Purification and Characterization of a Fish Scale-Degrading Enzyme from a Newly Identified Vogesella sp.

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• 作者：Min-Hsiung Pan ; Mei-Ling Tsai ; Wen-Ming Chen ; Ann Hwang ; Bonnie Sun Pan ; Yu-Ren Hwang ; Jen-Min Kuo
• 刊名：Journal of Agricultural and Food Chemistry
• 出版年：2010
• 出版时间：December 8, 2010
• 年：2010
• 卷：58
• 期：23
• 页码：12541-12546
• 全文大小：879K
• 年卷期：v.58,no.23(December 8, 2010)
• ISSN：1520-5118

文摘

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 K_m and V_max 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.

Keywords (keywords):

Fish scale; metalloprotease; purification; Vogesella sp.; collagen peptide