Paper No. FSR-98 of the Journal Series of the Department of Food Science, North Carolina State University, Raleigh, NC 27695-7624. Use of trade names in this publication does not imply endorsement by North Carolina Agricultural Research Service, nor criticism of similar ones not mentioned. The authors gratefully acknowledge support from AMPC Inc., Ames, Iowa, U.S.A.
Bovine Plasma Protein Functions in Surimi Gelation Compared with Cysteine Protease Inhibitors
Version of Record online: 28 JUN 2008
Journal of Food Science
Volume 64, Issue 5, pages 842–846, September 1999
How to Cite
Kang, I.S. and Lanier, T.C. (1999), Bovine Plasma Protein Functions in Surimi Gelation Compared with Cysteine Protease Inhibitors. Journal of Food Science, 64: 842–846. doi: 10.1111/j.1365-2621.1999.tb15924.x
- Issue online: 28 JUN 2008
- Version of Record online: 28 JUN 2008
- MS 0529 received 2/7/99; revised 4/29/99; accepted 5/10/99.
- bovine plasma;
- 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.