3. Introduction
Enzyme:
which are proteins which acts as
biological catalysts.
Play vital role in the function of cells and
activities of an organism.
Show maximum activity at 35-40 degree
C
Practically inactive at 0 degree C and
beyond 65 degree C, gets denatured.
4. 1. Papain
Source:
mixture of proteolytic enzymes obtained from the
latex of unripe fruit of tropical melon tree Carica papaya
Family: Caricaceae
Preparation:
◦ Latex of the these fruits is collected in aluminum trays.
◦ To the collected latex, Potassium metabisulphite is added.
◦ The extraneous matter is cleared out by passing through
sieves and latex is dried in vacuum shelf drier at 55-60
degree C
◦ It is also processed by spray drying method.
◦ This latex is called papain.
5. Description:
Available
as light brown or white colored amorphous powder with
typical odor and taste.
It shows maximum proteolytic activity between pH 5-6.
It is insoluble in water & glycerine.
Chemical nature:
Mixture of papain, chymopapain which acts upon polypeptie and
amides.
Identification:
It decolorizes aq. Potassium permanganate solution
It causes curdling of milk (prototypic activity)
Uses:
Clarification of beverages, meat tenderiser,
Cheese manufacturing, substitute of renin,
Degumming of silk fiber
Anti-inflammatory & symptoms of episiotomy
6. 2. Bromelain
Source:
mixture of proteolytic enzymes obtained from the
stem and ripen fruits of pineapple plant Ananas comosus
Family: Bromeliaceae
Description:
◦ Odorless to slightly putrid buff color powder with
irritating taste.
Solubility:
Soluble in water, insoluble in organic solvents like ether,
chloroform and alcohol
Use: treatment of soft tissue
inflammation, edema due to surgery and injury
7. 3. Malt Extract
Source:
obtained by extracting malt or malted barley, which is
partially and artificially germinated grain of one or more variety
of barley grain, Hordeum vulgare
Family: Graminae
Mixture of malted barley with NMT 33% malted wheat viz.
Triticum aestivum, family Graminae
Description:
◦ Occurs as yellowish-brown or amber colored viscous liquid
with a characteristic odor and taste.
◦ Contains nitrogen equivalent to NLT 4% protein.
◦ Along with protein, also contains maltose,
◦ dextrin, glucose and amylolytic enzymes.
Use: nutritive, flavouring agent, masking bitter
taste, vehicle for preparation containing codliver oil and
halibut liver oil.
8. 4. Serratiopeptidase
Source: proteolytic enzyme obtained from bacteria belonging to genus
Serratia, present in the gut of the silk worm.
Originally it was discovered in Serratia E15 species.
Now-a-days it is produced y fermentation biotechnology.
Considered as very effective bacterial enzyme and it is found to have
better effects than trypsin and chymotrypsin with negligible toxicity and
side effects,
Given orally, it enters systemic circulation in unchanged form and can
penetrate into all tissues, especially inflmaed areas.
It exerts histamine and bradykinin hydrolyzing and proteolytic effects.
Hence it reduces capillary permeability and also breakdown of proteins
and exudates and hence, supports wound healing.
Therapeutics application: resolution of inflammation, sputum
liquefaction due to lyses of various protein in sputum and hence
lowering viscosity, enhancement of antibiotic effect due to removal of
inflammatory barrier and hence, increasing antibiotic transfer to infected
areas.
9. 5. Urokinase
It
is an enzyme produced by kidney and
obtained from human urine or kidney tissue
cultures.
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 protein.
It is used to dissolve (lyse) fibrin or blood clots
in anterior chamber of eye and in acute massive
pulmonary emboli. As it is derived from human
source, it is less antigenic than enzymes with
similar actions like streptokinase.
10. 6. Streptokinase
It
is an enzyme obtained from cultures filtrates of beta
hemolytic, streptococci group C. This enzyme has the
property of activating human plasminogen to plasmin.
It is available as a sterile, friable solid or white powder.
It is soluble in water with maximum activity at pH 7, the
solution at higher concentration is stable for 6 hours at 4
degree C, otherwise dilute solutions are unstable.
It is used in the treatment of thromboembolic disorders
for the lysis of pulmonary emboli, arterial thrombus,
deep vein thrombus and acute coronary artery
thrombosis.
The activity of this enzyme is due to activation of
plasminogen to a proteolytic enzyme namely plasmin
which degrades fibrin clots, fibrinogen and other plasma
proteins.
11. 7. Pepsin
It is a substance containing proteolytic enzyme and is present in the
gastric juice of animals. It is obtained from the glandular layer (mucous
membrane) of fresh stomach of hog, sus scrofa variety domesticus,
belonging to family Suidae.
Pepsin is light buff or white colored amorphous powder, it also occurs
as translucent scales. It has a little acidic or saline taste with slightly
meaty odor. It is soluble in water, but insoluble in alcohol, ether and
chloroform.
If pepsin is heated with alkali or pancreatic enzymes, its biological
activity is lost, it 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 t 10,000
times their weight of coagulated egg albumin.
For preparation, the minced stomach linings are digested with HCl,
followed by clarification, controlled evaporation, dialysis and
concentration of the digested solution.
When processed, solution is subjected to carefully to vacuum
evaporation, spongy pepsin is obtained.
Pepsin degrades proteins into peptones and proteases.
12. 8. Lectins
They are proteins or glycoproteins without an immune origin.
They can agglutinate the cells and precipitate complex carbohydrates.
The agglutination activity of these highly specific carbohydrate binding
molecule is usually inhibited by a simple monosacchride, but for some, di,
tri and polysaccharides are required.
They are isolated from various natural sources like seeds, roots, bark,
bacteria, fungi, fish eggs, body fluids of invertebrates lower vertebrates,
mammalian cell membrane, seaweed and sponges.
Lectins are not directly used in medicines but have following utilities
1. for blood grouping and erythrocytes polyagglutination studies
2. for isolation, purification and structural studies of carbohydrate
containing molecules.
For histochemical studies of normal and pathological conditions.
For mitogenic stimulation of lymphocytes.
Lectin containing natural sources: Abrin (Abrus precatorius),
Concanavalin A (Conovalis ensiformis), Green marine algae (Codium
fragile, Horse gram (Dolichos biflorus) and Red kidney bean (Phaseolus
vulgaris)
