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CAS 8049-47-6 Digestive Enzyme Complex Digestive Enzyme Complex GMP Grade USP Grade EP Grade NF Grade

Pancreatin

IUPAC: Pancreatic Enzyme Complex (Amylase, Lipase, Protease) View on PubChem
CAS NUMBER
8049-47-6
MOL. FORMULA
N/A
MOL. WEIGHT
N/A
Scientific Overview

Pancreatin's three core enzyme classes each target a distinct macronutrient: amylase hydrolyzes starches into soluble carbohydrates, lipase breaks down dietary triglycerides into monoglycerides and free fatty acids, and protease (trypsin/chymotrypsin) cleaves proteins into peptides and amino acids. Unlike small-molecule APIs, pancreatin's potency is defined and standardized by enzymatic activity units (USP/Ph. Eur.) rather than molecular weight, since it is a complex, multi-component biological extract rather than a single defined chemical entity.

Pancreatin is a biologically derived mixture of digestive enzymes obtained from porcine (or bovine) pancreas, principally composed of amylase, lipase, and protease (trypsin, chymotrypsin, carboxypeptidase), along with ribonuclease. It is a critical active ingredient in pancreatic enzyme replacement therapy (PERT) for patients with exocrine pancreatic insufficiency.

Full Technical Data
Chemical Name Pancreatin (Pancreatic Extract)
CAS Number 8049-47-6
IUPAC Name Pancreatic Enzyme Complex (Amylase, Lipase, Protease)
Molecular Formula N/A
Molecular Weight N/A
Reaction Scheme
Fresh Porcine (or Bovine) Pancreas
NA
NA
Pancreatin
NA
Commercial Applications

Pancreatic Enzyme Replacement Therapy (PERT)

Core active ingredient in prescription enzyme supplements for exocrine pancreatic insufficiency (e.g., cystic fibrosis, chronic pancreatitis).

In Vitro Digestibility Testing

Used in food science and nutrition research to simulate gastrointestinal digestion of starches, proteins, and fats.

Nutraceutical & Dietary Supplement Manufacturing

Formulated into digestive support supplements aiding general food breakdown and nutrient absorption.

Industrial & Leather/Textile Processing

Applied historically in leather bating and textile desizing processes due to its proteolytic and amylolytic activity.

Market Therapeutic Focus
DIGESTIVE ENZYME COMPLEX PHARMACEUTICAL MANUFACTURING GASTROENTEROLOGY / PERT THERAPEUTICS NUTRACEUTICALS & DIETARY SUPPLEMENTS FOOD SCIENCE R&D CRO/CDMO
Scientific Literature

Pancreatic Enzyme Replacement Therapy: A Review

Authors: Domínguez-Muñoz, J.E.

World J. Gastroenterol.

Pancreatin in the Treatment of Exocrine Pancreatic Insufficiency

Authors: Layer, P.; Keller, J.

Best Pract. Res. Clin. Gastroenterol.

Standardization of Pancreatic Enzyme Preparations

Authors: Scharpé, S. et al.

Clin. Chem. (reference to unit conversion methodology)

Peer Queries & FAQs
Why is pancreatin's potency measured in units rather than molecular weight?
As a multi-enzyme biological extract rather than a single defined molecule, its potency is standardized by measurable enzymatic activity (amylase, lipase, protease units) per USP/Ph. Eur. assay methods, not by molecular weight.
What is the difference between pancreatin and pancrelipase?
Pancrelipase is a more purified, higher-potency, and specifically lipase-standardized form of pancreatin used in prescription PERT products, while pancreatin refers to the broader extract with a lower minimum activity specification.
What conditions inactivate pancreatin's enzymes?
Excessive acid or alkaline conditions render the enzymes inert, which is why enteric-coated formulations are commonly used to protect activity through gastric transit before release in the intestine.
What is the recommended storage condition?
Store in a tightly sealed, moisture-protected container under refrigeration (2--8°C) to preserve enzymatic activity, as pancreatin is temperature- and humidity-sensitive.

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