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Introduction
to
Plant Metabolites
Metabolites definition
• Metabolites are the intermediate products
produced during metabolism, catalyzed by
various enzymes that occur naturally within cells.
• Examples., Carbohydrate, proteins, antibiotics,
glucose, alkaloids, glycosides, tannins,
flavonoids, Tannins, lipids, resins and pigments.
• The term metabolites are usually used for small
molecules.
• Generated in plants and animals bodies.
• Plant metabolites are of two types:
1. Primary Metabolites
2. Secondary Metabolites
Primary metabolites
• Primary metabolites: Molecules that are essential for growth and
development of an organism.
• Involved in the primary metabolic processes of respiration and
photosynthesis.
• They maintain the physiological functions of the body and are known as
central metabolites.
• Produces in large quantity
• Not poisonous
• Similar in all plants
Examples:
1.Carbohydrates
2.Proteins & Enzymes
3.Lipids
4.Nucleic acids
5.Hormones
6. Amino acids
7. Ethanol/Butanol
8. Lactic acids
9. Vitamins
Secondary Metabolites
• Secondary metabolites: molecules that are not essential for growth and
development of an organism.
• Produces for defensive mechanism
• Secondary metabolites are considered to be the end products of primary metabolites
• Possibly over 250,000 secondary metabolites in plants
• Produces in a small quantity
• Some are poisonous
• Different in different plants
• Syntheses through some biosynthetic pathways
• Secondary metabolites are derived from primary metabolites
Examples:
1. Alkaloids
2. Glycosides
3. Tannins
4. Volatile oils
5. Resins
6. Flavonoids
7. Toxin
8. Terpenoids
Primary Metabolites FROM THE PLANT AND ANIMALS.pptx
Production Pathway of secondary
metabolites
Carbohydrate containing crude drugs
• 1. Acacia
• 2. Agar
• 3. Tragacanth
• 4. Honey
Covered the topic already.
Proteins and Enzymes
• 1. Gelatin,
• 2. Caesin,
• 3. Proteolytic enzymes (Papain, Bromelain,
Serratiopeptidase, Urokinase, Streptokinase,
Pepsin).
Lipids(Waxes, fats, fixed oils)
• 1. Castor oil,
• 2. Chaulmoogra oil,
• 3. Wool Fat,
• 4. Bees Wax
Proteins-Casein
• Casein, the chief protein in milk and the essential
ingredient of cheese.
• In pure form, it is an amorphous white solid, tasteless
and odourless, while its commercial type is yellowish
with a pleasing odour.
• Cow’s milk contains about 3 percent casein.
• The specific gravity is 1.25 to 1.31.
• Casein is a mixture of phosphoproteins of
differing molecular weight.
• Milk consists of 80% of milk proteins (casein).
• The major constituents of casein are alpha (s1) and
alpha (s2)-caseins, β-casein and kappa-casein.
• Identification test:
Preparation of cheese from casein:
Uses:
1. Casein is used in prepared foods,
2. In medicines (atopic dermatitis-eczema) and
3. Dietary supplements, and in cosmetics.
4. Major applications of casein are paper coatings, glues, paints, plastics, and
man-made fibres.
ENZYMES
• Enzymes are the proteins which act as biological
catalysts.
• Most enzymes act best at temperatures 35-40°C; above
65°C, & presence of moisture, destroy them, activity is
negligible at 0°C.
• Although, they are soluble in water and dilute alcohol,
concentrated alcohol precipitates them.
• pH of medium directly effect their action. Enzymatic
activity reduces by HCHO, free iodine, heavy metals
and tannins.
• Enzymatic reactions proceed 8 to 10 times more
rapidly than the corresponding non-enzymatic
reactions.
ENZYMES based on functions
Classification of Enzymes:
1. Hydrolases for catalysis of hydrolytic reactions.
2. Transferases for transfer of chemical group from 1 molecule to
another.
3. Oxido-reductases catalyse the oxidation-reduction reactions.
4. Lyses catalyse the addition of groups to double bonds vice-versa.
5. Isomerases are responsible for intra-molecular rearrangements.
6. Synthetases catalyse the condensation of two molecules coupled with
the cleavage of pyrophosphate bond of ATP or similar triphosphate.
