CBSE Class 11 Biology Revision Notes Chapter 9 Biomolecules

Biomolecules explains the chemical compounds found in living organisms and their role in cellular structure and function. In CBSE Class 11 Biology, this chapter covers metabolites, proteins, polysaccharides, nucleic acids, lipids and enzymes.

Biomolecules studies the organic and inorganic substances present in living tissues. Although living and non-living matter contain many similar elements, living organisms have a higher relative abundance of carbon, hydrogen and oxygen. These elements form molecules that support structure, energy storage, heredity, metabolism and enzyme activity.

Use CBSE Class 11 Biology Revision Notes Chapter 9 for 2026–27 to revise chemical composition, primary and secondary metabolites, biomacromolecules, proteins, polysaccharides, nucleic acids, protein structure and enzymes. The chapter also explains why water is the most abundant chemical in living organisms.

Key Takeaways

  • Biomolecules: All carbon compounds obtained from living tissues are called biomolecules.
  • Metabolites: Primary metabolites have identifiable functions, while many secondary metabolites are useful to humans and ecosystems.
  • Biomacromolecules: Proteins, nucleic acids and polysaccharides are true macromolecules.
  • Enzymes: Enzymes are biological catalysts that lower activation energy and increase reaction rate.

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Biomolecules Class 11 Biology Notes: Chapter Overview

Biomolecules are chemical compounds found in living organisms. They include small molecules such as amino acids, sugars and fatty acids, as well as large molecules such as proteins, polysaccharides and nucleic acids.

Category Examples
Inorganic constituents Water, salts, ions, phosphate, sulphate
Small organic molecules Amino acids, sugars, fatty acids, nucleotides
Biomacromolecules Proteins, nucleic acids, polysaccharides
Lipids Fatty acids, glycerol, phospholipids, triglycerides

Living organisms contain both organic and inorganic substances. From a biological point of view, many organic compounds are classified as amino acids, nucleotide bases, fatty acids and sugars.

How to Analyse Chemical Composition in Class 11 Biology Chapter 9 Notes

To analyse chemical composition, a living tissue is ground in trichloroacetic acid. This forms a thick slurry that is strained to obtain two fractions.

Fraction Also Called Contains
Filtrate Acid-soluble pool Small molecular weight compounds
Retentate Acid-insoluble fraction Macromolecules and membrane fragments

The acid-soluble pool contains many organic compounds. The acid-insoluble fraction contains proteins, nucleic acids, polysaccharides and lipids associated with membranes.

Analysis of Inorganic Constituents

For inorganic analysis, a tissue sample is weighed, dried and burnt. Water evaporates during drying, while carbon compounds are oxidised and removed during burning.

Step Result
Wet tissue is weighed Wet weight is obtained
Tissue is dried Water is removed
Tissue is burnt Carbon compounds are removed
Ash remains Inorganic elements and compounds are left

Ash contains inorganic elements such as calcium and magnesium. Inorganic compounds such as sulphate and phosphate may also occur in the acid-soluble fraction.

Elements in Living and Non-Living Matter

Living and non-living matter may contain similar elements, but their relative abundance differs.

Element Importance in Living Systems
Carbon Backbone of organic compounds
Hydrogen Present in water and organic molecules
Oxygen Present in water and many biomolecules
Nitrogen Present in proteins and nucleic acids
Sulphur Present in some amino acids
Phosphorus Present in nucleotides and phospholipids

A closer comparison shows that carbon and hydrogen are relatively more abundant in living tissues than in the earth’s crust.

Primary and Secondary Metabolites in Biomolecules Class 11 Notes

Metabolites are biomolecules involved in life processes. They are grouped into primary metabolites and secondary metabolites.

Primary Metabolites

Primary metabolites are biomolecules with identifiable functions in normal physiological processes.

Primary Metabolite Example or Function
Amino acids Building blocks of proteins
Sugars Energy source and structural role
Fatty acids Components of lipids
Nucleotides Building blocks of nucleic acids

Primary metabolites are commonly found in animal tissues and play known roles in growth, development and cellular function.

Secondary Metabolites

Secondary metabolites are mostly found in plants, fungi and microbes. Their direct role in the host organism may not always be clear, but many are useful to humans and ecosystems.

