Food Science and Biotechnology

Korean Society of Food Science and Technology (한국식품과학회)
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Characteristics of the Protease Inhibitor Purified from Chum Salmon (Oncorhynchus keta) Eggs

  • Kim, Kenn-Yeong (Faculty of Marine Bioscience and Technology, Kangnung National University) ;
  • Ustadi, Ustadi (Fisheries and Marine Department, Agriculture Faculty, Gadjah Mada University) ;
  • Kim, Sang-Moo (Faculty of Marine Bioscience and Technology, Kangnung National University)
  • Published : 2006.02.28
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Abstract

Protease inhibitor of 72.6 kDa was successively purified from chum salmon (Oncorhynchus keta) eggs by ion exchange, gel permeation, and affinity chromatographies. Protease inhibitor was purified with yield and purification fold of 1.50% and 58.11, respectively. SDS-PAGE results showed purified protease inhibitor consisted of two protein subunits of 54.0 and 18.6 kDa. Chum salmon inhibitor exhibited stability between 20 and $40^{\circ}C$ in weak acid environment (PH 6), and inhibited papain and cathepsin, members of cysteine protease, but not chymotrypsin. The protein inhibited cathepsin more effectively than did egg white protease inhibitor, whereas the reverse was true for papain. These results indicate chum salmon egg inhibitor is heterodimer, thus the inhibitor was classified as cysteine protease inhibitor.

Keywords

References

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