| Physiological effects | |
| Digestion of carbohydrates |
|
| Protein digestion |
|
| Digestion of fat |
|
| Milk sugar digestion |
|
| Cellulose digestion |
|
| Carbohydrate digestion |
|
The pancreatic enzyme amylase is produced in the pancreatic acinar cells and released into the digestive tract. In addition to pancreatic amylase, there is also saliva amylase, which is known as ptyalin. Saliva amylase begins the breakdown of of carbohydrate in the mouth (1). |
| Protein digestion |
|
Peptidases (short for peptide binding hydrolases) are enzymes that can cleave proteins or peptides. They catalyze the hydrolysis of peptide bonds. Peptidases are often referred to as proteases, proteinases or proteolytic enzymes, especially when larger proteins are cleaved. Trypsin is a mixture of three digestive enzymes which decompose proteins in the small intestine and belong to the group of peptidases: Trypsin-1 (cationic trypsin, ~2/3rds), trypsin-2 (anionic trypsin, *~1/3rd) and trypsin-4 (mesotrypsin, just a few percent) (2)(3).
Plant proteases Bromelain (also bromelin) is the name for two enzymes from the family of cysteine proteases. They are obtained from pineapple plant stem and fruit. Papain is found in the green peel and seeds of the unripe papaya fruit. The enzyme has a broad protein splitting effect and belongs to the group of cysteine proteases. Ficin (also known as ficain) is extracted from figs and is an enzyme with a protease effect.
|
| Fat digestion |
| Lipases are enzymes that break down fats ingested with food. This reaction is essential for fat digestion. |
| Lactose digestion |
| Lactase is an enzyme that splits lactose into its component sugars galactose and glucose. Without this chemical reaction, the components of lactose cannot be absorbed through the mucous membrane of the small intestine. |
| Cellulose digestion |
|
Cellulases are enzymes that are able to break down cellulose into its basic building block of β-glucose. Most animals do not produce cellulase and are dependent on exogenous cellulases of their endosymbionts for cellulose degradation. Both ruminants and non-ruminants use endosymbiotic prokaryotes in special stomachs or appendices in order to use the major part of the energy in plant food. Humans do not possess digestive enzymes for the degradation of cellulose. With the help of anaerobic bacteria in the first part of the large intestine, in the appendix and in the ascending colon, part of the cellulose is broken down from the food into short-chain fatty acids. These fatty acids form an important energy substrate for the bacteria living in the intestines. |
| Biological enzyme activity: F.I.P., U.S.P. and ALU |
| Biological activity is key to the therapeutic efficiency of enzymes. This is expressed in F.I.P. units or in U.S.P. units. F.I.P. stands for Fédération International Pharmaceutique, U.S.P. for United States Pharmacopoeia. These units correspond to defined enzyme quantities, which convert 1 µmol of defined substrate in a certain time under standard conditions. For lactase, the activity is expressed in ALU units (Acid Lactase Unit). |
| Laboratory diagnostic measures for the diagnosis of pancreatic insufficiency in digestive disorders |
| The occurrence of fat or protein malabsorption is often used as a criterion for assessing exocrine pancreatic function. However, malabsorption is an inadequate diagnostic tool due to the high reserve capacity of the pancreas. It is generally assumed that severe stool changes occur only after more than 90% of the pancrease is destroyed. Modern laboratory methods allow a much more sensitive diagnosis, which can be used to assess the function of the pancreas. |
| Pancreatic elastase 1 |
|
Since the introduction of the fecal parameter "pancreatic elastase 1", functional disorders of the pancreas have been detected in a significantly higher number of patients than previously found. In particular, symptoms for which no explanation has been established so far can now be better explained using modern stool diagnostics. The quantitative detection of pancreatic elastase 1 can reliably diagnose or rule out exocrine pancreatic insufficiency. The enzyme, which is produced in the acinar cells of the exocrine pancreas, enters the duodenum together with other pancreatic enzymes (amylase, lipase, trypsin). Elastase 1 survives the intestinal passage undamaged and can be easily detected in the stool using immunological methods. The concentration of elastase 1 in the stool reflects the secretion capacity of the exocrine pancreas. In contrast to chymotrypsin determination (an alternative parameter used in pancreas diagnostics), only a single stool sample is required. Since the detection of elastase 1 is not affected by replacement therapy, it is well suited for monitoring the course of chronic exocrine pancreatic insufficiency (4). |
| Reference values for pancreatic elastase 1 |
|
Standard value for adults and children from the 1st month of life: > 200 µg/g stool |
| Effect | Indication | Dosage |
| Physiological effects at a low intake |
In case of upper abdominal syndromes and dyspeptic complaints caused by digestive weakness, especially in elderly patients |
Amylase: >14000 U/d Protease: >3500 R/d Lactase: >2000 rpm Lipase: >500 U/d Cellulase: >100 rpm/d |
| General mode of administration | |
| When |
Digestive enzymes should be taken immediately before meals to support digestive performance. |
| Side effects | |
| No side effects are known to date. | |
| Contraindications | |
| No contraindications are known to date. | |
| Drug interactions | |
| None | No interactions are known to date. |
| Nutrient interactions | |
| None | No interactions are known to date. |
| Referenzen |
|
1) Biesalski, H. C. et al. Ernährungsmedizin: Nach dem Curriculum Ernährungsmedizin der Bundesärztekammer und der DGE, 4. Auflage. Stuttgart: Georg Thieme Verlag KG, 2010. |
