pesticide slides insecticides pesticised

pesticide slides

17. Dichlorodiphenyltrichloroethane

39. Dr.Ahmed Pharm.D, M.Phil. (Dept. of Pharmacognosy)
NATURAL PESTICIDES

40. •Pest is any animal , plant or micro –
organism that causes trouble , injuries
(Economic damage) or destruction to
plants or crops.

41. •The common pests includes
•insects,bacteria,fungi,rats(rodents)
and weeds.

42. •PESTICIDE-
•A pesticide is any toxic substance used to
kill animals or plants that causes
economic damage to crop or ornamental
plants.

43. METHODS OF PEST CONTROL
•There are two methods available for the
control of pest.
•1. Natural control
•2. Artificial control

44. •NATURAL CONTROL
•Topographical influence of the seasons
changes, changing temperatures, rainfall,
soil, atmospheric humidity and other
natural factors also shows their effect on
insects and their hosts.

45. •ARTIFICIAL CONTROL
•Artificial control of pest have been
developed by man.
•These methods can be categorized as
Mechanical, Agricultural, Chemical and
Biological methods

46. •Mechanical control:
•Byusingmanuallabouraswellas
mechanical devices for collection or
destruction of pest. like hand picking,
burning, trapping are employed for the
destruction of eggs, larvae and adult
insects

47. •Agriculture control:
•It is the oldest method.
•It includes deep ploughing for
eradication of weeds and early stages of
insects.

48. •Alternative crop rotation of changing
environmental conditions are some
methods which lead to obstruction of the
life cycle of pests.

49. •Chemical control:
•Chemical agents are used for killing pests
or for protecting crops, animals or other
properties against the attack of the pest.
Like DDT,BHC,Alderin, Endrin

50. •Biological control:
•Biological control by using plant or
animal materials for controlling many
harmful pests
•Likeinsect
hormones
( Juvenile)
•Insects are eaten by birds
Ecdysoneand

51. Classification of pesticides:
•Pesticides are classified according to the
pest they control
•Insecticides (Ants, moths, cockroaches)
•Herbicides (Weeds)
•Fungicides (Control fungal diseases)
•Rodenticides (Rats)

52. Mechanism of action of pesticides
•Broad categories - As
•1. Stomach poisons:
•Kill by being taken into stomach,
absorbed in the blood and leads to the
death of the pest due to the toxic action.

53. •2. Contact insecticides:
•Kill by direct or indirect contact with the
insect or sometimes it penetrates inside
the body and causes oxidation and
suffocates the insect.

54. •3. Fumigants:
•Can be applied only in enclosed areas
where it surrounds the insect, enters their
breathing pores and kills.

55. Advantages:
•1. They are cheap (They are economical)
•2.Theyarelessharmfultothehuman
beings and more effective against pest
•3.Theyaremorestableandcanbekept
for prolonged period (Degradation is less)

56. •4.They can be used to control the carriers
of vector borne diseases like malarial,
sleeping sickness and dengue fever.

57. •Dis- advantages:
•The onset of action is slow
•Thequantityofpesticiderequiredmay
be more due to crude components

58. Natural Pesticides:
Pyrethrum Flower ,
Neem leaves and oil ,
Tobacco leaves,
Nuxvomica seed,
Sabadilla seeds,
Ryania root and stem
Derris root and rhizome

59. •Synonyms:
•Natural pyrethrum, insect flowers
•Biological source:
•Pyrethrumconsistsofmoreorlessfully
expandedflowerheadsofChrysanthenium
cinerarifolium
•Family:Compositae

60. Chemical constituents:
Active constituents are Pyrethrins, which are
organic esters, chemicals made up of carboxylic
acid and keto alcohols.
The main constituents are Pyrethrin I and II. It
also contains Cinerin I and II, Jasmoline I and II

61. I.P. Standards
•i)Pyrethrumshouldcontainnotmorethan
5% of naturally adhering stems.
•ii) Ash: Not more than 8%
•iii) Acid insoluble ash - Not more than 1%

62. Uses:
•1.Used as insecticide
•2.Contact poison,
•It paralyses in short time, used in the form of
wettable powder, emulsion concentrate,
kerosene solution (20% of Pyrethrins)

63. •Many a time,
•Pyrethrumextractismixedwithother
insecticides ( like DDT
•(Dichloro-diphenyl-trichloro-ethane),
Sulfoxidesetc)whichincreasetheactionof
pyrethrum.

64. •Other varieties
•Chrysanthemum coccineum
•Chrysanthemum marschalli

65. •Synonyms :Tamaku (Hindi)
•Biological source:
•Tobaccoconsistsofthedriedleavesof
Nicotiana tobacum and Nicotiana rustica
•Family: Solanaceae

66. Chemical constituents:
•It contains pyridine alkaloids. The main
constituent is Nicotine, Nicotyrine, Nicotimine,
Anabasine, Anatabine
•It also contains carbohydrates – Sucrose,
starch, pectin, cellulose, lignins and pentoses

67. Uses:
•Sedative,
•Antispasmodic,
•Veterinary anthelmintic,
•Useful in smoking and agriculture insecticide
•Manufactureofnicotinicacidand
nicotinamides

68. •Synonyms:
•Hindi- Nim, Malayalam- Veppa
•Biological source:
•Itconsistsoffreshleavesoftheplantknown
as Azadirachta indica
•Family:Meliaceae

69. Chemical constituents:
•It contains bitter principle Nimbidin, complex
liminoid compound named azadirachtin,
meliantrol and salanin etc.

