Dipep
Dipep Uses, Dosage, Side Effects, Food Interaction and all others data.
Papain, also known as papaya proteinase I, is a cysteine protease (EC 3.4.22.2) enzyme that is found in species of papaya, Carica papaya and Vasconcellea cundinamarcensis. The enzyme is found to be localized in the skin of papaya, and is collected from slashed unripe papayas as a crude latex. Papain is used in food, pharmaceutical, textile, and cosmetic industries. While it has been used for the treatment of inflammation and pain via topical administration, papain has also shown to have anthelmintic and tooth-whitening properties. Present in over-the-counter mixture products consisting of different digestive enzymes, its active site contains a catalytic diad that plays a role in breaking peptide bonds. Papain is also used as an ingredient in various enzymatic debriding preparations.
Papain is a digestive enzyme and often acts as a skin allergen.
Pepsin is a potent enzyme in gastric juice that digests proteins such as those in meat, eggs, seeds, and dairy products .
Studies on gastric digestion from 1820-1840 led to the discovery of pepsin as the substance which, in the presence of stomach acid, causes nutrients including meat or coagulated egg whites to dissolve. Soon afterward, it was shown that these protein nutrients were cleaved by pepsin to products called peptones .
Pepsin is often used as a replacement enzyme for those with pancreatic insufficiency . Stimulation of the pancreas and therefore enzymatic digestion of food is a tightly controlled and is a hormonally mediated process. Any changes or conditions affecting metabolic steps for successful digestion and absorption negatively affect pancreatic enzymatic secretion, entry into the intestine, functionality once inside the intestine, and appropriate mixing with foods/nutrients. Many causes of pancreatic insufficiency require that enzyme replacement therapy is started, including cystic fibrosis, pancreatic cancer, acute and chronic pancreatitis, as well as pancreatic surgery .
Trade Name | Dipep |
Generic | Pepsin + Papain + Lipase + Fungal Diastase + Cellulase |
Weight | 25mg, 50mg |
Type | Capsule, Suspension |
Therapeutic Class | |
Manufacturer | Serum Institute Of India Private Limited |
Available Country | India |
Last Updated: | September 19, 2023 at 7:00 am |
Uses
Papain is a proteolytic enzyme derived from papaya used for its anti-inflammatory properties.
No FDA-approved therapeutic indications.
Pepsin is a protease indicated in the treatment of digestive disorders.
Used as a pancreatic enzyme replacement in pancreatic insufficiency . It is intended to mimic naturally produced human pepsin .
Pepsin powder is prepared from the gastric mucosa of pigs, cattle or sheep . In the laboratory, it is primarily used for the unspecific hydrolysis of proteins and peptides in acidic media. In addition, it provides limited hydrolysis of native immunoglobulins, yielding biologically active fragments .
In certain supplements, pepsin may be combined with betaine and HCl (hydrochloric acid) to aid in digestion in various gastrointestinal conditions , .
Dipep is also used to associated treatment for these conditions: InflammationDiarrhoea, Gastritis Chronic, Hypochlorhydria, Postoperative digestive insufficiency
How Dipep works
When topically applied, papain induces an allergen-like inflammatory response via recruiting neutrophils, mast cells, and CD3-positive cells and by induction of a TH2-biased antibody response . In vitro, treatment of papain resulted in the breakdown of tight junctions of primary human keratinocytes that maintain the epithelial barrier integrity. These tight junction proteins include zonula occludens-1, claudin-4, and occludin . It is proposed that papain induces allergic responses via activation of TLR4, leading to an increase in neutrophils, CD3+ cells, mast cells, and CCL8-positive cells .
Glands present in the mucous membrane lining of the stomach produce and store an inactive protein named pepsinogen. Impulses from the vagus nerve and the hormonal secretions of the hormones gastrin and secretin promote the release of pepsinogen into the stomach, where it is mixed with hydrochloric acid and quickly converted to the active enzyme pepsin. The digestive potency of pepsin is highest at the acidic pH of normal gastric juice. In the intestine, the gastric acids are then neutralized, and pepsin is no longer effective .
Pepsin, the proteolytic enzyme of the stomach is normally responsible for less than 20% of the protein digestion occuring the gastrointestinal tract. It is an endopeptidase enzyme that metabolizes proteins to peptides. It preferentially hydrolyzes peptide linkages where one of the amino acids is aromatic. Pepsin, like other protease enzymes, is produced from an inactive precursor, pepsinogen, which is stored in granule form in the chief cells of the stomach and are released by a process called exocytosis .
In the digestive tract, pepsin activity only contributes to the partial breakdown 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 .
Toxicity
Acute oral LD50 of 200 mcu papain is 4000 mg/kg in rat and 12500 mg/kg in mouse . It acts as an irritant in case of inhalation or contact with eyes.
Oral LD50 Rat 90000 mg/kg
Chronic backflow of pepsin, acid, and other substances from the stomach into the esophagus, is the basis of reflux conditions, particularly gastroesophageal reflux disease (GERD) and laryngopharyngeal reflux. In the latter, pepsin and acid travel all the way up to the larynx, where they can lead to damage of the laryngeal mucosa and lead to symptoms ranging from hoarseness of the voice and chronic cough to laryngospasm (involuntary contraction of the vocal cords) as well as laryngeal cancer .
Though limited data is available on the toxicity of exogenous pepsin (not naturally produced in one's gastrointestinal tract), it can be extrapolated from the above-mentioned information that pepsin overdose may lead to mucosal tissue damage of the gastrointestinal tract.
Volume of Distribution
No pharmacokinetic data available.
Elimination Route
No pharmacokinetic data available.
Half Life
No pharmacokinetic data available.
Clearance
No pharmacokinetic data available.
Elimination Route
No pharmacokinetic data available.
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