On the basis of site of action:
Endoenzymes/intracellular: Act only inside of cell: example:
synthetases, Isomerases, phosphorylases.
Exoenzymes/Extracellular: Secreted outside cell, examples:
proteases, lipases, amylases acting on proteins, lipids or starch
ENZYME STRUCTURE
• Enzymes contain a globular protein part
called apoenzyme and a non-protein part
named cofactor or prosthetic group or
metal-ion-activator.
• There are three kinds of cofactors present
in enzymes:
• Prosthetic groups: These are cofactors
tightly bound to an enzyme at all times. FAD
(flavin adenine dinucleotide) is a prosthetic
group present in many enzymes.
• Coenzyme: A coenzyme binds to an enzyme
only during catalysis. At all other times, it is
detached from the enzyme. NAD+ is a
common coenzyme.
• Metal ions: For the catalysis of certain
enzymes, a metal ion is required at the
active site to form coordinate bonds. Zn2+ is
a metal ion cofactor used by a number of
enzymes.
PAPAIN ENZYME
Biological Source: Mixture of proteolytic enzymes from latex of
unripe fruit tree Carica papaya, family Caricaceae
Method of Preparation: latex of fruits is collected in aluminium
trays + potassium metabisulphite (5 g/kg of latex) is added to
latex. Extraneous matter is cleared by passing through sieves.
latex is dried in vacuum shelf drier at 55-60°C. By spray-
drying method can be done. Dried latex is called papain.
Description: light brown or white colored amorphous powder,
typical odor & taste. Maximum proteolytic activity between
pH 5-6. Soluble in water and glycerine.
Chemical Nature: Proteolytic enzymes present in papain are
mixture of papain and chymopapain, proteolytic enzymes act
on polypeptides and amides.
Papaya fruit & latex
PAPAIN ENZYME
Identification Test:
1. It decolorises aqueous potassium permanganate solutions.
2. It causes curdling of milk (Proteolytic activity).
Uses
• Used in clarification of beverages & a meat tenderiser.
• Employed in cheese manufacture as a substitute of rennin.
• Used for degumming of silk fabrics in textile industry and in leather
industry for removing hairs of skins and hides.
• Medicinally, used as an anti-inflammatory agent.
BROMELAIN ENZYME
• Biological Source: Bromelin is a mixture of proteolytic enzymes
isolated from the stem & ripen fruit juice of Ananas comosus
(pineapple), family Bromeliaceae.
• Preparation: fruits are left on plant to ripen to full flavor. Dark green
unripe fruits gradually change to yellow and finally to deep orange. The
fruits are cut off. The enzyme bromelin does not disappear as the fruit
ripens. It is isolated from pineapple juice by precipitation with acetone
and also with ammonium sulphide.
• Characteristics
• Optimum pH of enzyme 5–8. pH below 3.0 & above 9.5 inactivates the
enzyme. Optimum temperature 50 & 60°C, effective between 20-65°C
too. The moisture content should not exceed 6%.
• Odorless to slightly putrid, buff colored powder, with irritating taste.
• Slightly soluble in water. Insoluble in organic solvents: ether,
chloroform, alcohol
BROMELAIN ENZYME
Chemical Constituents
• not a single substance, but collection of enzymes & other
compounds. It is a mixture of sulphur-containing protein-digesting
enzymes, called proteolytic enzymes or proteases. It also
contains several other substances in smaller quantities, including
peroxidase, acid phosphatase, protease inhibitors, and calcium.
Uses
• Fibrinolytic agent- Any agent that is capable of stimulating the
dissolution of a blood clot (thrombus)
• Inhibits platelet aggregation
• anti-inflammatory effect
• Increase antibiotic potentiation
PINEAPPLE FRUIT & JUICE
SERRATIOPEPTIDASE ENZYME
• Biological Source: Proteolytic enzyme derived from the bacteria
belonging to genus Serratia, present in the gut of silk worm.
Originally, it was discovered in Serratia E15 species. Now-a-days,
it is produced by fermentation bio-technology.
• Preparation
• Produced by fermentation technology by using non-pathogenic
enterobacteria species such as Serratia E 15. The larvae of silk
moth produce this enzyme in their intestine to break down
cocoon walls. It can thus be obtained from the silk moth larvae.
• Characteristics
• Vulnerable to degradation in acidic pH (destroyed by acid in
stomach).
