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- W2032023193 abstract "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." @default.
- W2032023193 created "2016-06-24" @default.
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- W2032023193 date "2010-11-03" @default.
- W2032023193 modified "2023-10-14" @default.
- W2032023193 title "Purification and Characterization of a Fish Scale-Degrading Enzyme from a Newly Identified <i>Vogesella</i> sp." @default.
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- W2032023193 doi "https://doi.org/10.1021/jf1034042" @default.
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