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BIOMOLECULES(UNDER-WATER LIFE)
MADE BY-
M. FLORA(14)
GITANJALI MOHAPATRA(54)
GUIDED BY-
ARUN KUMAR CHAB
BIOMOLECULES
• A biomolecule or biological molecule is a loosely used term for molecules present in organisms that are
essential to one or more typically biological processes, such as cell division , morphogenesis or
development.
• Biomolecules include large macromolecules (or polyanions) such as proteins, carbohydrates, lipids,
and nucleic acids, as well as small molecules such as primary metabolites, secondary
metabolites and natural products.
• A more general name for this class of material is biological materials. Biomolecules are an important
element of living organisms, those biomolecules are often endogenous , produced within the organismbut
organisms usually need exogenous biomolecules, for example certain nutrients, to survive.
CLASSIFICATION OF BIOMOLECULES
BIOCHEMISTRY
CARBOHYDRATES
SUGARS
STARCHES
CELLULOSE
LIPIDS
FATS AND OIL
PEPTIDE BONDS
SATURATED FATS
NUCLEIC ACID
UNSATURATED
FATS
BASES
MEMBRANES
PENTOSE SUGARS
PROTEINES
AMINO ACID
RNA
DNA NUCLEICOTIDES
PROTEINS
WHAT ARE PROTEINS ?
• Proteins are the most abundant biomolecules of the living system.
• They occur in every part of the body and form the fundamental basis of structure and functions of life.
• The word protein is derived from Greek word “proteios” which means primary or prime importance.
• All proteins are polymers of α-amino acids.
• A polypeptide with more than hundred amino acids residues , having molecular mass higher than
10000u is called a protein.
AMINO ACIDS
• An amino acid is an organic molecule that is made up of a basic amino group (−NH2), an acidic
carboxyl group (−COOH), and an organic R group (or side chain) that is unique to each amino
acid. The term amino acid is short for α-amino [alpha-amino] carboxylic acid.
• Amino acids can be classified as α , β ,γ, δ and so on.
α-Αmino Αcid
NH2 R-CH-COOH
CLASSIFICATION OF PROTEIN
• Amino acids are classified as acidic , basic or neutral depending upon relative number of amino and carboxyl
group in their molecule.
• Amino acids are usually colourless , crystalline solid , water soluble , high melting solids and behave like
salts.
• This behavior is due to presence of both acidic(carboxylic acid) and basic (amino group) in same molecule.
• Amino acid which can be synthesized in the body are known as non- essential amino acids.
• Amino acid which cannot be synthesized in the body are known as essential amino acids , which should be
obtained through our diet.
TYPES OF AMINO ACIDS
1.Acidic-(more number of carboxylic group)
Eg:- Glutamic Acid , Asparatic Acid , etc..
2.Basic-(more number of amine group)
Eg:- Histidine , Arginine, Lysine, etc..
3.Neutral-(equal number of carboxylic group and amine group)
Eg:- Leucine , Methionine , Phenylalanine , etc..
• Carboxylic group can lose a proton and amino group can accept a proton giving rise a dipolar ion known as zwitter ion.
This is neutral but containg
• In zwitter ionic form , amino acids shows amphoteric behaviour as they react with both with acids and bases.
• All naturally occurring α-Αmino Αcid show amphoteric behaviour except glycine.
• Higher percentages of protein are found in hair, bones, and other organs and tissues with a low water content.
STRUCTURE OF PROTEINS
• The polymers of α-amino acids are connected to each other by peptide bond or peptide linkage.
• Peptide linkage is an amide formed between –COOH group and –NH2 group.
• the reaction between two molecules of similar or different amino acids , proceeds through the
combination of the amino group of one molecule with the carboxyl group of other.
• This results in elimination of a water molecule and formation of a peptide bond –CO-NH-(dipeptide,
because it’s made up of 2 amino acids)
• Eg:- carboxyl group of glycine combines with the amino group of alanine we get a dipeptide
,glycylalanine
When a poly peptide chain
run
Parallel and are held
together by hydrogen And
di-sulphide bonds, the fiber
like structure is formed.
E.g: Keratin, myosin
Chains of polypeptides
Coil around to give a
spherical shape, these are
soluble in water.
