ENZYMES A protein with catalytic properties due to its power of specific activation Enzymes are biological catalysts.
Important ENZYMES amylolytic enzymes Lipolytic enzyme Proteolytic enzymes Oxidizing enzymes
Amylolytic ENZYMES DIASTASE and AMYLASE Salivary Diastase or Pty a lin Pancreatic diastase or amylopsin Malt diastase starch to maltose Invertase or sucrase sucrose to glucose & fructose Maltase maltose to glucose
Zymase monosaccharides to CO2 and alcohol Emulsin or ß glucosidase amygdalin to glucose, HCN and benzaldehyde Myrosin ase Sinalbin, Sinigrin and other glycoside
P r oteolytic enzymes Pepsin Proteins into proteoses & Peptons Trypsin proteoses & Peptons to polpeptides and amino acids Erepsin proteoses & Peptons to amino acids Rennin Curdles soluble casein of milk Papain meat tenderize proteoses & Peptons to polpeptides and amino acids
OXIDIZING Enzymes Peroxidases Oxidation reaction Thrombin Fibrinogen to Fibrin Zymase Monosaccharide spliting enzyme but works by oxidation
Phytoenzymes Malt Bromelain Papain
MALT EXTRACT BARLEY is dried grain of Botanical source : Hordeum vulgare Family : Graminae Cultivated through out the world wherever climate is favourable Malt or Malted Barley Dried, artificially germinated barley grain Grains kept wet with water in warm room germinate till caulicle protrudes dried quickly
Malt extract Extracting malt with hot water at 60C. Concentracted at 60C under pressure Malt extract is mixed with 10% glycerine It contains dextrin, maltose, glucose and amylolytic enzyme Starch soluble sugars
Dry malt resembles barley & has agreeable odour and sweet taste Contains sugar maltose 50-70% Dextrins 2-15% Proteins 8% Diastase and peptase emzyme Used in Brewing & alcohol industries
Uses Malt extract is used as easily digested nutritive and as an aid in starch digestion. 15g Diastase 50times starch sugars Lactase converts lactose galactose and glucose. It is used in pt having lactose intolerance
Papain Phytoenzyme Biological source Dried and purified latex of the unripe mature fruit of Carica papaya F amily : Caricaceae
Collection procedure The epicarp of the fruit adheres to the orange colour, fleshy sarcocarp, which surrounds the central cavity. Cavity contains a mass of nearly black seeds Full grown but unripe fruits are subjected to shallow incisions on the 4 sides. Latex flow for few seconds and then soon coagulates Latex is then collected
After collection coagulated lumps are shredded and dried by sun or by artificial heat Incisions & collections are made at weekly intervals as long as the fruit exudes the latex .
Potassium meta bisulphite is added in latex collected in trays as preservative. After this latex passed through sieve to remove unwanted material. After sieving dry latex in sun light or through artificial drying. The dry latex is called crude papain. Later methods yield better grades of crude papain Crude papain is purified by dissolving in distilled water and then precipitating with alcohol
Characteristics White or greyish white color Hygroscopic nature Soluble in water and glycerol Insoluble in organic solvents Best grade of papain can digest 300 times of its own weight of egg albumin Also function in neutral and alkaline media
Chemical Constituents Several proteolytic enzymes Peptidase 1 Renin like enzyme Clotting enzyme Amylolytic enzyme Referred as ‘vegetable pepsin’’ because it contain enzyme similar to that of Pepsin. However unlike Pepsin, Papain acts in acid, neutral and alkaline media . Crystalline papain most soluble at PH 5-7
Contain nitrogen and Sulphur containing protein It is protein of one folded polypeptide chain of 212 amino acids
Actions and uses of Papain Anti-inflammatory and wound healing property. Used as digestive aid Dyspepsia, edema Along with antibiotic to treat disease It is used as meat tenderizer It is used extensively in tenderization of beef
Used to relieve the symptoms of episiotomy Commercially: used to tenderize meat. Clearification of beverages Substitue of rennet, ( in cheese manufacturing as substitute of rennet) Used in textile industry Brewing industry In cosmetics industry.
Brom e l a in Syn : Stem Bromelain, Pineapple stem bromelain B.S.: it is proteolytic enzyme obtained from the stem & ripened fruit of Pineapple plant . Ananas comosus Family: Bromiliaceae Description: Odour : odourless Color : Buff colored powder Taste : Acrid
Preparation Fresh stem & fruits were collected, washed with H2O2 sol. , peeled off, cut into small pieces. Juice is collected from fresh pineapple fruit and cooled. It is then filter to remove solid particles. it is then centrifuged and solid particles settled down. Supernatatnt liquid collected and cold acetone added. Bromelain ppts by action of acetone. Again cetntrifugation bromelain ppts settled down and collected. It is then purified.
Characteristics The optimum pH of bromelain is 5.0–8.0. In solution pH below 3.0 and above 9.5 inactivates the enzyme. The optimum temperature is between 50 and 60°C, still it is effective between 20 and 65°C too. The moisture content should not exceed 6%. It is obtained in light yellow colour powder . Soluble in water Insoluble in alcohol and chloroform
Chemical Constituents Bromelain is not a single substance, but rather a collection of enzymes and 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 : ability to dissolve fibrin, reversible inhibition of platelet aggregation and relieve from blood coagulation diseases. Antithrombotic : prevention in treatment of thrombosis and thrombophlebitis ( inflammation of vein caused by blood clot). Anti-inflammatory: soft tissue inflammation and in case of edema caused by surgery and injury. Digestive enzyme : used successfully as a digestive enzyme following pancreatectomy , in cases of exocrine pancreas insufficiency and in other intestinal disorders.
