Microbial proteases are one of the largest groups of industrial enzymes.
Microbial proteases are also used widely as biocatalysts in organic synthesis.
Microbial proteases are one of the most commercially valuable enzymes, of which the largest market share has been taken by subtilases or alkaline proteases of the Bacillus species.
Microbial proteases are one of the most commercially valuable enzymes [ 1], of which the largest market share has been taken by subtilases or alkaline proteases of the Bacillus species, which has been extensively studied in terms of both biological properties and applications [ 1- 3].
The industrial production of microbial proteases is favored due to the fact that they have a short generation time, because of the ease of genetically manipulating microorganisms, and because of the diversity of species available in nature, many of which are still unexplored [ 2, 3].
Regarding the suitability of the enzymes in the protein hydrolyzation field, Alcalase, a microbial protease, is most preferred and is widely used.
Similarly, the property of microbial serine proteases was reported for polyethylene succinate biodegradation (Lim et al. 2005).
We therefore studied the structural similarity between gliadins and basic proline-rich proteins and investigated if gliadins may be substrates for oral microbial proteases and be degraded into non-immunogenic peptides.
However, various animals, plants, and microbial proteases have been suggested as milk coagulants (Zhang et al. 2011), but still attention has been focused on production of milk-clotting enzymes from microbial sources (Silveira et al. 2005; Wu et al. 2013) due to their rapid growth, relative inexpensive growth substrate, and diverse properties.
Microbial proteases can be produced in various ways and studies have shown that, depending on the culture conditions, different forms of the same protease can be expressed [ 19].