70. Uses:
•The bark of neem tree is a good bitter tonic,
used in malarial fever, and in skin diseases,
used as an insect repellent.
•Insecticide,
properties.
activity.
nematicideand
Seedoilpossesses
antimicrobial
spermicidal

71. •Biological source:
•It consists of dried root and rhizomes of
Derris elliptica and Derris malaccensis
•Family : Leguminosae

72. •Chemical constituents:
•It contains isoflavonoid derivativeRotenone
•Tephrosin
•Toxicarol
•Degnelin

73. •Uses :
•1. Contact poison
•2.Usedintheformofsprayforkilling
vegetable insects during harvesting time such
as leaf hopper

74. •Biological source:
•Itconsistsofdried
Schoenocaulon officinale
•Family : Liliaceae
ripeseedsof

75. •Chemical constituents:
•It contains
•Sabadine,
•Cevadine ( Veratrine),
•Eratridine,
•Sabadilline and
•Cavadine

76. •Uses:
•It is an insecticide used to kill house flies and
bugs in the form of spray or dust.

77. •Biologicalsource:Itconsistsofdriedroot
and stems of Ryania speciosa
•Family : Flacourtiaceae
constituents:Alkaloidi.e•Chemical
Ryanodine
•Uses: Insecticide

78. •Biological source:
•Nuxvomica consists of the dried, ripe seeds of
Strychnos nux-vomica
•Family:Loganiaceae
•It contains not less than 1.2% of strychnine.

79. •Active constituents:
•It contains about 1-5% of bitter alkaloids
( Indole alkaloids ).
•The chief constituents of alkaloids are
Strychnine, Brucine, vomicine,
pseudostrychinine, Glycoside – Monoterpene
glycoside - Loganin, Fixed oil - 2 - 4 %

80. •Uses:
•Spinal cord stimulant.
•In cases of neurasthenia (excessive fatigue of
neurotic origin).
•As a circulatory stimulant.
•Nerve and sex tonic.
•Bitter Stomachic (strengthening of stomach
and promoting its action).

81. ENVIRONMENTAL EFFECT OF HERBICIDES AND PESTICIDES

130. ENZYMES
Prepared by Dr. Ahmed Mirza

131. Enzymes
•Enzymes are the specialized protein which are synthesized in
the living cells & catalyze biochemical reactions in various
organs.
•The term enzyme was first proposed by Welhelm Kuhne in
1878
•Amelme Payen and Jean Francois reported the presence of
Diastase (known as amylase) which convert the starch into
sugar.

132. •Louis Pasteur postulated that enzyme of
the yeast are linked with structure and life
of the yeast.
•Sumner isolated urease enzyme in
crystalline form from jack bean extract.
He suggested that enzyme was protein in
nature,

133. General properties of enzymes
1.Enzyme are colloids and are soluble in water and dilute
alcohol, but are precipitated by concentrated alcohol.
2.Certain heavy metals, formaldehydes and free iodine retard
the enzyme activity. There activity is markedly affected by
the pH of the medium in which they act or by the presence
of other substances in this medium. They are highly
selective in their action.
3.Enzymes require a specific temperature called the optimum
temperature for their optimum activity which is around
37°C for human enzymes. Above 37°C the rate of enzyme
activity slow down and at about 60°C the get denatured and
the rate of reaction will be zero.

134. 5. The enzyme are proteins that range in molecular
weight from about 13,000 to as much as 840,000 Dalton.
6. Minute quantities of enzymes are required to
complete a chemical reaction.
7. The deficiency or absence of enzyme is a congenital
defect which leads to metabolic disorders.
8. Enzymes are used in the treatment of some diseases.
9. In industry, enzymes are also used for commercial
purposes.

135. Chemical nature of enzyme
•Simple Proteins
•Some enzymes are simple proteins because they require only protein
structure for their catalytic activity i.e. pepsin, trypsin and
chymotrypsin.
•Conjugated Proteins
•Several other enzymes are conjugated proteins. They require a non
protein component called a cofactor for their catalytic activity. If this
cofactor is metal ion like Mn,Mg,Zn,or Fe the enzymes are
activator.Several other enzyme require organic biomolecules as a
cofactor for the catalytic activity of the enzyme.This cofactor is
dialyzable and known as coenzyme.
•If the a cofactor metal ion or coenzyme is firmly bound to enzyme it
is called a prosthetic group.