Antibiotic potentiation is one of the primary uses of bromelain in several foreign countries ; it can modify the permeability of organs and tissues to different drugs. The potentiation of antibiotics and other medicines by bromelain may be due to enhanced absorption , as well as increased permeability of the diseased tissue which enhances the access of the antibiotic to the site of the infection . Cosmetics: as an active ingredient in tooth whitening dentrifrices , and skin products to treat acne, wrinkles and dry skin. In cleansing agents and facial cleansers.
bromelain prevents or minimizes the severity of angina pectoris and transcient ischemic attacks (TIA ). also exerts an antihypertensive effect in experimental animals. It may even be useful in the treatment of AIDS to stop the spread of HIV . Widely used in leather factory
Pepsin Animal enzyme Proteolytic enzyme Biological source Enzyme obtained from the glandular layer of the fresh stomach of various animals like Pig, sheep or calf. Commonly from pig, Sus scrofa ( suidae ) Ovis aries ( Bovidae )
Preparation of pepsin Pepsin is prepared by using stomach linings The mucous membrane is separated from the stomach by the process of stripping or it is scrapped off Then it is placed in acidified water for autolysis at 37ºC for 2 hours The liquid so obtained consists of both pepsin and peptone
It is then filtered and sodium or ammonium salts are added to the liquid till it is half saturated At this point only the pepsin separates out in the form of precipitates, and the peptone remains in solution The precipitates are collected and subjected to dialysis for the separation of salts Remaining amount of pepsin if any in the aqueous solution is precipitated by the addition of alcohol into it.
Concentrated solution containing precipitates, is poured on glass plates to dry forming Scale pepsin Or concentrated solution is carefully evaporated in vacuum forming spongy pepsin
Description of enzyme Pepsin is lustrous, transparent or translucent scales or occurs as granular or spongy masses. Colour ranges between light yellow to light brown or as fine white or cream coloured amorphous powder It is free from offensive odour and has a slightly acid or saline taste. It show optimal activity at a pH 1.8 to 3.5 Reversibly inactive at pH 7 to 8
Pepsin best act at a temperature 40ºC and pH 2-4 Pepsin denatured at 70ºC and in the presence of alcohol. Pepsin can be stored at 2-8ºC for about 1-2 years
Uses pepsin is used in deficiency of gastric secretion Pepsin is administered to assist digestive digestion in combination with pancreatin. It is proteolytic enzyme is administered after meals and followed by a dose of hydrochloric acid, its Usual dose is 500mg It is used in laboratory analysis of various proteins. It is used in preparation of cheese and other protein containing food
Pancreatin Animal enzyme Pancreatin is a mixture of several digestive enzymes. It is composed of Amylase (hydrolyses starches to oligo & disaccharides maltose) Lipase (hydrolyses fats to fatty acids and glycerols) Trypsin ( hydrolyses proteins to oligopeptides)
Biological source Pancreatin is produced by the exocrine cells of the pancreas of Pig or Hog, Sus scrofa Family Suidae or from Pancreas of Ox or calf Bos taurus Family Bovidae
Preparation method The Pancreas is a gland that lies directly inside the posterior wall of the abdomen. Fresh glands are minced and extracted by similar methods as employed in the manufacture of Pepsin
Properties It show optimal activity in neutral or faintly alkaline solution More than traces of mineral acids or large amounts of alkali hydroxide render pancreatin inert, and excess of alkali carbonates inhibits its action
Pancreatin – uses Pancreatin is a mixture of several digestive enzymes. This mixture is used to treat conditions in which pancreatic secretions are deficient, such as surgical pancreatectomy, pancreatitis and cystic fibrosis. Enteric coated granules are used to treat infants with celiac disease and related pancreatic deficiencies,. Usual dose is 325mg – 1g as tablets, capsules or granules
Routine cancer eradication As is mixture of enzymes but proteolytic enzyme play role in cancer eradication Effected by protein rich foods at inappropriate time or in excessive amount Body need 12 hrs time free of protein consumption for proper working of this defen s e system
Pancreatin become inactive in acid or with alcohol contact cancer continuously produce acids Many cosmetic contain acid or alcohol special concern with the skin cancer
Biological source It is produced by the exocrine cells of the pancreas of Pig or Hog, Sus scrofa Family Suidae or from Pancreas of Ox or calf Bos taurus Family Bovidae Pancrelipase
Uses Employed as digestive aid It increase intestinal absorption of fat used to treat steatorrhea Usual dose is 8000 to 24000 USP units Dose is determined on the basis of clinical evaluation according to pancreatic insufficiency
Ren n in Animal enzyme Protease enzyme Milk curdling enzyme Biological source Rennin is partially purified enzyme obtained from the glandular layer of the stomach of the calf, Bos taurus Family : Bovidae
Preparation method Rennin is prepared by macerating the minced glandular layer of the digestive stomach of the calf in 0.5% sodium chloride solution. Filtration is then carried out Filtrate is acidified with hydrochloric acid Then saturation is carried out with sodium chloride Which precipitates the Rennin Rennin is then separated and dried and powdered
Standard Rennin Rennin occur as a yellowish white powder or as yellowish grains or scales It has characteristic and slightly saline taste It has peculiar odour Standard Rennin can coagulate approximately 25000 times its own weight of fresh cow’s milk
Uses Rennin is used to coagulate milk, thus rendering it more digestible for convalescents It is ingredient in Rennin and pepsin elixir called pepsin essence . Protease enzyme that curdles the casein in milk, helping young mammals digest their mothers' milk. Its principal used is in the manufacture of cheese, mainly for coagulation of milk
Used to separate milk into solid curds used for cheese making and liquid whey