E.g: insulin, albumins
Proteins
Fibrous
proteins
Globular
proteins
Proteins can be classified into types on the basis of their molecular shape
primary secondary tertiary quaternary
α- helix β- pleated Sheet
Globular
structure
• One or more polypeptide
chain
• Specific sequence of
arrangement of amino acid
in a polypeptide
• Overall folding of
polypeptide chain
• Stabilized by hydrogen
bond , di-sulphide
linkage, Van der waals
force
• Two or more
polypeptide
chain
• Long polypeptide chain
• Regular folding of chain
CLASSIFICATION OF PROTEIN
A. B.
α-helix structure of
protein
β-pleated sheet
structure of protein
PROTEIN STRUCTURES
PRIMARY STRUCTURE SECONDARY STRUCTURE
TERTIARY STRUCTURE QUATERNARY STRUCTURE
SOURCES OF PROTEINS
Selenium
Actin and myosin
Lysine,methionine,etc.
Sarcoplasmic Myofibrillar
Myoglobin
Tyrosine. Casein.
RELATION OF UNDERWATER LIFE AND
BIOMOLECULES
• marine biotechnology is “a natural extension of cultural practices of garnering food from the ocean”
• The marine ecosystem is large, and thus there are many sub-fields of marine biology. A subfield of marine
biology studies the relationships between oceans and ocean life, and global warming and environmental
issues (such as carbon dioxide displacement).
• Recent marine biotechnology has focused largely on marine biomolecules, especially proteins, that may
have uses in medicine or engineering. Marine environments are the home to many exotic biological
materials that may inspire biomimetic materials.
• biomolecules such as important polysaccharides which are the most abundant renewable biomaterial
found in oceans.
• One of the world’s healthiest protein sources comes from the ocean. It is the largest global biomass,
virtually accessible from all corners of the world. There are various fish species that are abundant and
sustainable, and fish are the healthiest protein source on the planet.
• Fish also contains a complete amino acid profile to assure optimal healthy development of the brain, bones
and whole body. In fact, fish has higher nutrient and protein value than any other type of protein available.
In short, fish is a complete protein source
UNDERWATER ORGANISMS
~Yellowtail
The genus Seriola or yellowtail, a highly active fish belonging
to the Carangidae family, is found in the Atlantic, Indian and
Pacific oceans, with most species occurring in tropical and
subtropical waters
One four-ounce filet of this slightly oily fish has a potent 34
grams of protein for 212 calories.
SCINTIFIC NAME- Labeo Catla
INFORMATION - Catla is a fish with large and
broad head, a large protruding lower jaw, and
upturned mouth. It has large, greyish scales on
its dorsal side and whitish on its belly.
Catla is a surface and midwater feeder.
Adults feed on zooplankton using large gill
rakers, but young ones on both zooplankton and
phytoplankton.
MEDICAL USE- Asthma , heart diseases,
inflammatory diseases, mineral deficiency.
UNDER-WATER ORGANISM
A tuna (also called tunny) is a saltwater fish that belongs to
the tribe Thunnini , a subgrouping of the Scombridae
(mackerel) family.
Yeah, tuna fish! Four ounces contain 33 grams of
protein and 225 calories
b.TUNA
Duckweed, the smallest flowering plant in the world, has
protein contents of up to 45 percent, which is among the
highest protein levels in the plant kingdom. Although usually
perceived as food sources for birds and fish, people in Laos,
Thailand, Vietnam, and parts of Africa have been eating
various duckweeds for centuries. Add in some info about
legumes, whole grains, seeds
PLANTS-DUCKWEED
MEDICAL USE- According to some
medical research, several chemicals
found in brown algae can work as
antioxidants, cancer suppressant as
well as an anti-inflammatory and immunity booster.
Microalgae are single-cell organisms that can only be seen with the aid of a microscope, and
mostly occur in fresh and marine water. Both micro- and macroalgae are nutrient dense with
varying amounts of vitamins A, C, E, folate, calcium, iodine, iron, omega-3 fatty acids,
carbohydrates, protein and a variety of other nutrients. The protein content macroalgae range
from 3 to 50 percent and microalgae's protein content is even higher, ranging up to 70 percent.
3.ALGAE- (a. Brown algae)
• Spirulina is an organism that grows in both
fresh and salt water.
• It is a type of cyanobacteria, which is a
family of single-celled microbes that are
often referred to as blue-green algae.
• Just like plants, cyanobacteria can produce
energy from sunlight via a process called
photosynthesis.
• Spirulina is blue or green algae that contain
around 8 g of protein per 2 tablespoons. It is also
rich in nutrients, such as iron, B vitamins —
although not vitamin B-12 — and manganese
b. Spirulina
DENATURATION OF PROTEINS
• Denaturation, in biology, process modifying the molecular structure of a protein. Denaturation
involves the breaking of many of the weak linkages, or bonds (e.g., hydrogen bonds), within a
protein molecule that are responsible for the highly ordered structure of the protein in its natural
(native) state. Denatured proteins have a looser, more random structure; most are insoluble.
