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Bacterial neutral proteases are active in a narrow pH range (pH 5 to 8) and have relatively low thermotolerance. Due to their intermediate rate of reaction, neutral proteases generate less bitterness in hydrolyzed food proteins than do the animal proteinases and hence are valuable for use in the food industry. Neutrase, a neutral protease, is insensitive to the natural plant proteinase inhibitors and is therefore useful in the brewing industry. The bacterial neutral proteases are characterized by their high affinity for hydrophobic amino acid pairs.
The IgA proteases, which vary in their requirements for metal ions, are neutral endopeptidases whose role in the infectious process is not known but whose pronounced substrate specificity for human proteins of the IgA1 subclass has repeatedly been demonstrated.s reagents, the IgA proteases are useful in cleaving IgA molecules to yield intact Fc alpha and Fab alpha fragments that will allow the study of the structure and function of the two large regions of IgA immunoglobulin proteins.