Secondary Metabolite Examples
Pigments Carotenoids, anthocyanins
Alkaloids Morphine, codeine
Terpenoids Monoterpenes, diterpenes
Essential oils Lemon grass oil
Toxins Abrin, ricin
Lectins Concanavalin A
Drugs Vinblastin, curcumin
Polymeric substances Rubber, gums, cellulose

Some secondary metabolites are used in medicines, perfumes, spices and dyes. Some also have ecological importance.

Biomacromolecules in CBSE Class 11 Biology Notes Chapter 9

Biomolecules are classified by molecular weight and solubility.

Type Molecular Weight Fraction
Micromolecules Usually less than 1000 Da Acid-soluble pool
Biomacromolecules Usually above 10,000 Da Acid-insoluble fraction

Proteins, nucleic acids and polysaccharides are true biomacromolecules because they are large polymeric substances.

Acid-Soluble and Acid-Insoluble Fractions

Fraction Represents Examples
Acid-soluble pool Cytoplasmic composition Amino acids, sugars, nucleotides
Acid-insoluble fraction Macromolecules from cytoplasm and organelles Proteins, nucleic acids, polysaccharides, membrane lipids

Together, these two fractions represent the chemical composition of living tissues.

Why Are Lipids Found in the Acid-Insoluble Fraction?

Lipids have molecular weights below 800 Da, so they are not true macromolecules. Still, they occur in the acid-insoluble fraction because they form cell membranes and other membrane structures.

When tissues are ground, membranes break into vesicles. These vesicles are not water-soluble, so they separate with the acid-insoluble fraction.

Average Chemical Composition of Cells

Water is the most abundant chemical in living organisms.

Component Approximate Percentage of Cellular Mass
Water 70–90%
Proteins 10–15%
Nucleic acids 5–7%
Carbohydrates 3%
Lipids 2%
Ions 1%

This table helps revise the relative abundance of major cellular components.

Amino Acids in Biomolecules Class 11 Biology Notes

Amino acids are organic compounds with an amino group and an acidic group attached to the same alpha carbon.

Part of Amino Acid Description
Amino group –NH₂
Carboxyl group –COOH
Hydrogen atom Attached to alpha carbon
R group Variable side chain
Alpha carbon Carbon to which all groups are attached

There are 20 types of amino acids found in proteins. Their properties depend mainly on the amino group, carboxyl group and R group.

Types of Amino Acids

Type Basis Example
Acidic amino acid Extra carboxyl group Glutamic acid
Basic amino acid Extra amino group Lysine
Neutral amino acid Balanced groups Valine
Aromatic amino acid Aromatic ring present Tyrosine, phenylalanine, tryptophan

Zwitterion in Amino Acids

Amino acids show ionisable –NH₂ and –COOH groups. In solutions of different pH, their structure changes.

A zwitterion is a dipolar form of an amino acid. It has both positive and negative charges within the same molecule.

Lipids in Class 11 Biology Chapter 9 Notes

Lipids are generally insoluble in water but soluble in non-polar solvents such as ether, chloroform and benzene.

Lipid Type Example or Feature
Fatty acids Long hydrocarbon chain with carboxyl group
Glycerol Trihydroxy propane
Triglycerides Fatty acids esterified with glycerol
Phospholipids Contain phosphorus and occur in membranes
Cholesterol Steroid lipid

Fatty Acids

Fatty acids have a carboxyl group attached to a hydrocarbon chain. They may be saturated or unsaturated.

Type Meaning
Saturated fatty acid No carbon-carbon double bond
Unsaturated fatty acid One or more carbon-carbon double bonds
Essential fatty acid Must be obtained from diet
Non-essential fatty acid Can be synthesised in the body

Palmitic acid has 16 carbon atoms, including the carboxyl carbon. Arachidonic acid has 20 carbon atoms, including the carboxyl carbon.

Functions of Lipids

Function Explanation
Energy storage Fats store energy
Membrane structure Phospholipids are major membrane components
Protection Lipids protect and insulate organisms
Neural role Some neural tissues have complex lipids

Proteins in Biomolecules Class 11 Notes

Proteins are polypeptides. They are linear chains of amino acids linked by peptide bonds.

Feature Description
Monomer Amino acid
Bond Peptide bond
Polymer type Heteropolymer
Number of protein amino acids 20
Ends of chain N-terminal and C-terminal

A protein is a heteropolymer because it contains different types of amino acids.

