• bovine plasma;
  • surimi;
  • gelation;
  • cysteine protease


The protease inhibitory activity of bovine plasma protein (BPP) and its gel strengthening effect on Pacific whiting surimi were compared with E-64 [L-trans-epoxysuccinylleucylamido (4-guanidio) butane], iodoacetic acid (IAA), and a recombinant soybean cystatin (RSC). In terms of inhibitory activity, as low as 1.2 mM E-64,37.7 mM IAA, or 17.9 mg RSC were equivalent to 1% BPP. To produce the same gel strength as the 1% BPP-treated surimi, 10 times that level of E-64 and RSC were required, while 100 times that level of IAA did not increase the gel stress as effectively. Thus, plasma contributed to enhanced gelation of Pacific whiting surimi by inhibition of fish protease and also by other gel-enhancing factors in the plasma.