136. MECHANISM OF ENZYMES
qThe active site of an enzyme is the region that binds
substrates, co-factors and prosthetic groups and contains
residue that helps to hold the substrate.
qActive sites generally occupy less than 5% of the total
surface area of enzyme.
qActive site has a specific shape due to tertiary structure of
protein.
qA change in the shape of protein affects the shape of
active site and function of the enzyme.

137. q When enzyme binds with the substrate to form
Enzyme-substrate complex
qIn this way bond between substrate is broken and
converted into products.
qEnzyme remain unchanged

138. Lock-and key Model
qProposed by EMIL FISCHER in
1894.
qLock and key hypothesis assumes
the active site of an enzymes are
rigid in its shape.
qThere is no change in the active
site before and after a chemical
reaction.

139. Induced-Fit Model
q More recent studies have revealed that
the process is much more likely to involve
an induced fit model(proposed by DANIAL
KOSH LAND in 1958).
qSuggests that the active site is not rigid as
the Lock-and-Key Model, but flexible. That
is, the site changes in conformation upon
binding to a substrate in order to yield an
enzyme-substrate fit.

140. Factor Altering enzyme activity
The action of various factors, e.g temperature,
concentration of the enzyme and substrate .
Contact between enzyme and substrate
Enzyme being proteins form a colloidal solution. The
substrate also must be a water soluble substance. If the
substrate is a lipid, it must be emulsified to enable it to
come into contact with the enzyme

141. Concentration of the substrate
•Keeping all other factors and using increasing concentration of the substrate,
the velocity of the reaction (v) is increased until V maximum Vmax is
reached. After Vmax is achieved any further increase in substrate
concentration falls to increase the reaction rate.After Vmax achireved the
reaction of zero order is reached .rate of reaction is directly proportional to
the concentration of enzyme itself.At this point called km the michaelis
constant
•pH
•Some enzymes act best in alkaline medium other act best in an acidic
medium.for every enzyme there is pH it acts as its best and its optimal
pH.The optimal pH for the pepsin is around 2.00.
•Trypsin the optimal pH varies 8-9 and its attack best the negatively
charged.beyond the optimal pH the rate of enzymatic reaction decreases.

142. Temperature
•All the chemical reactions are accelerated with rise in temperature
whether or not mediated by a catalyst.
•In case of enzyme catalyzed reactions it holds good up to limited
increase in temperature 50oc .Above the
temperature ,denaturation of enzyme proteins begins and the rate
of enzymatic reaction rapidly decreases showing the decrease if
enzymatic activity.

143. Enzyme Inhibition
•Certain compounds inhibit the enzyme activity. They are
called enzyme inhibitors and the phenomenon is known
as enzyme inhibition.
•Competitive inhibition
•A competitive inhibitor is any compound that bears a
close structural resemblance to a particular substrate and
compete with the substrate for binding at the same
active site on the enzyme. The inhibitor is not acted
upon by the enzyme and so remains bound to the
enzyme as enzyme-inhibitor complex

144. Chemical nature of enzymes
qMany enzymes are inactive when first
produced.
q Such enzymes inactive form are called
proenzymes or zymogens.
qThey are inactive because the active site is
not exposed and unable to bind with
substrate. Later by the action of essential
coenzymes or activator they made active.

145. qEnzymes often occur in combination with inorganic and
organic substances that have an important part in the
catalytic action.
qIf these are non protein organic compounds known as
coenzymes.
qIf they are inorganic ions, they are referred as activator.
qCoenzymes are integral part of enzyme system. Several
vitamins, thiamine chloride, riboflavin, nicotinic acid are
recognized as having a enzymatic function.
qBoth are collectively called cofactors. The cofactors bound
to the protein part of enzyme tightly. In this case cofactor
is termed as prosthetic cofactor or prosthetic group.

146. NomeNclature of eNzymes
oAn enzyme is named according to the name of the
substrate it catalyses.
oSome enzymes were named before a systematic way
of naming enzyme was formed.
Example: pepsin, trypsin and rennin
oBy adding suffix -ase at the end of the name of the
substrate, enzymes are named.
oEnzyme for catalyzing the hydrolysis is termed as
hydrolase.

147. 2. Example :
1. Esterases: including lipase, phospholipase, acetycholinesterase
and others.
carbohydrases: including diastase, lactase, maltase, invertase,
cellulase, lysozyme etc.
3. Nucleases: including ribonuclease, desoxyribonuclease,
nucleophosphatase etc.
4. Nuclein deaminases: including adenase, adenosine deaminase etc.
5. Amidases: including arginase, urease etc.
6. Proteolytic enzymes: including pepsin, trypsin, chymotrypsin,
papin, fibrinolysin, streptokinase, urokinase etc.