Peptides and Polypeptides

Term Meaning
Peptide bond Bond joining amino acids
Dipeptide Two amino acids joined together
Tripeptide Three amino acids joined together
Oligopeptide Short chain of amino acids
Polypeptide Long chain of amino acids

The first amino acid of a polypeptide is called the N-terminal amino acid. The last amino acid is called the C-terminal amino acid.

Essential and Non-Essential Amino Acids

Type Meaning
Essential amino acids Must be obtained from food
Non-essential amino acids Synthesised in the body

Dietary proteins supply essential amino acids.

Functions of Proteins

Protein Function
Collagen Intercellular ground substance
Trypsin Enzyme
Insulin Hormone
Antibody Fights infectious agents
Receptor Sensory reception
GLUT-4 Glucose transport into cells

Collagen is the most abundant protein in the animal world. RuBisCO is the most abundant protein in the biosphere.

Polysaccharides in CBSE Class 11 Biology Notes Chapter 9

Polysaccharides are long chains of sugars. They are macromolecules present in the acid-insoluble fraction.

Polysaccharide Building Block Function
Cellulose Glucose Plant cell wall structure
Starch Glucose Energy storage in plants
Glycogen Glucose Energy storage in animals
Inulin Fructose Storage polysaccharide
Chitin Amino-sugar derivative Arthropod exoskeleton

Starch, Glycogen and Cellulose

Feature Starch Glycogen Cellulose
Main role Plant energy storage Animal energy storage Plant structural material
Monomer Glucose Glucose Glucose
Structure Helical regions Branched Linear
Iodine reaction Blue colour Does not match starch response No blue colour

Starch can hold iodine molecules in its helical portion, giving a blue colour. Cellulose does not form such complex helices.

Chitin

Chitin is a complex polysaccharide found in the exoskeleton of arthropods. It contains amino-sugar derivatives such as N-acetyl glucosamine.

Nucleic Acids in Biomolecules Class 11 Biology Notes

Nucleic acids are polynucleotides. DNA and RNA are nucleic acids that function as genetic material.

Nucleic Acid Full Form Sugar
DNA Deoxyribonucleic acid Deoxyribose
RNA Ribonucleic acid Ribose

Nucleotide Structure

A nucleotide has three components.

Component Description
Nitrogenous base Purine or pyrimidine
Sugar Ribose or deoxyribose
Phosphate group Phosphoric acid group

A nucleoside contains a nitrogenous base and sugar. A nucleotide contains a nucleoside plus phosphate.

Nitrogenous Bases

Base Type Bases
Purines Adenine, Guanine
Pyrimidines Cytosine, Thymine, Uracil

DNA contains adenine, guanine, cytosine and thymine. RNA contains adenine, guanine, cytosine and uracil.

DNA and RNA Difference

Feature DNA RNA
Sugar Deoxyribose Ribose
Bases A, G, C, T A, G, C, U
Structure Usually double-stranded Usually single-stranded
Function Genetic material Protein synthesis and other cellular roles

Structure of Proteins in Class 11 Biology Chapter 9 Notes

Protein structure is explained at four levels: primary, secondary, tertiary and quaternary.

Primary Structure of Protein

Primary structure is the linear sequence of amino acids in a polypeptide chain.

Feature Description
Arrangement Linear
Bond Peptide bond
First amino acid N-terminal amino acid
Last amino acid C-terminal amino acid

The primary structure determines how the protein folds.

Secondary Structure of Protein

Secondary structure refers to local folding of the polypeptide chain.

Type Description
Alpha helix Helical form of polypeptide
Beta-pleated sheet Sheet-like arrangement of chain segments

Hydrogen bonds help stabilise secondary structures. In proteins, only right-handed helices are observed.

Tertiary Structure of Protein

Tertiary structure is the three-dimensional folding of one polypeptide chain.

Stabilising Force Role
Hydrogen bonds Stabilise folding
Hydrophobic interactions Help non-polar regions move inward
Electrostatic interactions Stabilise charged groups
Van der Waals forces Support close molecular packing
Disulphide bonds Stabilise some proteins

Tertiary structure is essential for many biological activities of proteins.

Quaternary Structure of Protein

Quaternary structure is found in proteins with more than one polypeptide chain or subunit.

Example Structure
Haemoglobin Two alpha and two beta subunits

The arrangement of these subunits forms the functional protein.

