Abstract
The ocean harbors a variety of bacteria that contain huge protease resources and offer a great potential for industrial and biotechnological applications. Here, we isolated a protease-secreting bacterium Vibrio pomeroyi strain 12613 from Atlantic seawater and purified a protease VP9 from strain 12613. VP9 was identified as a metalloprotease of the M4 family. VP9 could hydrolyze casein and gelatin but not elastin and collagen. With gelatin as the substrate, VP9 showed the highest activity at 40°C and pH 6.0–8.0. It was stable at temperatures of 50°C and less and in the range of pH 5.0–11.0. VP9 also had good tolerance to NaCl, non-ionic detergents, and organic solvent methanol. Unlike other M4 metalloproteases, VP9 has distinct collagen-swelling ability, and its collagen-swelling effect was concentration dependent. The relative expansion volume of collagen increased by approximately eightfold after treatment with 10 μM VP9 at 37°C for 12 h. The collagen-swelling mechanism of VP9 on bovine-insoluble type I collagen was further studied. Atomic force microscopy observation and biochemical analyses showed that VP9 can degrade proteoglycans in collagen fibers, resulting in the release of collagen fibrils from collagen fibers and the swelling of the latter. In addition, VP9 can degrade glycoproteins, a non-collagenous constituent interacting with collagen in the skin. The characteristics of VP9, such as sufficient specificity toward proteoglycans and glycoproteins but no activity toward collagen, suggest its promising potential in the unhairing and fiber-opening processing in leather industry.
Highlights
The ocean covers approximately 71% of the earth’s surface and contains huge and various microbial resources
The S8 serine protease MCP-01 produced by marine sedimentary Pseudoalteromonas sp
VP9 can degrade glycoproteins, which are related to the structural stability of collagen and extracellular matrix (ECM). These results indicate that VP9 is a new M4 metalloprotease with specificity for the degradation of proteoglycans and glycoproteins in collagen and skin ECM, which may have a potential in the dehairing and fiber-opening processes in leather industry
Summary
The ocean covers approximately 71% of the earth’s surface and contains huge and various microbial resources. Some proteases secreted by marine bacteria have been identified and characterized, most of which have special properties, indicating that marine bacteria are good sources to find novel proteases (Chen et al, 2007, 2009; Zhao et al, 2012; Ran et al, 2014). Some proteases from marine microorganisms have been shown to have promising application prospects in industry (Vázquez et al, 2008; Cristóbal et al, 2011). SM9913 has high collagenolytic activity and has good potential in preparing collagen oligopeptides from cod skin (Zhao et al, 2008; Chen et al, 2017). Only a few proteases from marine microorganisms with biotechnical/industrial potentials have been reported. New proteases with potential biotechnological/industrial applications are still necessary to be discovered from marine microorganisms
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