148. Classification of enzymes
There are several methods for classification of
enzymes few are given below.
qClassification on the basis of reaction they control
qClassification on the basis of site of action
qClassification on the basis of nature of substrate

149. Classification on the basis of reaction they
control
Six major classes are recognized
•1. Oxidoreductases
•2. Transferases
•3. Hydrolases
•4. Lyases
•5. Isomerases
•6. Ligases

150. 1. Oxidoreductases: Catalyzing oxidoreductions between
two substances.
e.g. peroxides, glucose 6-phosphate
2. Transferases: Catalyzing a transfer of functional group,
other than hydrogen, between a pair of substrates. e.g.
transmethylase, transaminase.
3. Hydrolases: Addition of H2O to the substrate and
decompose it.They don not include the enzymes catalyzing
addition or removal of water molecule from the substrate.
Catalyzing hydrolysis of esters, ether, peptide, glycosyl,
acid-anhydride, C-C, C-halide or P-N bonds. e.g.
carbohydrases, lipases, proteinases

151. 4. Lyases: catalyzing removal of groups from
substrates by mechanisms other than
hydrolysis, leaving double bond. e.g.
Fumerase
5. Isomerases: catalyzing inter conversion of
optic, geometric or positional isomers.
e.g. G-6-phosphate isomerase.
6. Ligases:These enzyme catalyse all reactions
involving the linking together of two compounds
thus forming new bonds.They are also called
synthetasescoupled to the breaking of a
pyrophosphate bond in ATP or a similar compound.
e.g. Acetyl Co-A carboxylase.

152. Classification on the basis of site of
action
•Enzyme are classified into two groups
•Endoenzymes: these enzymes act inside the cells
also called intracellular enzymes. These enzyme
are responsible for synthesis of cell components,
production of energy and metabolism. Examples
are synthetase, isomerase and phosphorylase.

153. Exoenzyme:
•They act out side the cell and called extracellular
enzymes.
•Such enzymes are digestive in their function i.e.
break down complex molecule into small units.
Examples proteases, lipases, amylases.

154. Important ENZYMES
1.The amylolytic enzymes
2. Lipolytic enzyme
3. Proteolytic enzymes
4. Oxidizing enzymes

155. Classification on the basis of nature
of substrate
•The amylolytic Enzyme or carbohydrates :
•Diastase and amylase: term applied to 2 well known
amylolytic enzymes salivary diastase or ptyalin and
pancreatic diastase or amylopsin are found in digestive
tract of animals
•Malt diastase: it is formed during the germination of
barley grains and converts starch into lactose.
•Invertase or sucrase: found in yeast and intestinal juices.
It brings hydrolysis of sucrose into glucose and fructose.

156. Maltase: cause conversion of maltose
into glucose.
Zymase: fermentation enzyme cause
conversion of monosaccharides into
alcohol and carbon dioxide.

157. The esterases
•Lipase: it is a lipolytic enzyme widely distributed in
animal and vegetable kingdoms. Found in pancreatic
juice of animals and oily seeds.
•Pectase: splits pectin into pectic acid and methyl
alcohol.
•Steapsin: it is lipolytic enzyme capable of methyl
alcohol.
•Urease: obtained from soybeans and used in laboratory
reagent for converting urea to ammonia.

158. The proteolytic enzymes
•Pepsin: is proteolytic enzyme found in the gastric
juice. And active at pH 1.8.
•Trypsin: it is formed when the proenzyme
trypsinogen is acted on by the enterokinase of the
intestinal juice. It is more active than pepsin and
converting proteoses and peptones into
polypeptides and amino acids. It is active at pH 8.

159. •Erepsin: it is found in intestinal juices. It
converts proteoses and peptones into amino
acids.
•Rennin: it is a coagulating enzyme present
in the mucous membrane of the stomach of
mammals. It curdles the soluble casein of
milk.
•Papain: it is a mixture of active proteolytic
enzymes found in the unripe fruit of the
papaya tree.

160. The oxidizing enzymes
•Peroxides: are widely distributed in plants, they
bring about the oxidation reactions that cause the
discoloration of bruised fruits.
•Thrombin: converts the fibrinogen of the
circulating blood into the insoluble fibrin of the
blood clot.
•Zymase: splitting of monosaccharides by oxidation.

161. Enzymes in diagnosis of diseases
•1.Lipase Plasma lipase levels are elevated in the acute pancreatitis
and carcinoma of pancreas.They are decreased in liver
disease,vitamin A deficiency and in diabetes mellitus.
•Amylase: Plasma amylase is increased in acute pancreatitis and in
inflammatory of salivary glands. It is decreased in liver disease.
•Trypsin: This is raised in pancreatic disease.
•Cholinesterase:Low plasma levels are seen in liver
disease,malnutrition and anemia.It is raised in nephrosis.The
enzyme is inhibited by certain drugs,poisons and insectisides and its
estimation in plasma will help in the follow up of cases of
poiusoning by these substances.

