What kind of pancreatin available?
What is Pancreatin ?
What is the application ?
What kind of pancreatin available?
Product | Product code | Quality |
Pancreatin USP |
XS-PAN-USP-1A | 1 X USP powder |
XS-PAN-USP-2A | 2 X USP powder | |
XS-PAN-USP-3A | 3 X USP powder | |
XS-PAN-USP-4A | 4 X USP powder | |
XS-PAN-USP-4B | 4 X USP granular | |
XS-PAN-USP-5A | 5 X USP powder | |
XS-PAN-USP-5B | 5 X USP granular | |
XS-PAN-USP-6A | 6 X USP powder | |
XS-PAN-USP-6B | 6 X USP granular | |
XS-PAN-USP-7A | 7 X USP powder | |
XS-PAN-USP-7B | 7 X USP granular | |
XS-PAN-USP-8A | 8 X USP powder | |
XS-PAN-USP-8B | 8 X USP granular | |
XS-PAN-USP-HIA | Higher power powder | |
XS-PAN-USP-HIB | Higher power granular | |
Pancreas powder EP |
XS-PAN-EP-1A | 1 X Ph. Eur. powder |
XS-PAN-EP-1B | 1 X Ph. Eur.granular | |
XS-PAN-EP-2A | 2 X Ph. Eur. powder | |
XS-PAN-EP-2B | 2 X Ph. Eur.granular | |
XS-PAN-EP-3A | 3 X Ph. Eur. powder | |
XS-PAN-EP-3B | 3 X Ph. Eur.granular | |
XS-PAN-EP-HIA | Higher power powder | |
XS-PAN-EP-HIB | Higher power granular | |
Pancreatin BP | XS-PAN-BP-1A | powder |
XS-PAN-BP-1B | granular | |
Pancreatin JP | XS-PAN-JP-1A | powder |
XS-PAN-JP-1B | granular | |
Pancreatin CP | XS-PAN-CP-1A | powder |
XS-PAN-CP-1B | granular | |
Amylase | XS-AMY-USP-200A | 200 powder |
Technical Data Sheet | ||
Lipase | XS-LIP-USP-8A | 8 powder |
XS-LIP-USP-16A | 16 powder | |
XS-LIP-USP-24A | 24 powder | |
XS-LIP-USP-30A | 30 powder | |
Technical Data Sheet | ||
Pancrelipase | XS-PANLIP-USP-A | USP powder |
What is Pancreatin ?
Pancreatin is the name of an extract from porcine pancreas.
CAS-No. 8049-47-6
The pancreas is a gland with a small endocrine part (Islets of Langerhans), and a large exocrine part. The Islets of Langerhans secrete insulin and glucagon, whilst the cells of the exocrine part produce various hydrolytic enzymes most of which have digestive functions. Upon synthesis, the proteins are deposited in granules, either as active enzymes or as inactive precursors (zymogens). When the secretion is induced, the contents of the granules are released into a system of ducts and finally reach the duodenum where the zymogens are being transformed into active enzymes.
The pancreatic enzymes can be classified in four groups:
Pancreatin contains many of these enzymes. The quality of any Pancreatin preparation is defined by three enzyme activities, Protease, Amylase and Lipase. The pharmacopoeias specify minimum activity levels (in units per mg) for each of these three enzymes in Pancreatin. In both absolute and relative terms, the activities of these enzymes vary with, and depend upon, the origin of the pancreas and the treatment of the glands. Porcine pancreas is preferred for the industrial manufacture of Pancreatin for the following reasons:
Pancreas proteases
The pancreas contains a mixture of endo- and exopeptidases. Trypsin (EC 3.4.21.4), Chymotrypsin (EC 3.4.21.1) and Elastase (EC 3.4.21.36) are specific endopeptidases which cleave peptide bonds preferentially at the carboxyl end of basic, aromatic and aliphatic L-amino acids, respectively. Carboxypeptidase A (EC 3.4.17.1) and Carboxypeptidase B (EC 3.4.17.2) are exopeptidases which cleave L-amino acids from the free carboxyl terminus of peptides with a preference for C-terminal hydrophobic and basic amino acids, respectively.
This broad spectrum of specificities has two important implications. Physiologically, it provides an efficient tool for the degradation of proteinaceous food components into resorbable fragments. Biochemically, in any assay for Protease activity in Pancreatin only a protein substrate, e.g. casein, can supply a sufficient range of susceptible bonds for all Proteases present. In the assay, the protein substrate should be denatured prior to use because Trypsin and Chymotrypsin which together contribute the most abundant part of the endopeptidases in Pancreatin both display a preference for unfolded proteins.
