Pankreasenzyme

Pankreasenzyme, or pancreatic enzymes, are digestive enzymes produced by the exocrine pancreas. They are synthesized by pancreatic acinar cells as inactive zymogens and released into the duodenum via the main pancreatic duct. In the small intestine, these enzymes are activated to digest proteins, carbohydrates, fats, and nucleic acids. The pancreatic juice is typically alkaline, aiding digestion.

Major pancreatic enzymes include proteases such as trypsin, chymotrypsin, and carboxypeptidases that break down proteins; amylase that cleaves starches; and lipase, which digests fats. Lipase activity is enhanced by colipase and requires bile acids for optimal function. Nucleases such as RNase and DNase may also be present in pancreatic juice.

Secretion is regulated by hormonal and neural signals. Cholecystokinin stimulates enzyme-rich secretion, while secretin promotes bicarbonate-rich fluid to neutralize gastric acid in the duodenum. The alkaline environment helps optimize enzyme activity and protect mucosa during digestion.

Clinically, impairment of pancreatic exocrine function leads to malabsorption and steatorrhea, known as exocrine pancreatic insufficiency. Acute or chronic pancreatitis can reduce enzyme output. Enzyme replacement therapy provides pancreatic enzymes with meals to improve digestion in affected individuals.

The term Pankreasenzyme refers to pancreatic enzymes in German-language context; in English, the term is pancreatic enzymes or exocrine pancreatic enzymes.