162. ANIMAL ENZYMES

164. Pepsin qProteolytic enzyme
Biological source
q Enzyme obtained from the glandular layer of the fresh stomach
of various animals like Pig, sheep or calf. Commonly from pig,
Sus scrofa family Suidae Sus is from Greek word Us meaning
HOG, scrofa is latin and means breeding sow and domesticus is
latin means the household.
qIn the digestive tract pepsin effects only partial degradation of
proteins into smaller units called peptides, which then either are
absorbed from the intestine into the bloodstream or are broken
down further by pancreatic enzymes.
qPepsin's proenzyme, pepsinogen, is released by the chief cells
in the stomach wall, and upon mixing with the hydrochloric acid
of the gastric juice, pepsinogen activates to become pepsin.

165. qPepsin is one of three principal protein-degrading, or
proteolytic, enzymes in the digestive system, the other two
being chymotrypsin and trypsin. The three enzymes were
among the first to be isolated in crystalline form.
qIn the laboratory studies pepsin is most efficient in cleaving
bonds involving the aromatic amino acids, phenylalanine,
tryptophan, and tyrosine.
qA growing problem is impaired HCl production. Without
enough HCl, pepsinogen can not be converted into pepsin,
which means that you can not break down the protein in your
food.

166. qNot producing enough HCl also makes you more prone
to bacterial and fungal overgrowths and parasites. These
can further hamper your digestion and have numerous
other negative health impacts on your body. Low HCl
also puts you at greater risk for food poisoning and
infections. Low HCl production is also associated with
increased risk in gastric cancer and many disease related
to nutrient deficiencies. For instance low B12 is
associated with Alzheimer’s but many of these cases are
because they don’t produce enough stomach acid to
absorb the B12.

167. When a piece of meat was
allowed placed in
simulated gastric juices and
heated to body temperature
only the mixture
containing full pepsin and
HCl broke down the meat
fully.

168. Preparation of pepsin
q Pepsin is prepared by using stomach linings
q The mucous membrane is separated from the
stomach by the process of stripping or it is
scrapped off
q Then it is placed in acidified water for
autolysis at 37ºC for 2 hours
qThe liquid so obtained consists of both pepsin
and peptone

169. Pepsin extract
qPepsin occur as lustrous, transparent, or translucent
scales, as granular or spongy masses.
qranging in color from light yellow to light brown, or
as fine white or cream colored amorphous powder.
qIt is free from offensive odor and has a slightly acid
or saline taste.
qPepsin digests not less than 3000 and not more than
3500 times its weight of coagulated egg albumin.
qA pepsin of higher digestive power may be reduced to
the standard by admixture with a pepsin of lower
power or with lactose.

170. Uses
qPepsin is administered to assist gastric digestion. It is a
proteolytic enzyme and should preferably be given after
meals and followed by a dose of HCl acid.
qUsually dose is 500mg.
qIt is often combined with pancreatin in product
fromulations.
qPepsin is used for a variety of applications in food
manufacturing: to modify and provide whipping qualities
to soy protein and gelatin.
qPepsin has a long history of use in medicine, but its actual
beneficial contribution is poorly documented.

171. qIt is used in the leather industry to remove hair
and residual tissue from hides.

172. RENNIN

173. RENNIN
qRennin, also called chymosin or rennin is a protease
found in rennet.
qIt is produced by newborn ruminant animals in the
lining of the abomasum to curdle the milk they ingest,
allowing a longer residence in the bowels and better
absorption.
qRennin is the partially purified milk-
curdling enzyme obtained from the glandular layer of
the stomach of the calf (Bostaurus Linne),
qbelongs to family Bovidae.

174. qIn its inactive form, rennin is known as prorennin. When milk
is consumed, the stomach produces hydrochloric acid. This
immediately connects with the prorennin and activates it,
forcing the enzyme to produce beneficial rennin. Milk
contains the caseinogen protein that includes
Økappa-casein
Øbeta-casein
Øalpha-s2
Øalpha-s1 molecules
qThe last 3 molecules catalyze the interaction between calcium
and milk. Kappa-casein doesn’t have any activity on milk and
calcium, but it can put an end to the other molecules from
precipitating. This is when the rennin enzyme becomes
effective. It hides the kappa-casein, allowing the precipitation
of beta-casein, alpha-s2 and alpha-s1 and the absorption of
milk.

175. qrennin is beneficial for coagulating or curdling
the milk. It breaks down the milk into whey or
liquid and semisolid substance. Thus, the
stomach can digest and absorb milk proteins,
which is extremely important for the human
body. In case the stomach doesn’t produce
enough rennin, the milk is not digested properly
and the calcium cannot be absorbed in the
bones and body.

176. qRenin may be prepared by macerating the minced
glandular layer of the digestive stomach of the calf in
0.5% sodium chloride solution, filtering, acidifying the
filtrate with hydro- chloric acid.
qThe enzyme is precipitated by the sodium chloride,
separated, dried, and powdered.
Description or characteristics
qRennin occurs as a yellowish white powder, or as
yellow grains or scales.
q It has a characteristic and slightly saline taste
and a special, not unpleasant odor.
Preparation of Rennin

177. Standardization
qIt is usually standardized so that it coagulates
approximately 25,000 times its own weight of
fresh cow's milk.
qIf it coagulates milk more then 25,000 times of
its own weight than lactose or NaCl is mixed
to bring its required strength.
qRennin curdles milk by converting milk
protein casein into para-casein by partial
hydrolysis.

