Lysozyme is a protein that was discovered by Alexander Fleming in 1922.

Rumor has it that in 1921, a droplet from Fleming’s nose (who was nursing a cold while working in his lab) accidentally fell into one of the Petri dishes containing microorganisms. Noticing the reaction of the bacteria to the fluid, Fleming deduced that it must have contained a “remarkable bacteriolytic element”, and so he set out to isolate it.

That same year he announced that this element, (which he named LYSOZYME because of its lysing action) was present in many tissues and secretions and was able to interfere with the growth of some specific bacterial colonies. He went on studying its’ various characteristics, and in 1922 he isolated the enzyme from hen egg white.

Some years later, the bactericidal activity of Lysozyme was widely confirmed, and after 1930 several studies reported how every living organism produces Lysozyme.

The term “Lysozyme” refers to an enzyme with a well-defined hydrolysis activity. In nature there are different types of Lysozyme with different characteristics, according to their origin. Generally, one can distinguish between human Lysozyme, (contained in various secretions such as tears, saliva and mother’s milk), and animal or plant produced Lysozyme.

It so happens that Mother Nature has provided hen egg white (albumin) with a very high content of Lysozyme in order to protect the integrity of the yolk, thus the chick embryo. This is why albumin is the raw material of choice for the industrial scale production of Lysozyme.

Here we shall refer to Lysozyme as the one extracted from hen egg white, consisting of 129 amino acids.