[3] Thermolysin specifically catalyzes the hydrolysis of peptide bonds containing hydrophobic amino acids.

[4] Thermolysin is the most stable member of a family of metalloproteinases produced by various Bacillus species.

The prosequence then acts as a molecular chaperone and leads to autocleavage of the peptide bond linking pro and mature sequences.

[8] The thermal stability of members of the TLP family is measured in terms of a T50 temperature.

However, while calcium binding makes a significant contribution to stabilising thermolysin, more crucial to stability is a small cluster of N-terminal domain amino acids located at the proteins surface.