• By Enteric coated tablets absorption through intestine.
• One unit of the enzyme hydrolyses casein to produce color
equivalent to 1.0 µmol of tyrosine per minute at pH 7.5 and 35°C.
SERRATIOPEPTIDASE ENZYME
• Chemical Constituents
• It is a proteolytic enzyme of protease type XXVI. The preparation
contains 7.1 units/mg solid.
• Uses
• Widely prescribed anti-inflammatory enzyme & enhance the
action of antibodies.
• Used as fast wound healing agent.
• Proving to be a superior alternative to the non-steroidal anti-
inflammatory drugs used to treat rheumatoid arthritis and
osteoarthritis.
• Applications in trauma surgery, plastic surgery-as a pain killer,
Respiratory medicine, obstetric and gynaecology.
UROKINASE ENZYME
• Synonym: Uroquinase.
• Biological Source: It is serine protease enzyme isolated from
human urine and from human kidney cells by tissue culture or
by recombinant DNA technology.
• Preparation
• It is a fibrinolytic enzyme produced by recombinant DNA using
genetically manipulated E. coli cells. Produced 1st as prourokinase,
then converted to active form by plasmin or kallikreins. For
medicinal use it is purified directly from human urine. A range of
adsorbents like silica gel or kaolin can be used to concentrate and
purify the product. Can further be purified by precipitation with
NaCl or ethanol or by chromatography. Human urokinase needs
sterile filtration, a septic filling and freeze drying.
UROKINASE ENZYME
• Description
• It occurs in 2 different forms: single and double polypeptide chain
forms.
• Has a half-life of 10–16 minutes after I.V. administration.
• It is lyophilised white powder, soluble in water. It is an activator of
endogenous fibrinolytic system, which converts plasminogen to
plasmin and degrades fibrinogen, fibrin clots and other plasma
proteins.
• Chemical Constituents
• They are serine proteases occur as a single low molecular weight
(33 kDa) and double, high molecular weight (54 kDa) polypeptide
chain forms.
• Uses: used to dissolve (lyse) fibrin or blood clots in anterior
chamber of eye and in acute massive pulmonary emboli.
administered I.V. dose of 4,400 units/kg body wt./ hr for 12 hrs.
STREPTOKINASE ENZYME
• Synonym: Estreptokinase, plasminokinase.
• Biological Source: It is purified bacterial protein produced from the
strains of group C β-haemolytic S.griseus.
• Preparation
• It is a bacteria derived enzyme of serine protease group. It is produced
by fermentation using streptococcal culture and isolated from the
culture filtrate. It is produced in the form of a lyophilized powder in
sterile vials containing 2,50,000 to 7,50,000 IUs.
• Description: Sterile, friable solid or white powder. Soluble in water
with maximum activity at pH 7. Solution at higher conc. is stable for 6
hours at 4°C, otherwise dilute solutions are unstable.
• Uses: Treatment of thromboembolic disorders for the Lysis of
pulmonary emboli, arterial thrombus, deep vein thrombus & acute
coronary artery thrombosis.
PEPSIN ENZYME
• Biological Source: It is obtained from the glandular layer (mucous membranes) of
fresh stomach of hog, Sus scrofa var– domesticus, belonging to family Suidae.
• Preparation
• Minced stomach linings are digested with HCl, 37°C, 2hr followed by
clarification, controlled evaporation and concentration of the digested solution.
• When processed, solution is subjected carefully to vacuum evaporation, spongy
pepsin is obtained.
• Description:
• Light buff or white colored amorphous powder.
• Occurs as translucent scales.
• Has a little acidic or saline taste with slightly meaty odour.
• Soluble in water, insoluble in alcohol, ether & chloroform.
• If heated with alkali or pancreatic enzymes, biological activity is lost. Shows
maximum activity at pH 1.8.
• Pepsin has the capacity to digest 2500 times its weight of coagulated egg albumin.
It is also available in other forms which may digest even up to 10,000 times their
weight of coagulated egg albumin.
PEPSIN ENZYME
• USES:
• It is used in the deficiency of gastric secretion.
• Pepsin is also used in the laboratory analysis of various proteins; in
the preparation of cheese, and other protein-containing foods.
• Tomorrow, continue with Lipids, lipids containing crude drugs.
