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ESOC's action mechanism

Ovomucoids and Ovoinhibitors:


This polypeptide has three very similar functional domains that are each capable of fixing a protease (for example trypsin). It substantially reduces the production of IgE (immunoglobulins E) antibody and consequently is a powerful inhibitor of the release of histamine by basophils and mastocytes. Even at low levels, ovomucoid, by contrast to the majority of anti-allergic substances, strongly and effectively inhibits the release of histamine by the basophils.

The ovomucoid from quail's eggs (Ovogenics strain) is one of the most powerful natural inhibitors of human trypsin (serine-protease).


The ovoinhibitor in the whites of quail's eggs (Ovogenics strain) is a glycoprotein whose structure differs from that of the ovomucoid. Like the ovomucoid, the ovoinhibitor is one of the inhibitors of serine-proteases. It is a powerful inhibitor of elastase, bacterial and fungal proteases.

Ovoinhibitors are distinguished from ovomucoid in their capacity to inhibit aspergillus oryzae proteinase.

There are many recent publications on the subject of serine-proteases. The ovomucoid and ovoinhibitor from the albumen of quail's eggs (Ovogenics strain) are recognised as powerful inhibitors of serine-proteases and are the only avian eggs capable of inhibiting trypsin.

Table showing the activity of different ovoinhibitors calculated vis-à-vis the inhibiting activity of hen's egg white on aspergillus oryzae fungal protease:

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