Thulitera asks a single, narrowly framed question: where calcium ions are involved in the structure of the pancreas’s digestive enzymes — together with the complete wording of the EU-authorized claim.
Step Into the GuideEach day, the pancreas releases a whole series of proteins into the small intestine, where they break complex food components down into smaller building blocks. For such a protein to work catalytically at all, its chain of amino acids has to take on one very specific three-dimensional shape — only in that shape does the active site fit its substrate.
This shape doesn’t always come from the amino acid sequence alone. In several of these proteins, a bound metal ion holds a section of the chain in the needed arrangement without taking part in the actual chemical reaction itself. Calcium is one of these ions, and its part in this connection has been assessed in a statement from the European Food Safety Authority (EFSA).
On this basis, the European Commission authorized the following claim:
“Calcium contributes to the normal function of digestive enzymes”
EU-authorized wording · Regulation (EU) No 432/2012
The following sections describe three specific proteins where this structural contribution can be traced scientifically — as background knowledge, not as an extension of the wording quoted above.
Each of the three proteins does its own job in the small intestine — and each one carries a calcium-binding site at a specific spot.
The pancreatic enzyme that breaks starch chains down into smaller sugar building blocks carries a single calcium ion at a spot on the protein set apart from the catalytic pocket itself. This ion anchors a loop of the amino acid chain and, in doing so, keeps open the space where the substrate binds.
Pancreatic lipase works at the interface between a fat droplet and its watery surroundings. A small companion protein, colipase, anchors lipase at that interface so it stays in place. Calcium ions contribute to stabilizing the arrangement of this shared complex of lipase, colipase and interface.
The pancreas first releases its proteases as an inactive precursor. Only in the small intestine does an enzyme from the intestinal lining, enteropeptidase, cut off a short piece and release active trypsin. A calcium-binding site of its own in the finished trypsin then stabilizes a loop near the spot where the enzyme would otherwise cut itself apart.
The three enzyme systems on this page explained in full, plus a comparison table and the regulation text with nothing cut.
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