Abstract

Gels from spotted featherback (SF) muscle were prepared by different setting conditions including 4 °C/18 h, 25 °C/30 min, 25 °C/2 h, 40 °C/30 min and 60 °C/30 min followed by cooking at 90 °C/20 min. Directly cooked gel was used as a control. SF gels set at 4 °C/18 h and 60 °C/30 min exhibited higher proteolytic degradation than did by other setting temperatures and control (P < 0.05) as evidenced by TCA-soluble peptides and the marked decrease in myosin heavy chain (MHC) under SDS-PAGE. For gelling properties, setting at 60 °C/30 min showed the gel with lowest breaking force and highest expressible drip whereas setting at 25 °C/30 min rendered the gel with highest breaking force (P < 0.05). Indeed, the higher the setting temperature applied the lower the a* value was observed (P < 0.05). However, the L* and b* values were varied among setting conditions. A finer structure of SF gel correlated well with the breaking force, particularly at medium setting temperature (25 °C/30 min). Therefore, the setting regimes strongly influenced the proteolysis and gel properties of SF muscle. Setting at 25 °C for 30 min was the best suit to prevent the proteolysis and hence strengthen the gel of SF muscle.