• 1. Castor oil,
• 2. Chaulmoogra oil,
• 3. Wool Fat,
• 4. Bees Wax
Primary Metabolites FROM THE PLANT AND ANIMALS.pptx

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Primary Metabolites FROM THE PLANT AND ANIMALS.pptx

  • 2. Metabolites definition • Metabolites are the intermediate products produced during metabolism, catalyzed by various enzymes that occur naturally within cells. • Examples., Carbohydrate, proteins, antibiotics, glucose, alkaloids, glycosides, tannins, flavonoids, Tannins, lipids, resins and pigments. • The term metabolites are usually used for small molecules. • Generated in plants and animals bodies. • Plant metabolites are of two types: 1. Primary Metabolites 2. Secondary Metabolites
  • 3. Primary metabolites • Primary metabolites: Molecules that are essential for growth and development of an organism. • Involved in the primary metabolic processes of respiration and photosynthesis. • They maintain the physiological functions of the body and are known as central metabolites. • Produces in large quantity • Not poisonous • Similar in all plants Examples: 1.Carbohydrates 2.Proteins & Enzymes 3.Lipids 4.Nucleic acids 5.Hormones 6. Amino acids 7. Ethanol/Butanol 8. Lactic acids 9. Vitamins
  • 4. Secondary Metabolites • Secondary metabolites: molecules that are not essential for growth and development of an organism. • Produces for defensive mechanism • Secondary metabolites are considered to be the end products of primary metabolites • Possibly over 250,000 secondary metabolites in plants • Produces in a small quantity • Some are poisonous • Different in different plants • Syntheses through some biosynthetic pathways • Secondary metabolites are derived from primary metabolites Examples: 1. Alkaloids 2. Glycosides 3. Tannins 4. Volatile oils 5. Resins 6. Flavonoids 7. Toxin 8. Terpenoids
  • 6. Production Pathway of secondary metabolites
  • 7. Carbohydrate containing crude drugs • 1. Acacia • 2. Agar • 3. Tragacanth • 4. Honey Covered the topic already.
  • 8. Proteins and Enzymes • 1. Gelatin, • 2. Caesin, • 3. Proteolytic enzymes (Papain, Bromelain, Serratiopeptidase, Urokinase, Streptokinase, Pepsin).
  • 9. Lipids(Waxes, fats, fixed oils) • 1. Castor oil, • 2. Chaulmoogra oil, • 3. Wool Fat, • 4. Bees Wax
  • 10. Proteins-Casein • Casein, the chief protein in milk and the essential ingredient of cheese. • In pure form, it is an amorphous white solid, tasteless and odourless, while its commercial type is yellowish with a pleasing odour. • Cow’s milk contains about 3 percent casein. • The specific gravity is 1.25 to 1.31. • Casein is a mixture of phosphoproteins of differing molecular weight. • Milk consists of 80% of milk proteins (casein). • The major constituents of casein are alpha (s1) and alpha (s2)-caseins, β-casein and kappa-casein.
  • 12. Preparation of cheese from casein: Uses: 1. Casein is used in prepared foods, 2. In medicines (atopic dermatitis-eczema) and 3. Dietary supplements, and in cosmetics. 4. Major applications of casein are paper coatings, glues, paints, plastics, and man-made fibres.
  • 13. ENZYMES • Enzymes are the proteins which act as biological catalysts. • Most enzymes act best at temperatures 35-40°C; above 65°C, & presence of moisture, destroy them, activity is negligible at 0°C. • Although, they are soluble in water and dilute alcohol, concentrated alcohol precipitates them. • pH of medium directly effect their action. Enzymatic activity reduces by HCHO, free iodine, heavy metals and tannins. • Enzymatic reactions proceed 8 to 10 times more rapidly than the corresponding non-enzymatic reactions.
  • 14. ENZYMES based on functions Classification of Enzymes: 1. Hydrolases for catalysis of hydrolytic reactions. 2. Transferases for transfer of chemical group from 1 molecule to another. 3. Oxido-reductases catalyse the oxidation-reduction reactions. 4. Lyses catalyse the addition of groups to double bonds vice-versa. 5. Isomerases are responsible for intra-molecular rearrangements. 6. Synthetases catalyse the condensation of two molecules coupled with the cleavage of pyrophosphate bond of ATP or similar triphosphate.
