Purification and characterization of a fish scale-degrading enzyme from a newly identified Vogesella sp.

The objective of the present study is to purify and characterize the fish scale-degrading enzyme from Vogesella sp.7307-1, which was newly identified and isolated from fish scales. The enzyme from Vogesella sp.7307-1 was assayed with casein and confirmed as a protease. Crude protease was extracted, isolated, and purified 35.7-fold with 19.6% recovery using 20-80% saturation of ammonium sulfate fractionation, Q FF ion exchange chromatography, and Superdex 200 gelfiltration. The molecular weight of the purified enzyme was 119 kDa. The Km and Vmax were 0.067 mM and 425.5 U/mg-min, respectively using azo-casein as substrate. The optimum pH of the purified enzyme was 7.5, and the optimum temperature was 50 °C. The enzyme was stable at temperatures below 55 °C and pH range 7.5 to 9.0. The enzyme activity of the purified protease was completely inhibited by EDTA (ethylene diamine teraacetates), indicating the enzyme was a metalloprotease. Hydrolysates from fish scales treated with protease 7307-1 were found having low molecular weight peptides (<1 kDa). The protease 7307-1 is a promising enzyme for preparing smaller peptides from fish scales.