTION
CONFIRMATION - Increased number of hydrogen atoms
- Sodium Borohydride (NaBH4) is used
SIX-MEMBERED RING C-chair, B-boat, S-skew as a reagent
or twist boat - produce s sugar alcohol (alditol)
➢ 1° alcohol
FIVE-MEMBERED RING E-envelope, T-twist - Concerns the C-1 only
- Carbohydrates adapt the chair structure more SUGAR SUGAR ALCOHOL
➢ Due to the issue of stability
➢ Boat structure is less stable than the Glucose Sorbitol
chair structure

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 Galactose Galactitol

Mannose Mannitol

DERIVATIVES: PHOSPHATE ESTER FORMATION

PHOSPHATE ESTER FORMATION

❖ Formation of Derivatives
- One atom is replaced with another SUBSTRATE OH group of
➢ Glycoside formation monosaccharide
➢ Exhaustive methylation
REAGENT Inorganic oxyacids
➢ Phosphate ester formation
➢ Amino sugar formation PRODUCT Inorganic esters
DERIVATIVES: GLYCOSIDE FORMATION
- Does not react with the following reagents
DERIVATIVES: SUGAR SULFATE FORMATION
which react with C-1:
- Some polysaccharides contains sulfates
➢ Tollen’s
esterified at C-2, C-4, and/or C-6
➢ Benedict’s
- No reaction
➢ Fehling’s
- The sulfate group is negatively charged at
- Anomeric carbon replaced by glycoside
physiological pH
GLYCOSIDE FORMATION
SUGAR SULFATES IN THE BODY
SUBSTRATE Monosaccharide
(hemiacetal**) Keratan Sulfate Cornea, cartilage, and
bone
**HEMIACETAL: alcohol and ether
attached to the same carbona and Dermatan sulfate Skin, blood vessels, heart
fourth attachment occupied by a
hydrogen valves, tendons, and
lungs
REAGENT Alcohol in acid solution
Chondroitin-4-sulfate Important structural
PRODUCT Glycoside (acetal) component of cartilage
➢ Does not go and provides resistance
mutarotation to compression

DERIVATIVES: AMINO SUGAR FORMATION
- Amino sugar as the product
➢ Existence of an amine group
- Most monosaccharides can acquire an amine
group at C-2
➢ Acquired amine group can be acetylated
to form N-acetyl derivatives
DISACCHARIDES
- 2 specific sugar monomers involved and their
configurations
EXAMPLES:
➢ SUCROSE: d-glucose and d-fructose
➢ MALTOSE: d-glucose
- The order of the 2 monomer units is necessary
if they are different kinds
EXAMPLE:
➢ LACTOSE: d-galactose + d-glucose
- The anomeric configuration of the hydroxyl
groups of each monosaccharide is different
- Joined by a glycosidic bond
- The carbons involved with the linkage is
indicated

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 EXAMPLES:
Monosaccharide Units α-D-Glucose and
➢ SUCROSE: 1→2
β-D-fructose
➢ TREHALOSE: 1→1
➢ LACTOSE: 1→4 Glycosidic Linkage 1→2
DISACCHARIDES: STRUCTURE NOMENCLATURE
- Written starting with the nonreducing sugar - Also known as the table sugar
end at the left - Only 1 form exists in either solid state or
- Anomeric and enantionmeric forms are solution
designated by prefixes - Undergo hydrolysis
➢ ANOMERIC: α and β ➢ Through sucrase (body system) or
➢ ENANTIOMERIC: d and l enantiomers acidic condition (laboratory)
EXAMPLE: - Non-reducing sugar
➢ α-D-Glucopyranosyl-(1→4)-β-D-glucopy ➢ Negative in the Tolen’s, Benedict’s and
ranose Fehling’s
➢ The anomeric part in the first
monosaccharide cannot bond because
it used for the glycosidic bond
GLUCOSE: INVERSION
- The change in the direction of rotation of the
plane-polarized light
- Catalyzed by invertase
➢ The glycosidic bond will be broken
down for the component parts of
- The atoms between the glycosidic bonds sucrose to be released
formed are indicated by numbers in - Polarimeter will be used in the laboratory to
parentheses distinguish the polarization
DISACCHARIDE FORMATION
- Monosacchardies with different numbers of DIRECTION IN POLARIMETER
rings can join together
SUCROSE Clockwise
- One water molecule will be one of the products
of this reaction INVERT SUGAR Counterclockwise
- The main product is the formation of
disaccharides
MALTOSE

SUCROSE

α-D-Glucopyranosyl-(1→4)-D-glucose

Monosaccharide Units Two D-glucose

Glycosidic Linkage α(1→4)**

**it is considered as α glycosidic

bond because the hydroxyl in the
anomeric carbon of the of reducing
sugar and the C6 of the nonreducing
sugar is on opposite sides

- Also known as malt sugar

α-D-Glucopyranosyl-(1→2)-β-D-fructofuranoside
➢ Exists in plants
- A reducing sugar

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 ➢ Positive in the Tolen’s, Benedict’s, and - Undergo hydrolysis
Fehling’s ➢ Through cellobiase (system) or aidic
- Undergoes mutarotation condition (laboratory)
➢ Inversion POLYSACCHARIDES
- Undergoes hydrolysis - Contain many monosaccharide units bonded
➢ Through sucrase (body system) or to each other by glycosidic linkages
acidic condition (laboratory) - Not sweet
LACTOSE - Yields negative results in Tolen’s and
Bendict’s solutions
- Have limited water solubility
- OH groups present can individually become
hydrated by water molecules