178. Uses
q Its principal use, however, is to coagulate
milk for the manufacture of cheese.
qRennin is used as digestant in pepsin and
rennin elixir.
qUse in formation of curds.

179. Pancreatin
qPancreatin, are commercial mixtures of amylase, lipase,
and protease.
qIt is obtained from the pancreas of the hog ,Sus scorfa
Linne var.domesticus Gray (Fam.Suidae),or ox Bos
Taurus Linne (Fam. Bovidae)
qIt is a gland that lies directly inside the posterior wall of
the abdomen.
qPancreatin is used to treat a deficiency of pancreas
secretion.

180. Preparation
The fresh glands arc minced and extracted by
methods similar to those employed in the
manufacture of pepsin.

Description or characteristics
qPancreatin is a cream-colored amorphous powder
qwith a faint, characteristic, but not offensive, odor.
qIts greatest activity
is in neutral or faintly alkaline solution.
q More than traces of mineral acids or large
amounts of alkali hydroxides render pancreatin inert, and an excess
of alkali carbonates inhibits its action.

181. q Pancreatin contains, in each mg, not less
than
q1mg =25 USP units of amylase ,
q 1mg = not less than 2 USP units of lipase,
q 1mg= not less than 25 USP units of protease.
q Pancreatin of a higher digestive power may be labeled to
indicate its strength in whole-number multiples of the
3 minimum activities or may be diluted by appropriate
admixture to conform to aforementioned specifications.

182. USES
qPancreatin is a digestive aid and is also used in the
preparation of predigested foods for invalids.
qThey are used to treat malabsorption syndrome due
to pancreatic problems. Malabsorption can be caused by
conditions such as celiac disease, Crohn's disease, lactose
intolerance, and intestinal damage.
qcystic fibrosis, surgical removal of the pancreas, long
term pancreatitis, or pancreatic cancer among others.
q Enteric-coated granules of pancreatin have been used to
treat infants with celiac disease and related pancreatic
deficiencies.

183. Adverse effects
Some of these are mild such as a
q stomach upset, which may be avoided by
taking the medication with food.
qMinor reactions may go away on their
own but if they persist, contact the
physician. For major reactions, the patient
should contact the physician immediately.

184. •PROPRIETARY PRODUCTS. Elzyme ". Pan-teric®,
Viokase", Products containing both pepsin and
pancreatin in combination with bile salts. Usual dose
is 325 mg to 1 g as tablets, capsules, or granules

185. PANCRELIPASE
qPancrelipase is essentially a more concentrated form of
pancreatin.
qIt contains in
1 mg =not less than 24 USP units of
lipase ,
q100 USP units of amylase ,
q and 100 USP units of protease.
qThe primary difference between these two enzymes is
that pancrelipase contains more active lipase enzyme
than pancreatin.

186. Uses
qEmployed as a digestive aid,
qPancrelipase increases the intestinal
absorption of fat,
qthus aiding in the control of
steatorrhea.
Available form
capsules, powder packets, and tablets.

187. q The usual dose range is 8000 to 24,000 USP units of
lipolytic activity prior to each meal, to be determined by
the practitioner according to the needs of the patient
suffering from pancreatic insufficiency.
PROPRIETARY PRODUCTS
Cotazymv, Ilozyrnev, , Pancreasev.

188. Trypsin
•Crystallized trypsin is a proteolytic enzyme crystallized from an
extract of the pancrease glands of the Ox .Bos Taurus Linne
(Fam.Bovidae).
•Production
•Trypsin is produced by pancreas in the form of
trypsinogen.Trypsin is then transported to the small
intestine,where the protein cleaved into polypeptides and amino
acids.
•Process of digestion by trypsin gets started in stomach and is
continued to the small intestine where environment is slightly
alkaline.Trypsin has maximum enzymatic activity at pH 8
• h

189. Uses
•In a tissue culture lab ,trypsin is used to resuspend
cells adherent to the petri dish wall during the
process of harvesting cells
•It is also used to harvest corn and oats.
•Trypsin is vital in a cow’s diet, without it they would
not be able to digest the grass they eat.
•It has been employed orally,topically or by inhalation
or local injection for debridement of narcotic and
pyrogenic surface lesions. The current use of trypsin
is primarily topical by aerosol application for wound
and ulcer cleaning.

190. Hyaluronidase
•Hyaluronidase is an enzyme product prepared from
mammalian testes which shows the capability of
hydrolyzing hyaluronic acid like mucopolysaccharides.
Skin is considered as the largest store of hyaluronidase
in the body.
•Hyaluronidase for injection contains not more than
0.25 µg of tyrosine for each USP hyaluronidase.
•Hyaluronidase also occur in various bacterial culture
as a metabolic product.