Enzymes in CBSE Class 11 Biology Revision Notes Chapter 9

Enzymes are biological catalysts. Almost all enzymes are proteins, but some nucleic acids also show catalytic activity and are called ribozymes.

Feature Description
Nature Mostly proteins
Function Catalyse biochemical reactions
Active site Pocket where substrate binds
Specificity Specific for substrate
Effect Lowers activation energy
Reuse Enzyme is released after reaction

All enzymes are proteins, but all proteins are not enzymes.

Enzyme Action

An enzyme works through its active site.

Step Explanation
Substrate binding Substrate binds to active site
Shape adjustment Enzyme fits more closely around substrate
Bond change Substrate bonds break or form
Product formation Enzyme-product complex forms
Product release Product leaves and enzyme is free again

Enzymes increase reaction rate without being consumed.

Activation Energy and Enzymes

Activation energy is the energy needed to start a reaction. Enzymes lower activation energy, so reactions occur faster.

For example, carbonic anhydrase speeds up the formation of carbonic acid from carbon dioxide and water.

Factors Affecting Enzyme Activity

Enzyme activity depends on temperature, pH, substrate concentration and chemicals that bind to enzymes.

Temperature and pH

Factor Effect
Low temperature Enzyme becomes temporarily inactive
Optimum temperature Maximum enzyme activity
High temperature Enzyme may denature
Optimum pH Maximum activity at specific pH
pH change Alters enzyme structure and activity

Each enzyme has an optimum temperature and optimum pH.

Substrate Concentration

With increasing substrate concentration, the reaction velocity rises at first. After a point, all enzyme active sites become occupied.

Stage Explanation
Low substrate concentration Reaction rate increases
More substrate added More enzyme-substrate complexes form
Saturation point All active sites are occupied
Vmax Maximum velocity is reached

After Vmax, adding more substrate does not increase the reaction rate.

Enzyme Inhibition

Enzyme activity can decrease when a chemical binds to the enzyme. This process is called inhibition, and the chemical is called an inhibitor.

Type Meaning Example
Competitive inhibition Inhibitor resembles substrate and competes for active site Malonate inhibits succinic dehydrogenase

Competitive inhibitors reduce enzyme action by preventing the substrate from binding to the active site.

Classification of Enzymes in Biomolecules Class 11 Notes

Enzymes are classified based on the type of reaction they catalyse.

Enzyme Class Reaction Catalysed
Oxidoreductases Oxidation-reduction reactions
Transferases Transfer of a group other than hydrogen
Hydrolases Hydrolysis of bonds
Lyases Removal of groups without hydrolysis
Isomerases Interconversion of isomers
Ligases Joining of two compounds

These six classes are important for quick enzyme revision.

Cofactors, Coenzymes and Prosthetic Groups

Some enzymes need non-protein components to become catalytically active. These components are called cofactors.

Term Meaning
Apoenzyme Protein part of enzyme
Cofactor Non-protein component needed for activity
Prosthetic group Organic cofactor tightly bound to apoenzyme
Coenzyme Organic cofactor loosely or transiently bound
Metal ion Inorganic ion required by some enzymes

Examples of Cofactors

Cofactor Type Example
Prosthetic group Haem in catalase and peroxidase
Coenzyme NAD and NADP
Metal ion Zinc in carboxypeptidase

If the cofactor is removed, catalytic activity may be lost.

Biomolecules Class 11 Notes: Quick Comparison Table

Topic Key Point
Chemical composition Living tissues contain organic and inorganic compounds
Acid-soluble pool Contains small molecules
Acid-insoluble fraction Contains macromolecules and membrane lipids
Primary metabolites Have known physiological roles
Secondary metabolites Often found in plants, fungi and microbes
Proteins Polymers of amino acids
Polysaccharides Long chains of sugars
Nucleic acids Polymers of nucleotides
Enzymes Biological catalysts

