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Bovine Plasma Protein Functions in Surimi Gelation Compared with Cysteine Protease Inhibitors
Author(s) -
Kang I.S.,
Lanier T.C.
Publication year - 1999
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1999.tb15924.x
Subject(s) - iodoacetic acid , chemistry , whiting , cystatin , protease , cysteine protease , chromatography , cysteine , biochemistry , food science , fish <actinopterygii> , cystatin c , enzyme , fishery , biology , renal function
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.