Authors would like to acknowledge the partial financial supports of the National Center for Genetic Engineering and Biotechnology (BIOTEC) and National Science and Technology Development Agency (Bangkok, Thailand).
Proteolytic Degradation of Tropical Tilapia Surimi
Version of Record online: 28 JUN 2008
Journal of Food Science
Volume 65, Issue 1, pages 129–133, January 2000
How to Cite
Yongsawatdigul, J., Park, J.W., Virulhakul, P. and Viratchakul, S. (2000), Proteolytic Degradation of Tropical Tilapia Surimi. Journal of Food Science, 65: 129–133. doi: 10.1111/j.1365-2621.2000.tb15967.x
- Issue online: 28 JUN 2008
- Version of Record online: 28 JUN 2008
- MS 1999-0309 received 3/2/99; revised 8/16/99; accepted 8/26/99.
- enzymatic degradation;
- serine proteinase
Proteolytic degradation of tropical tilapia surimi was biochemically and rheologically characterized to identify a group of proteinase(s) responsible for its textural degradation. Proteolysis of tilapia surimi occurred as the temperature increased and attained the highest activity at 65 °C. Smaller proteins with molecular weight of 116-97 kDa were noted as a result of myosin heavy chain (MHC) degradation. MHC completely disappeared when incubated at 65 °C for 4 h. Proteolysis was significantly inhibited by soybean trypsin inhibitor (SB) and leupeptin (LE). Storage modulus (G′) of surimi gels mixed with either SB or LE was higher than other inhibitors indicating that serine type proteinase(s) were involved in proteolysis of tropical tilapia surimi.