Important Terms from Biomolecules Class 11 Biology Notes

Term Meaning
Biomolecule Chemical compound found in living organisms
Acid-soluble pool Filtrate obtained after TCA treatment
Acid-insoluble fraction Retentate containing macromolecules
Primary metabolite Biomolecule with known physiological function
Secondary metabolite Compound with unclear direct host role but ecological or human use
Micromolecule Small biomolecule below about 1000 Da
Biomacromolecule Large molecule in acid-insoluble fraction
Amino acid Monomer of proteins
Peptide bond Bond joining amino acids
Protein Heteropolymer of amino acids
Polysaccharide Long chain of sugars
Nucleotide Nitrogen base, sugar and phosphate
Nucleoside Nitrogen base and sugar
Enzyme Biological catalyst
Active site Substrate-binding pocket of enzyme
Cofactor Non-protein component needed for enzyme activity
Competitive inhibitor Inhibitor that competes with substrate for active site

NCERT-Based Exam Points

  • Living and non-living matter may contain similar elements.
  • Carbon and hydrogen are relatively more abundant in living organisms than in the earth’s crust.
  • Trichloroacetic acid is used to analyse organic compounds in living tissue.
  • The filtrate is called the acid-soluble pool.
  • The retentate is called the acid-insoluble fraction.
  • Ash contains inorganic elements.
  • All carbon compounds obtained from living tissues are called biomolecules.
  • Amino acids have an amino group and an acidic group on the alpha carbon.
  • Proteinaceous amino acids are of 20 types.
  • Lipids are generally water-insoluble.
  • Phospholipids are found in cell membranes.
  • Nitrogenous bases include adenine, guanine, cytosine, thymine and uracil.
  • Nucleoside contains a base and sugar.
  • Nucleotide contains base, sugar and phosphate.
  • DNA and RNA function as genetic material.
  • Primary metabolites have identifiable physiological functions.
  • Secondary metabolites include alkaloids, flavonoids, rubber and essential oils.
  • Biomacromolecules include proteins, nucleic acids and polysaccharides.
  • Lipids are not strictly macromolecules.
  • Water is the most abundant chemical in living organisms.
  • Proteins are polypeptides.
  • Proteins are heteropolymers of amino acids.
  • Collagen is the most abundant protein in the animal world.
  • RuBisCO is the most abundant protein in the biosphere.
  • Starch is the storage polysaccharide in plants.
  • Glycogen is the storage polysaccharide in animals.
  • Cellulose is a structural polysaccharide in plant cell walls.
  • Chitin occurs in arthropod exoskeletons.
  • Proteins have primary, secondary, tertiary and quaternary structures.
  • Almost all enzymes are proteins.
  • Ribozymes are nucleic acids with catalytic activity.
  • Enzymes lower activation energy.
  • Enzyme activity depends on temperature, pH and substrate concentration.
  • Malonate is a competitive inhibitor of succinic dehydrogenase.
  • Enzymes are classified into six major classes.

Useful Links for Class 11 Biology Revision Notes

Section Useful Links
Revision Notes CBSE Class 11 Biology Revision Notes
Biology Notes CBSE Class 11 Biology Revision Notes Chapter 1
Biology Notes CBSE Class 11 Biology Revision Notes Chapter 2
Syllabus CBSE Class 11 Biology Syllabus
NCERT Solutions NCERT Solutions Class 11 Biology
Sample Papers CBSE Sample Papers for Class 11 Biology
Important Questions Important Questions Class 11 Biology
NCERT Books NCERT Books for Class 11 Biology

FAQs (Frequently Asked Questions)

Biomolecules Class 11 notes cover chemical composition, primary and secondary metabolites, biomacromolecules, proteins, polysaccharides, nucleic acids, protein structure and enzymes. These topics explain the molecules that build living tissues and support cellular functions.

Revise protein structure in four levels: primary, secondary, tertiary and quaternary. Primary structure is the amino acid sequence. Secondary structure includes alpha helix and beta-pleated sheet. Tertiary structure is three-dimensional folding. Quaternary structure has multiple polypeptide subunits.

Primary metabolites have known functions in normal physiological processes. Amino acids, sugars and fatty acids are examples. Secondary metabolites occur mainly in plants, fungi and microbes. Alkaloids, flavonoids, essential oils, rubber and antibiotics are examples.

Lipids are small molecules, but they form cell membranes and other membrane structures. During tissue grinding, membranes break into water-insoluble vesicles. These vesicles separate with the acid-insoluble fraction, so lipids appear in that fraction.

Enzymes are biological catalysts that increase reaction rate by lowering activation energy. They are classified into six major groups: oxidoreductases, transferases, hydrolases, lyases, isomerases and ligases.