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Pancreatin
[CAS# 8049-47-6]

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Complete supplier list of Pancreatin
Identification
Classification Biochemical >> Enzymes and coenzymes
Name Pancreatin
CAS Registry Number 8049-47-6
EC Number 232-468-9
Safety Data
Hazard Symbols symbol symbol   GHS07;GHS08 Danger    Details
Hazard Statements H315-H317-H319-H334-H335    Details
Precautionary Statements P261-P264-P271-P280-P302+P352-P305+P351+P338    Details
Hazard Classification
up    Details
HazardClassCategory CodeHazard Statement
Respiratory sensitizationResp. Sens.1H334
Skin irritationSkin Irrit.2H315
Eye irritationEye Irrit.2H319
Skin sensitizationSkin Sens.1H317
Specific target organ toxicity - single exposureSTOT SE3H335
SDS Available
up Discovory and Applicatios
Pancreatin is a mixture of digestive enzymes produced by the exocrine portion of the pancreas. It primarily contains amylase, lipase, and protease, which collectively facilitate the digestion of carbohydrates, fats, and proteins, respectively. The compound is derived from porcine or bovine pancreas through extraction and purification processes that preserve enzymatic activity. Pancreatin has been known for over a century and was first isolated as researchers studied the digestive function of the pancreas. Early studies demonstrated that pancreatic extracts could hydrolyze dietary macromolecules, establishing the foundation for its therapeutic applications in enzyme replacement therapy.

The production of pancreatin involves homogenization of pancreatic tissue, followed by stabilization and drying under controlled conditions to yield a powder or granular preparation. Standardization ensures that each batch contains a defined enzymatic activity, expressed in units specific to each enzyme type. Modern preparations may include enteric coating or microencapsulation to protect enzymes from gastric acid and to ensure release in the small intestine, where digestion occurs. Quality control measures focus on activity retention, absence of contaminants, and consistent performance in hydrolyzing specific substrates.

Pancreatin is primarily used as a pharmaceutical preparation to treat exocrine pancreatic insufficiency, a condition in which the pancreas fails to produce sufficient digestive enzymes. This insufficiency can result from chronic pancreatitis, cystic fibrosis, pancreatic surgery, or other pancreatic disorders. By supplementing the deficient enzymes, pancreatin facilitates the breakdown and absorption of nutrients, alleviating symptoms such as steatorrhea, malnutrition, and weight loss. It is administered orally, often in capsule or tablet form, and dosing is adjusted according to the severity of enzyme deficiency and the composition of meals.

Beyond clinical enzyme replacement, pancreatin has been employed in biochemical research and industrial applications. Its proteases, amylases, and lipases are used in studies of protein digestion, carbohydrate hydrolysis, and lipid metabolism. In laboratory assays, pancreatin serves as a convenient source of mixed enzymes to mimic digestive conditions or to hydrolyze substrates under controlled conditions. Industrially, similar enzyme preparations have been used in food processing to modify starches, proteins, and fats, although pharmaceutical-grade pancreatin is primarily reserved for therapeutic use.

The pharmacological effectiveness of pancreatin depends on the stability of its enzymes and their ability to function in the small intestine. The inclusion of lipase is particularly critical because fat digestion is most susceptible to deficiency in exocrine pancreatic disorders. Enteric-coated formulations protect lipase and other enzymes from gastric acid degradation, enhancing bioavailability. The activity of proteases and amylases contributes to protein and carbohydrate digestion, respectively, and supplementation improves overall nutrient absorption. Clinically, enzyme activity is often monitored and adjusted to achieve optimal nutritional outcomes and minimize gastrointestinal discomfort.

Pancreatin preparations are generally well-tolerated, with minimal adverse effects when dosed appropriately. Side effects can include gastrointestinal discomfort, such as bloating or mild diarrhea, particularly if enzyme activity exceeds the patient’s digestive needs. In rare cases, hypersensitivity reactions may occur, especially in individuals with allergies to porcine or bovine proteins. Regulatory oversight ensures that commercial preparations meet stringent standards for purity, potency, and safety.

In addition to therapeutic and research applications, pancreatin has contributed to understanding human digestive physiology. Studies using pancreatin as a model for pancreatic secretion have provided insights into enzyme-substrate specificity, pH-dependent activity, and the kinetics of macronutrient hydrolysis. These investigations have informed dietary recommendations, the development of enzyme supplements, and strategies to manage digestive disorders.

Overall, pancreatin is a clinically and scientifically important preparation of pancreatic enzymes that supports digestion in individuals with enzyme insufficiency and serves as a tool in biochemical research. Its combination of amylase, lipase, and protease activities enables comprehensive digestion of carbohydrates, fats, and proteins, making it a cornerstone in the management of exocrine pancreatic disorders and in studies of human and animal digestive processes.

References

1976. Transfer RNA methyltransferase activity in Paramecium aurelia. Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 447(2).
DOI: 10.1016/0005-2787(76)90260-4
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