Trypsin Inhibitory Activity and Gel-Enhancing Effect of Sarcoplasmic Proteins from Common Carp
Article first published online: 14 SEP 2012
© 2012 Institute of Food Technologists®
Journal of Food Science
Volume 77, Issue 10, pages C1124–C1130, October 2012
How to Cite
Siriangkanakun, S. and Yongsawatdigul, J. (2012), Trypsin Inhibitory Activity and Gel-Enhancing Effect of Sarcoplasmic Proteins from Common Carp. Journal of Food Science, 77: C1124–C1130. doi: 10.1111/j.1750-3841.2012.02919.x
- Issue published online: 12 OCT 2012
- Article first published online: 14 SEP 2012
- MS 20120802 Submitted 6/9/2012, Accepted 7/17/2012.
- fish protein;
- sarcoplamic proteins;
Abstract: Proteinase inhibitory activity of sarcoplasmic protein (SP) extracted from common carp (Cyprinus carpio) muscle and its gel-improving ability were investigated. SPs displayed 89% and 54% inhibitory activity toward trypsin at 40 and 65 °C, respectively. Protein bands with molecular mass of 69, 50, 44, 41, and 35 kDa appeared on trypsin inhibitory activity staining under nonreducing condition when incubated at 40 °C, while 2 protein bands at 54 and 35 kDa were observed at 65 °C. Addition of SP at 0.18 g protein/100 g increased textural properties of threadfin bream surimi gel. However, when SP was added in combination with various CaCl2 concentrations (0.1% to 0.5%) it did not further improve textural properties as compared to the addition of SP alone. Retention of myosin heavy chain of threadfin bream surimi was greater with the addition of SP. These results indicated that the gel-enhancing effect of common carp SP was due to the inhibitory activity toward endogenous trypsin-like proteinases in threadfin bream surimi.
Practical Application: Sarcoplasmic protein from common carp muscle could be used as a functional protein ingredient that minimizes muscle proteolysis and improves textural properties of surimi containing trypsin-like endogenous proteinases.