• Eg:- The coagulation of egg white on boiling .
• Curdling of milk
THANK YOU

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Biomolecules.pptx

  • 1. BIOMOLECULES(UNDER-WATER LIFE) MADE BY- M. FLORA(14) GITANJALI MOHAPATRA(54) GUIDED BY- ARUN KUMAR CHAB
  • 2. BIOMOLECULES • A biomolecule or biological molecule is a loosely used term for molecules present in organisms that are essential to one or more typically biological processes, such as cell division , morphogenesis or development. • Biomolecules include large macromolecules (or polyanions) such as proteins, carbohydrates, lipids, and nucleic acids, as well as small molecules such as primary metabolites, secondary metabolites and natural products. • A more general name for this class of material is biological materials. Biomolecules are an important element of living organisms, those biomolecules are often endogenous , produced within the organismbut organisms usually need exogenous biomolecules, for example certain nutrients, to survive.
  • 3. CLASSIFICATION OF BIOMOLECULES BIOCHEMISTRY CARBOHYDRATES SUGARS STARCHES CELLULOSE LIPIDS FATS AND OIL PEPTIDE BONDS SATURATED FATS NUCLEIC ACID UNSATURATED FATS BASES MEMBRANES PENTOSE SUGARS PROTEINES AMINO ACID RNA DNA NUCLEICOTIDES
  • 5. WHAT ARE PROTEINS ? • Proteins are the most abundant biomolecules of the living system. • They occur in every part of the body and form the fundamental basis of structure and functions of life. • The word protein is derived from Greek word “proteios” which means primary or prime importance. • All proteins are polymers of α-amino acids. • A polypeptide with more than hundred amino acids residues , having molecular mass higher than 10000u is called a protein.
  • 6. AMINO ACIDS • An amino acid is an organic molecule that is made up of a basic amino group (−NH2), an acidic carboxyl group (−COOH), and an organic R group (or side chain) that is unique to each amino acid. The term amino acid is short for α-amino [alpha-amino] carboxylic acid. • Amino acids can be classified as α , β ,γ, δ and so on. α-Αmino Αcid NH2 R-CH-COOH
  • 7.
  • 8. CLASSIFICATION OF PROTEIN • Amino acids are classified as acidic , basic or neutral depending upon relative number of amino and carboxyl group in their molecule. • Amino acids are usually colourless , crystalline solid , water soluble , high melting solids and behave like salts. • This behavior is due to presence of both acidic(carboxylic acid) and basic (amino group) in same molecule. • Amino acid which can be synthesized in the body are known as non- essential amino acids. • Amino acid which cannot be synthesized in the body are known as essential amino acids , which should be obtained through our diet.
  • 9. TYPES OF AMINO ACIDS 1.Acidic-(more number of carboxylic group) Eg:- Glutamic Acid , Asparatic Acid , etc.. 2.Basic-(more number of amine group) Eg:- Histidine , Arginine, Lysine, etc.. 3.Neutral-(equal number of carboxylic group and amine group) Eg:- Leucine , Methionine , Phenylalanine , etc..
  • 10. • Carboxylic group can lose a proton and amino group can accept a proton giving rise a dipolar ion known as zwitter ion. This is neutral but containg • In zwitter ionic form , amino acids shows amphoteric behaviour as they react with both with acids and bases. • All naturally occurring α-Αmino Αcid show amphoteric behaviour except glycine. • Higher percentages of protein are found in hair, bones, and other organs and tissues with a low water content.
  • 11. STRUCTURE OF PROTEINS • The polymers of α-amino acids are connected to each other by peptide bond or peptide linkage. • Peptide linkage is an amide formed between –COOH group and –NH2 group. • the reaction between two molecules of similar or different amino acids , proceeds through the combination of the amino group of one molecule with the carboxyl group of other. • This results in elimination of a water molecule and formation of a peptide bond –CO-NH-(dipeptide, because it’s made up of 2 amino acids) • Eg:- carboxyl group of glycine combines with the amino group of alanine we get a dipeptide ,glycylalanine
  • 12. When a poly peptide chain run Parallel and are held together by hydrogen And di-sulphide bonds, the fiber like structure is formed. E.g: Keratin, myosin Chains of polypeptides Coil around to give a spherical shape, these are soluble in water. E.g: insulin, albumins Proteins Fibrous proteins Globular proteins Proteins can be classified into types on the basis of their molecular shape
  • 13. primary secondary tertiary quaternary α- helix β- pleated Sheet Globular structure • One or more polypeptide chain • Specific sequence of arrangement of amino acid in a polypeptide • Overall folding of polypeptide chain • Stabilized by hydrogen bond , di-sulphide linkage, Van der waals force • Two or more polypeptide chain • Long polypeptide chain • Regular folding of chain CLASSIFICATION OF PROTEIN
  • 14. A. B. α-helix structure of protein β-pleated sheet structure of protein
  • 15. PROTEIN STRUCTURES PRIMARY STRUCTURE SECONDARY STRUCTURE TERTIARY STRUCTURE QUATERNARY STRUCTURE
  • 16. SOURCES OF PROTEINS Selenium Actin and myosin Lysine,methionine,etc. Sarcoplasmic Myofibrillar Myoglobin Tyrosine. Casein.