  • 15. On the basis of site of action: Endoenzymes/intracellular: Act only inside of cell: example: synthetases, Isomerases, phosphorylases. Exoenzymes/Extracellular: Secreted outside cell, examples: proteases, lipases, amylases acting on proteins, lipids or starch
  • 16. ENZYME STRUCTURE • Enzymes contain a globular protein part called apoenzyme and a non-protein part named cofactor or prosthetic group or metal-ion-activator. • There are three kinds of cofactors present in enzymes: • Prosthetic groups: These are cofactors tightly bound to an enzyme at all times. FAD (flavin adenine dinucleotide) is a prosthetic group present in many enzymes. • Coenzyme: A coenzyme binds to an enzyme only during catalysis. At all other times, it is detached from the enzyme. NAD+ is a common coenzyme. • Metal ions: For the catalysis of certain enzymes, a metal ion is required at the active site to form coordinate bonds. Zn2+ is a metal ion cofactor used by a number of enzymes.
  • 17. PAPAIN ENZYME Biological Source: Mixture of proteolytic enzymes from latex of unripe fruit tree Carica papaya, family Caricaceae Method of Preparation: latex of fruits is collected in aluminium trays + potassium metabisulphite (5 g/kg of latex) is added to latex. Extraneous matter is cleared by passing through sieves. latex is dried in vacuum shelf drier at 55-60°C. By spray- drying method can be done. Dried latex is called papain. Description: light brown or white colored amorphous powder, typical odor & taste. Maximum proteolytic activity between pH 5-6. Soluble in water and glycerine. Chemical Nature: Proteolytic enzymes present in papain are mixture of papain and chymopapain, proteolytic enzymes act on polypeptides and amides.
  • 18. Papaya fruit & latex
  • 19. PAPAIN ENZYME Identification Test: 1. It decolorises aqueous potassium permanganate solutions. 2. It causes curdling of milk (Proteolytic activity). Uses • Used in clarification of beverages & a meat tenderiser. • Employed in cheese manufacture as a substitute of rennin. • Used for degumming of silk fabrics in textile industry and in leather industry for removing hairs of skins and hides. • Medicinally, used as an anti-inflammatory agent.
  • 20. BROMELAIN ENZYME • Biological Source: Bromelin is a mixture of proteolytic enzymes isolated from the stem & ripen fruit juice of Ananas comosus (pineapple), family Bromeliaceae. • Preparation: fruits are left on plant to ripen to full flavor. Dark green unripe fruits gradually change to yellow and finally to deep orange. The fruits are cut off. The enzyme bromelin does not disappear as the fruit ripens. It is isolated from pineapple juice by precipitation with acetone and also with ammonium sulphide. • Characteristics • Optimum pH of enzyme 5–8. pH below 3.0 & above 9.5 inactivates the enzyme. Optimum temperature 50 & 60°C, effective between 20-65°C too. The moisture content should not exceed 6%. • Odorless to slightly putrid, buff colored powder, with irritating taste. • Slightly soluble in water. Insoluble in organic solvents: ether, chloroform, alcohol
  • 21. BROMELAIN ENZYME Chemical Constituents • not a single substance, but collection of enzymes & other compounds. It is a mixture of sulphur-containing protein-digesting enzymes, called proteolytic enzymes or proteases. It also contains several other substances in smaller quantities, including peroxidase, acid phosphatase, protease inhibitors, and calcium. Uses • Fibrinolytic agent- Any agent that is capable of stimulating the dissolution of a blood clot (thrombus) • Inhibits platelet aggregation • anti-inflammatory effect • Increase antibiotic potentiation
  • 23. SERRATIOPEPTIDASE ENZYME • Biological Source: Proteolytic enzyme derived from the bacteria belonging to genus Serratia, present in the gut of silk worm. Originally, it was discovered in Serratia E15 species. Now-a-days, it is produced by fermentation bio-technology. • Preparation • Produced by fermentation technology by using non-pathogenic enterobacteria species such as Serratia E 15. The larvae of silk moth produce this enzyme in their intestine to break down cocoon walls. It can thus be obtained from the silk moth larvae. • Characteristics • Vulnerable to degradation in acidic pH (destroyed by acid in stomach). • By Enteric coated tablets absorption through intestine. • One unit of the enzyme hydrolyses casein to produce color equivalent to 1.0 µmol of tyrosine per minute at pH 7.5 and 35°C.
