ENZYMES
&
PROTEIN
DRUGS
Content
1.
2.
3.
4.
5.
6.
7.
8.

Introduction
Papain
Bromelain
Malt extract
Serratiopeptidase
Urokinase
Streptokinase
Peps...
Introduction
Enzyme:

which are proteins which acts as
biological catalysts.
Play vital role in the function of cells an...
1. Papain
 Source:

mixture of proteolytic enzymes obtained from the
latex of unripe fruit of tropical melon tree Carica ...
 Description:
 Available

as light brown or white colored amorphous powder with
typical odor and taste.
 It shows maxim...
2. Bromelain
 Source:

mixture of proteolytic enzymes obtained from the
stem and ripen fruits of pineapple plant Ananas c...
3. Malt Extract
 Source:

obtained by extracting malt or malted barley, which is
partially and artificially germinated gr...
4. Serratiopeptidase










Source: proteolytic enzyme obtained from bacteria belonging to genus
Serratia, pres...
5. Urokinase
It

is an enzyme produced by kidney and
obtained from human urine or kidney tissue
cultures.
It is lyophili...
6. Streptokinase
 It

is an enzyme obtained from cultures filtrates of beta
hemolytic, streptococci group C. This enzyme ...
7. Pepsin











It is a substance containing proteolytic enzyme and is present in the
gastric juice of animals...
8. Lectins













They are proteins or glycoproteins without an immune origin.
They can agglutinate the ce...
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Enzymes of Natural Origin

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Enzymes of Natural Origin

  1. 1. ENZYMES & PROTEIN DRUGS
  2. 2. Content 1. 2. 3. 4. 5. 6. 7. 8. Introduction Papain Bromelain Malt extract Serratiopeptidase Urokinase Streptokinase Pepsin
  3. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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)

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