191. qIn head of leaches and in snake venom. Because
of its action on hyaluronic acid this enzyme
promotes diffusion and hastens absorption of
subcutaneous infusions.
qUsual dose is 150USP units.
Uses
•Hyaluronidase for injection is used in the
condition of hypodermoclysis.
•It promotes diffusion, absorption and
reabsorption.

192. Urokinase
•Urokinase is a fibrinolytic enzyme isolated from
human urine. This enzyme has thrombolytic
activity and is used as an alternative to
streptokinase in the treatment of pulmonary emboli.
•Urokinase appears to have a reduced probability of
serious allergic reactions but it should be used with
caution.
•The usual dosage regimen is 4,400 units per kg of
body weight per hour for 12 hours by intravenous
infusion.

193. Streptokinase and
streptodoronase
•These are two enzyme elaborated by hemolytic
streptococci and in combination are applied locally
or topically wherever clotted blood or fibrinous or
purulent accumulations appear following injury to
the tisses.
•Streptokinase breaks down fibrin,whereas
streptodornase affects desoxyribonucleic acid and
desoxyribonucleoprotein which are the chief
constituents of pus and necrotic tissue.
•The enzyme combination is available as injection
for intramuscular use as a solution or jelly for
topical application,and as tablets for buccal and
oral administration.

194. COLLAGENASE
•Collagenase is an enzyme preparation obtained from
fermentative cultures of Clostridium histolyticum .It
cleaves collagen and is used topically to debride dermal
ulcers and severely burned areas. Care should be
exercised to avoid heavy metal inactivation of the
enzyme.Burow’s solution can be used to stop the
enzyme action it the risk of bactermia develops.
Available ointments contains 250units of collagenase
activity per g.

195. FIBRRINOLYSIN
•Fibrinolysin is in the blood serum as a protease and
in plasma as the inactive precursor,profibrinolysin (or
plasminogen),It is prepared commercially by
activating a human blood plasma fraction with
streptokinase. In the dried form ,fibrinolysin retains
its proteolytic activity almost indefinitely:however,in
solution form, it rapidly deteriorates. Its enzymatic
activity is lost completely when it is exposed to room
temperature for 6bto 8 hours. It can attack the
protein portions of dead tissues,exdutaes and

196. burns. Fibrinolysin is used primarily in
the treatment of blood clots within the
cardiovascular system. Exclusive of
thrombi of the coronary and cerebral
arteries. It is administered by
intravenous infusion in conditions such
as
phlebothrombosis ,thrombophelebitis
and pulmonary emboli.

197. SUTILAINS
Sutilains is a substances containing proteolytic
enzymes derived from the bacterium Bacillus subtillis.
It contains not less than 2.5millions USP casein units
of proteolytic activity per g.. This cream colored
powder is applied topically: in ointment form.2 to
4times daily, for wound debridement.

198. Plant Enzyme

199. PAPAIN
Botanical name: Carica papaya L.
Local name :Papita

200. PAPAIN
Papain is a substance which contains a mixture of proteolytic
enzymes found in the unripe fruit of papaya tree.
Source:
qThe papaya tree is indigenous to tropical America and is
cultivated in Sri Lanka, Tanzania, Hawaii, and Florida.
qIt attains a height of about 5 or 6 meters.
qThe fruit grows to a length of about 30 cm and a weight of 5
kg.
qThe epicarp adheres to the orange-colored, fleshy sarcocarp,
which surrounds the central Cavity. This cavity contains a
mass of nearly black seeds.

201. Isolation of papain
qThe full grown but unripe fruit is subjected to
shallow incisions on the 4 sides.
q The latex flows freely for a few seconds, but soon
coagulates.
q After collection, the coagulated lumps are shredded
and dried by the sun or by the use of artificial heat.
qIncisions and collections are made at weekly intervals
as long as the fruit exudes the latex.
qThe crude papain is purified by dissolving in the
water and precipitating with alcohol.

202. Chemical constituents
qpepsin; however, unlike pepsin, papain acts in
acid, neutral, or alkaline media.
qPapain contains several enzymes: one or more
proteolytic enzymes, among which is peptidase
I, capable of converting proteins into dipeptides
and polypeptides;
qa rennin like, coagulating enzyme that acts on
the casein of milk;

203. qan amylolytic enzyme; a clotting enzyme similar
to pectase; and an enzyme that has a feeble
activity on fats. It is quite apparent that more
than one proteolytic enzyme is present because a
single sample of papain yields variable results,
depending on the protein used. Although
differing in strength in accordance with the
method of manufacture, papain can digest about
35 times its own weight of meat.

204. Uses
qPapain is used as a digestant for proteins because it has
an action much like that of pepsin. The best grade of
papain digests 300 times its own weight of egg albumin.
qIt is employed to relieve the symptoms of episiotomy
qIt is used to tenderize meats. In the meat packing
industry, papain is used extensively for tenderizing beef.
qPROPRIETARY PRODUCTS. “Caroid " and Papase.