  • 24. SERRATIOPEPTIDASE ENZYME • Chemical Constituents • It is a proteolytic enzyme of protease type XXVI. The preparation contains 7.1 units/mg solid. • Uses • Widely prescribed anti-inflammatory enzyme & enhance the action of antibodies. • Used as fast wound healing agent. • Proving to be a superior alternative to the non-steroidal anti- inflammatory drugs used to treat rheumatoid arthritis and osteoarthritis. • Applications in trauma surgery, plastic surgery-as a pain killer, Respiratory medicine, obstetric and gynaecology.
  • 25. UROKINASE ENZYME • Synonym: Uroquinase. • Biological Source: It is serine protease enzyme isolated from human urine and from human kidney cells by tissue culture or by recombinant DNA technology. • Preparation • It is a fibrinolytic enzyme produced by recombinant DNA using genetically manipulated E. coli cells. Produced 1st as prourokinase, then converted to active form by plasmin or kallikreins. For medicinal use it is purified directly from human urine. A range of adsorbents like silica gel or kaolin can be used to concentrate and purify the product. Can further be purified by precipitation with NaCl or ethanol or by chromatography. Human urokinase needs sterile filtration, a septic filling and freeze drying.
  • 26. UROKINASE ENZYME • Description • It occurs in 2 different forms: single and double polypeptide chain forms. • Has a half-life of 10–16 minutes after I.V. administration. • It is lyophilised white powder, soluble in water. It is an activator of endogenous fibrinolytic system, which converts plasminogen to plasmin and degrades fibrinogen, fibrin clots and other plasma proteins. • Chemical Constituents • They are serine proteases occur as a single low molecular weight (33 kDa) and double, high molecular weight (54 kDa) polypeptide chain forms. • Uses: used to dissolve (lyse) fibrin or blood clots in anterior chamber of eye and in acute massive pulmonary emboli. administered I.V. dose of 4,400 units/kg body wt./ hr for 12 hrs.
  • 27. STREPTOKINASE ENZYME • Synonym: Estreptokinase, plasminokinase. • Biological Source: It is purified bacterial protein produced from the strains of group C β-haemolytic S.griseus. • Preparation • It is a bacteria derived enzyme of serine protease group. It is produced by fermentation using streptococcal culture and isolated from the culture filtrate. It is produced in the form of a lyophilized powder in sterile vials containing 2,50,000 to 7,50,000 IUs. • Description: Sterile, friable solid or white powder. Soluble in water with maximum activity at pH 7. Solution at higher conc. is stable for 6 hours at 4°C, otherwise dilute solutions are unstable. • Uses: Treatment of thromboembolic disorders for the Lysis of pulmonary emboli, arterial thrombus, deep vein thrombus & acute coronary artery thrombosis.
  • 28. PEPSIN ENZYME • Biological Source: It is obtained from the glandular layer (mucous membranes) of fresh stomach of hog, Sus scrofa var– domesticus, belonging to family Suidae. • Preparation • Minced stomach linings are digested with HCl, 37°C, 2hr followed by clarification, controlled evaporation and concentration of the digested solution. • When processed, solution is subjected carefully to vacuum evaporation, spongy pepsin is obtained. • Description: • Light buff or white colored amorphous powder. • Occurs as translucent scales. • Has a little acidic or saline taste with slightly meaty odour. • Soluble in water, insoluble in alcohol, ether & chloroform. • If heated with alkali or pancreatic enzymes, biological activity is lost. Shows maximum activity at pH 1.8. • Pepsin has the capacity to digest 2500 times its weight of coagulated egg albumin. It is also available in other forms which may digest even up to 10,000 times their weight of coagulated egg albumin.
  • 29. PEPSIN ENZYME • USES: • It is used in the deficiency of gastric secretion. • Pepsin is also used in the laboratory analysis of various proteins; in the preparation of cheese, and other protein-containing foods. • Tomorrow, continue with Lipids, lipids containing crude drugs. • 1. Castor oil, • 2. Chaulmoogra oil, • 3. Wool Fat, • 4. Bees Wax