Protease is one of the most industrially important enzymes.

Protease enzymes are

manufactured commercially from plants, animals, and microorganisms, and they can be
one of the most significant categories of industrial enzymes that are widely employed.
Proteases are a significant class of enzymes that carry out proteolysis by hydrolysing the
peptide bonds holding the amino acids in the polypeptide chain together.
All microbes have the ability to produce proteases (Singh, 2019). This indicates that
microbes, especially protease enzymes, are fantastic metabolite repositories. Proteases
are divided into three classes based on their acid-base behaviour: acid, neutral, and
alkaline proteases. Specifically for this study the focus will be more on protease producing
microorganisms in fermented foods.
Proteases break the peptide bonds that connect the amino acid residues in lengthy protein
chains into smaller pieces (Nadeem, 2020). The endopeptidases trypsin, chymotrypsin,
pepsin, and elastase attack the internal peptide bonds of a protein while the exopeptidase
amino peptidases and carboxypeptidase can detach the terminal amino acid from the
protein chain. Since the discovery of enzymes, proteases have also been classified as an
exotoxin, a virulence factor in bacterial pathogenesis that can harm extracellular
structures.

Naveed, M., Nadeem, F., Mehmood, T., Bilal, M., Anwar, Z. and Amjad, F., 2021. Protease—a
versatile and ecofriendly biocatalyst with multi-industrial applications: an updated review. Catalysis
Letters, 151, pp.307-323.

Thakrar, F.J. and Singh, S.P., 2019. Catalytic, thermodynamic and structural properties of an
immobilized and highly thermostable alkaline protease from a haloalkaliphilic actinobacteria,
Nocardiopsis alba TATA-5. Bioresource technology, 278, pp.150-158.