In Pancreatin the major amount of each proteolytic enzyme is present as the corresponding Zymogen, i.e. as Trypsinogen, Chymotrypsinogen, procarboxypeptidase A, procarboxypeptidase B, and proelastase. Therefore an assay performed with Pancreatin as such will simply determine any free Protease activity. The total Protease activity can only be measured after preincubation of a Pancreatin solution with an activating compound. Enterokinase is routinely used for this purpose. This enzyme renders Trypsin active and thus triggers the activation of the other zymogens.
The catalytic optima of the pancreas proteases are in good agreement with the physiological requirements, i.e. about 37 °C and between pH 7 and 9. Due to the nature of the enzymes a Pancreatin solution is not very stable under these conditions because autolytic and proteolytic degradation of the enzymes takes place. Calcium ions increase the activity and stabilize Trypsin against the autolytic attack. The same holds true for Chymotrypsin though the stabilizing effect of calcium is less pronounced than with Trypsin (1).
Pancreas Lipase
Pancreatic Lipase (EC 3.1.1.3) can be characterized both by its ability to liberate fatty acids from emulsified long-chain triglycerides and by its action at the oil-water interface (2, 3). Like other esterases, pancreatic Lipase has a low substrate specificity. The Enzyme hydrolyzes not only tri-, di- and monoglycerides but also esters of n-alcohols and fatty acids with short to long carbon chains. The rate of hydrolysis decreases in the order tri-, di- and monoglyceride (1, 3, 4). The reaction velocity also decreases with increasing fatty acid chain lengths of triglycerides, that is e.g. from tributyrin to triolein.
On the other hand, in the same order triglycerides become more specific substrates (2). Therefore triolein (or olive oil as its natural substitute) is used as a substrate in most of the assays on pancreatic Lipase.
Several factors are known to affect the activity of pancreatic Lipase. Since pancreatic Lipase acts at the oil-water interface, the reaction rate depends on the surface area of the substrate and thus on the degree of emulsification (3). Bile salts promote emulsification and they are therefore used - together with gum arabic - for the preparation of stable substrate emulsions. Colipase, a small protein (molecular weight approx. 10,000), is a specific cofactor of Pancreatin Lipase. It is synthesized and secreted by the Pancreas and serves to anchor pancreatic Lipase on the substrate surface in the presence of bile acids or other amphipaths like proteins and fatty acids (2). Sodium chloride is absolutely required for and increases the activity of pancreatic Lipase (1). Calcium ions improve the thermal stability of pancreatic Lipase and also enhance the activity of the enzyme (3). Pancreatic Lipase is active in the range of pH 6.5 to 9.0 (1).
Pancreas Amylase
a-Amylase (EC 3.2.1.1; 1,4-a-D-glucan Glucanohydrolase) hydrolyzes 1,4-a-D-glucosidic linkages in polysaccharides containing 3 or more 1,4-a-linked D-glucose units (5). The enzyme from porcine pancreas is composed of 2 subunits and has a molecular weight of 50,000 (6).
Three types of amylases can be distinguished:
a-Amylase is an endoamylase which is found in all living organisms. a-Amylase acts in a random fashion by a multiple-attack mechanism on starch, glycogen and related polysaccharides and oligosaccharides ultimately yielding glucose and maltose as well as larger oligosaccharides. Reducing groups are in the a-configuration. The Enzyme cannot hydrolyze 1,6-a-bonds in glycogen and amylopectin, but it is able to bypass these branch points (1, 5).
ß-Amylase and g-Amylase are exoamylases which are exclusively found in plants and microorganisms.
ß-Amylase (EC 3.2.1.2; 1,4-a-D-glucan maltohydrolase) can neither hydrolyze 1,6-a-bonds nor bypass these branch points. This enzyme acts on the same substrates as a-Amylase but it removes successive maltose units from the non-reducing end; by inversion the maltose units released are in the ß-configuration (5).
γ-Amylase (EC 3.2.1.3; 1,4-a-D-glucan Glucohydrolase) releases ß-D-glucose successively from the non-reducing end of the polysaccharide chains (5).
What is the application ?
Applications/Uses:
* Nutritional formulas (tablets/capsules/powders) as a digestive aid
* Food/Cheese manufacturing
* Hydrolysis of proteins,carbohydrates or fats
* Animal Health formulas as a digestive aid
* Leather hides preparation
* Meat tenderizing formulas