Extracellular metalloproteases from bacteria

Abstract

Bacterial extracellular metalloproteases (BEMPs) are a large group of metal-containing proteases secreted by heterotrophic bacteria. In this review, the diversity, structural characteristics, mechanisms of maturation, physiological roles, and applications of BEMPs are described. BEMPs are distributed among nine families of metalloproteases because of differences in primary sequences and structural characteristics. Until now, all of the BEMPs identified have been endoproteases harboring one catalytic Zn(2+) in the active centers. BEMPs are usually synthesized as inactive zymogens with a propeptide that is covalently linked to and inhibits the catalytic domain. The removal of the propeptides of BEMPs is dependent on other proteases or an autocleavage process. The main physiological function of BEMPs is to degrade environmental proteins and peptides for bacterial heterotrophic nutrition. As extracellular proteases, BEMPs vary greatly in enzymology properties to adapt to their respective environments. BEMPs have been widely used in the food and pharmaceutical industries. In order to broaden the application of BEMPs, it is essential to explore novel BEMPs and apply gene/protein engineering to improve the production and properties of promising BEMPs.

Purification and Characterization of 50 kDa ExtracellularMetalloprotease from Serratia sp. ZF03

“…The metalloprotease activity at pH ranging from 5.0 to 9.0 increased steadily until achieving the maximum activity at approximately pH 9.0. This metalloprotease was optimally active at the pH range of 8.0-10.0 (with a maximum activity at pH 9.0) ( Figure 5B) similar to most alkaline metalloproteases (7,12,16,(31)(32)(33)(34)(35). For example, Metalloprotease produced by S. marcescens ATCC 25419 has pH profile with the maximum activity at pH 8.5 and temperature profile (optimal activity at 45ºC) (16).…”

“…Serrapeptase (also known as serrapeptidase, serratiopeptidase and serratia peptidase) is a metalloprotease that has been purified and characterized from the Serratia. sp E-15 strain which was isolated from the gut of a larval silkworm (7,12). This enzyme dissolved the rigid proteins of cocoon and allowed the moth to come out (17).…”

Clostridium difficile secreted Pro‐Pro endopeptidase PPEP‐1 (ZMP1/CD2830) modulates adhesion through cleavage of the collagen binding protein CD2831

“…In addition to toxins, that have a direct deleterious effect on the host, bacteria also secrete proteases to perform 'housekeeping' functions such as signalling, attachment, and providing nutrients [1]. Some extracellular proteases are involved in interspecies competition by lysing cell walls of other bacteria [2,3].…”

Characterization of a metalloprotease from an isolate Bacillus thuringiensis 29-126 in animal feces collected from a zoological garden in Japan

“…Among the various proteases from diverse sources, microbial proteases are important industrial enzymes. They have been used in various industries: food, pharmaceuticals, baking, brewing, leather processing, and filming (Wu and Chen 2011 (Wu and Chen 2011).…”