205. PAPAIN PRODUCT

206. Chymopapain
qchymopapain is a non pyrogenic proteolytic enzyme
obtained from latex of papaya Linn.

it is sulfhydryl enzyme similar to the papain with respect
to substrate specificities but differing in electrophoretic,
mobility, stability and solubility.
Uses
used to treat herniated lower lumbar discs in the spine.
chymopapain injections are normally given under local,
rather than general, anesthesia. About 75% of patient so
treated respond favorably.

207. Side effect
Serious side effects from the use of chymopapain
include anaphylaxis, paralysis of the legs, or death.
Dosage
The dose for a single intervertebral disc is 2 to 4
nanokatals, with a maximum dose per patient of 8
nanokatals. The procedure is referred to as
chemonucleolysis.
Available Product
Chymodiactin

208. Bromelain
botanical name:
Ananas comosus
Family :
Bromeliaceae

209. Sources
qBromelain or bromelin is a protein digesting
and milk-clotting enzyme obtained from the
juice of the pineapple plant.
qAlthough this enzyme can appear in the juice of
the fruit, it can also occur in the stem of the
plant and it is obtained from both the ripe and
unripe fruits.
qgrown in several tropical and subtropical
countries including Philippines, Thailand,
Indonesia, Malaysia, Kenya, India, and China.

210. qThe proteolytic enzymes are sulfhydryl proteases; a free sulfhydryl
group of a cysteine amino acid side chain is required for function.
qBromelain also contains peroxidase, acid phosphatase, several
protease inhibitors, and organically-bound calcium.
qThe material is blended and pressed through a filter to obtain
a supernatant liquid containing the soluble bromelain enzyme.
Further processing includes purification and concentration of the
enzyme.
qExtract of bromelain has been exhibit its over a pH range 4.5-9.8.

211. Uses
qBromelain is also employed in the production of protein
hydrolysates, in tenderizing meats, and in the leather industry.
qReduce tumor cell growth.
qBromelain has potent anti-inflammatory properties and
therefore may be useful in promoting the healing of minor
muscle injuries such as sprains and strains.
qThe bromelain content of raw pineapple is responsible for the
sore mouth feeling often experienced when eating it, due to the
enzymes breaking down the proteins of sensitive tissues in the
mouth.
q Also,raphides, needle-shaped crystals of calcium oxalate that
occur in pineapple fruits and leaves, likely cause
microabrasions, contributing to mouth discomfort.

212. q
The enzyme may also enhance the effect of the
antibiotics amoxicillin, erythromycin, penicillamine,
and penicillin.
Bromelain is a natural anticoagulant that works
by breaking down the blood-clotting protein fibrin,
so taking bromelain will improve circulation and
prevent heart conditions.
It is used commercially in many applications in the
food, beverage, cosmetic, pharmaceutical, and textile
industries.
PRESCRIPTION PRODUCT: Ananase ".

213. Interaction
Bromelain may be unsafe for some users, such as
in pregnancy, allergies, or anticoagulation therapy.
Dosage
Bromelain has demonstrated therapeutic benefits in
doses as small as 160 mg per day; however, it is thought
for most conditions the best results occur at doses of
750-1,000 mg per day.

214. BROMELAIN PRODUCT

215. BARLEY is dried grain of Hordeum vulgare
Family-Graminae
Local name -Joo

216. MALT EXTRACT
qCultivated through out the world wherever climate is
favorable
Malt or Malted Barley
qDried, artificially germinated barley grain
qGrains kept wet with water in warm room temp for two to
three days to allow the grain to absorb moisture and to start
to germinate sprout
qThe grain at this stage is called green malt.
qdried quickly and pre –toasted in an oven or kiln to the
desired colour
qMalts range in colour from very pale through crystal and
amber to chocolate or black malts

217. qEnzyme diastase Converts starch to maltose
q Stimulate embryo formation which is killed by drying
q Dry malt resembles barley & has agreeable odor and
sweet taste
q Contains sugar maltose 50-70%
qDextrins 2-15%
q Proteins 8%
qDiastase and peptase enzyme

218. Malt Extract
Dry malt extract Liquid malt extract

219. Malt extract
qExtracting malt infused with hot water at 60°C
q Concentrated at 60°C under reduced pressure
q Malt extract is mixed with 10% glycerin
q It contains dextrin, maltose, glucose and
amylolytic enzyme
qStarch soluble sugars (5times of its own
weight).

220. Uses
q Malt extract is used as easily digested nutritive and
as an aid in starch digestion.
q15g
qDiastase 50times starch sugars
q Lactase converts lactose galactose and glucose.
It is used in pt having lactose intolerance
qUsed in chronic constipation, irritable bowl
syndrome, soluble fibers may also lower the
cholesterol 10-15%.It is a bulking agent promote
bowl regularity
qUsed in Brewing & alcohol industries

221. q
Used in pharmaceutical,bakery,food items.(malt extract
syrup)
Interaction –No any interaction with food &
drug.Diabetic and allergic pt consult with doctor before use.
Available form – Liquid &Powder
An example is Maltsupex

222. MALT
PRODUCT