  • 17. RELATION OF UNDERWATER LIFE AND BIOMOLECULES • marine biotechnology is “a natural extension of cultural practices of garnering food from the ocean” • The marine ecosystem is large, and thus there are many sub-fields of marine biology. A subfield of marine biology studies the relationships between oceans and ocean life, and global warming and environmental issues (such as carbon dioxide displacement). • Recent marine biotechnology has focused largely on marine biomolecules, especially proteins, that may have uses in medicine or engineering. Marine environments are the home to many exotic biological materials that may inspire biomimetic materials. • biomolecules such as important polysaccharides which are the most abundant renewable biomaterial found in oceans. • One of the world’s healthiest protein sources comes from the ocean. It is the largest global biomass, virtually accessible from all corners of the world. There are various fish species that are abundant and sustainable, and fish are the healthiest protein source on the planet. • Fish also contains a complete amino acid profile to assure optimal healthy development of the brain, bones and whole body. In fact, fish has higher nutrient and protein value than any other type of protein available. In short, fish is a complete protein source
  • 18. UNDERWATER ORGANISMS ~Yellowtail The genus Seriola or yellowtail, a highly active fish belonging to the Carangidae family, is found in the Atlantic, Indian and Pacific oceans, with most species occurring in tropical and subtropical waters One four-ounce filet of this slightly oily fish has a potent 34 grams of protein for 212 calories.
  • 19. SCINTIFIC NAME- Labeo Catla INFORMATION - Catla is a fish with large and broad head, a large protruding lower jaw, and upturned mouth. It has large, greyish scales on its dorsal side and whitish on its belly. Catla is a surface and midwater feeder. Adults feed on zooplankton using large gill rakers, but young ones on both zooplankton and phytoplankton. MEDICAL USE- Asthma , heart diseases, inflammatory diseases, mineral deficiency. UNDER-WATER ORGANISM
  • 20. A tuna (also called tunny) is a saltwater fish that belongs to the tribe Thunnini , a subgrouping of the Scombridae (mackerel) family. Yeah, tuna fish! Four ounces contain 33 grams of protein and 225 calories b.TUNA
  • 21. Duckweed, the smallest flowering plant in the world, has protein contents of up to 45 percent, which is among the highest protein levels in the plant kingdom. Although usually perceived as food sources for birds and fish, people in Laos, Thailand, Vietnam, and parts of Africa have been eating various duckweeds for centuries. Add in some info about legumes, whole grains, seeds PLANTS-DUCKWEED
  • 22. MEDICAL USE- According to some medical research, several chemicals found in brown algae can work as antioxidants, cancer suppressant as well as an anti-inflammatory and immunity booster. Microalgae are single-cell organisms that can only be seen with the aid of a microscope, and mostly occur in fresh and marine water. Both micro- and macroalgae are nutrient dense with varying amounts of vitamins A, C, E, folate, calcium, iodine, iron, omega-3 fatty acids, carbohydrates, protein and a variety of other nutrients. The protein content macroalgae range from 3 to 50 percent and microalgae's protein content is even higher, ranging up to 70 percent. 3.ALGAE- (a. Brown algae)
  • 23. • Spirulina is an organism that grows in both fresh and salt water. • It is a type of cyanobacteria, which is a family of single-celled microbes that are often referred to as blue-green algae. • Just like plants, cyanobacteria can produce energy from sunlight via a process called photosynthesis. • Spirulina is blue or green algae that contain around 8 g of protein per 2 tablespoons. It is also rich in nutrients, such as iron, B vitamins — although not vitamin B-12 — and manganese b. Spirulina
  • 24. DENATURATION OF PROTEINS • Denaturation, in biology, process modifying the molecular structure of a protein. Denaturation involves the breaking of many of the weak linkages, or bonds (e.g., hydrogen bonds), within a protein molecule that are responsible for the highly ordered structure of the protein in its natural (native) state. Denatured proteins have a looser, more random structure; most are insoluble. • Eg:- The coagulation of egg white on boiling . • Curdling of milk