β-D-galactopyranosyl-(1→4)-D-glucose
Monosaccharide Units α-D-Glucose and
β-D-galactose

Glycosidic Linkage β(1→4)** BIOLOGICALLY-IMPORTANT POLYSACCHARIDES

❖ STORAGE POLYSACCHARIDE
**it is considered as β glycosidic
bond because the hydroxyl in the
➢ Starch
anomeric carbon of the of reducing ➢ Glycogen
sugar and the C6 of the nonreducing
sugar is on same side ❖ STRUCTURAL POLYSACCHARIDE
➢ Cellulose
- Also known as the milk sugar
➢ Chitin
- Undergoes mutarotation
❖ ACIDIC POLYSACCHARIDE
- Undergo hydrolysis
➢ Hyaluronic acid
➢ Through lactase (body system) and
➢ Heparin
acidic condition (laboratory)
STORAGE POLYSACCHARIDES
CELLOBIOSE

STORAGE POLYSACCHARIDES

FUNCTION Energy source in cells

EXAMPLES Starch (plants), glycogen

(animals)
❖ STARCH
β-D-gluco-hexopyranosyl-(1→4)- β-D-gluco-hexopyranose
- Homopolysaccharide
➢ Connected monosaccharides of
Monosaccharide Units Two D-glucose one kind
➢ Monosaccharide: Glucose
Glycosidic Linkage β(1→4) - Has nutritional value for humans
- Source is cellulose - Can be detected by iodine test
- Almost the same as maltose - Contains the following:
➢ Both contain 2 D-glucose AMYLOSE
➢ Difference in glycosidic bond
- A reducing sugar STRUCTURE Spiral-like
➢ Positive if it undergoes Tolen’s,
Benedict’s LENGTH OF 300-500 monomer units
- Can exist in 3 forms in aqueous solution POLYMER CHAIN

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 - FUNCTIONS:
DEGREE OF None (linear)
BRANCHING ➢ Structural component of plant
cell walls
GLYCOSIDIC α(1→4) ➔ Cotton: 95% cellulose
BOND ➔ Wood: 50% cellulose
➢ Source of nutrition
AMOUNT 15-20% of starch is in ➢ As a dietary fiber
this form
➢ Has a role in weight control
- Homopolysaccharide
AMYLOPECTIN ➢ Repeating monosaccharide:
glucose
STRUCTURE Spiral-like - Glycosidic linkage: β(1→4)
- Linear structure
LENGTH OF 100,000 monomer units - 5000 monomer units in length
POLYMER CHAIN
- Unbranched
DEGREE OF A branch occurs once - Molecular mass: 900,000 amu
BRANCHING every 25-30 glucose ❖ CHITIN
units - Gives rigidity to the exoskeletons of
crustaceans, insects, other arthropods
GLYCOSIDIC α(1→4) and α(1→6)** - Cells walls of fungi
BOND - Homopolysaccharide
**α(1→4) is used as a glycosidic
linkage but α(1→6) is used to ➢ Repeating monosaccharide:
branch out N-acetyl-α-D-glucosamine
- Glycosidic linkage: β(1→4)
AMOUNT 80-85% of starch is in - Linear in structure
this form
ACIDIC POLYSACCHARIDES
❖ GLYCOGEN
- Homopolysaccharide
STRUCTURAL POLYSACCHARIDES
➢ Repeating monosaccharide:
glucose FUNCTION Involved in a variety of
- Glycosidic linkage: α(1→4) and celular functions and
α(1→6) tissues
➢ α(1→4) is used as the
glycosidic linkage EXAMPLES Hyaluronic acid, heparin
➢ α(1→6) is used for branching - Presence of COOH makes it acidic
- Length goes up to 1,000,000 monomer ❖ HYALURONIC ACID
units - Heteropolysaccharide
- A branch occurs about once every 8-12 ➢ More than 1 monosaccharides
glucose units in a repeating unit
- Repeating units:
➢ N-acetyl-β-D-glucosamine
STRUCTURAL POLYSACCHARIDES ➢ d-GLUCURONIC ACID
- Glycosidic linkage: alternates between β(1→3)
and β(1→4)
STRUCTURAL POLYSACCHARIDES
- Approximately 50,000 disaccharide units per
FUNCTION Structural element in cain
plant cell walls. - Unbranched
Exoskeletons in animals FUNCTIONS:
➢ Lubricants in the fluid of joints
EXAMPLES Cellulose, chitin
➢ Jelly-like consistency of the vitreous
❖ CELLULOSE humor of the eye
- Water-insoluble ❖ HEPARIN
- Fibrous - Heteropolysaccharide
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 - Repeating monosaccharide:
➢ D-guluronate-2-sulfate
➢ N-sulfo-Dglucosamine-6-sulfate
- Glycosidic linkage: α(1→4)
- Approximately 15-90 disaccharide units
per chain
- Unbranched
- FUNCTION: anticoagulant
DIETARY CONSIDERATIONS

SIMPLE COMPLEX
CARBOHYDRATE CARBOHYDRATE

Dietary monosaccharide Dietary polysaccharide

or disaccharide

Sweet to taste Not sweet to taste

Natural sugar: milk, fruit Starch and cellulose

Refined sugar: sugar
cane

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