89B-15

R. M. URESTI¹, G. Velazquez², J. A. Ramírez³, M. Vázquez³, and J. A. Torres⁴. (1) Food Science and Technology, Food Process Engineering Group at Oregon State Univ. and Univ. Autónoma de Tamaulipas, UAM-Reynosa-Aztlán, Calle 16 y Lago de Chapala. Col. Aztlán, Reynosa, Tam., 88740, Mexico, (2) Food Science and Technology, Food Process Engineering Group at Oregon State Univ. , Autónoma de Tamaulipas and Oregon State Univ., UAM-Reynosa-Aztlán, Calle 16 y Lago de Chapala. Col. Aztlán, Reynosa, Tam., 88740, Mexico, (3) Food Science and Technology, Univ. Autónoma de Tamaulipas, UAM-Reynosa-Aztlán, Calle 16 y Lago de Chapala. Col. Aztlán, Reynosa, Tam., 88740, Mexico, (4) Food Process Engineering Group, Dept. of Food Science & Technology, Oregon State Univ., 100 Wiegand Hall, Corvallis, OR 97331-6602

Arrowtooth flounder is an underutilized and most abundant fishery resource in the Gulf of Alaska. However, it has only minor commercial interest because its flesh texture degrades during cooking or frying, a phenomenon that has been associated with endogenous proteases. The objective of this study was to evaluate the effect of high pressure processing (HPP) at 400 and 600 MPa for 1 and 5 min on the mechanical and functional properties of heat-induced fish gels obtained from arrowtooth flounder fish paste at different temperatures. Gels were obtained at 40 °C for 30 min plus 90 °C for 15 min (setting) and 60 °C for 30 min plus 90 °C for 15 min (modori) and compared with control samples obtained at 90 °C for 15 min. Mechanical properties (TPA analysis), functional properties (amount of expressed water), color parameters and electrophoretic pattern of proteins (SDS-PAGE) were then determined for control and pressure-treated samples. Gels obtained by HPP without cooking were stronger than gels obtained by cooking at 90 °C. HPP improved the mechanical properties of heat-induced gels. No setting effect was observed when samples were obtained at 40 °C for 30 min. Proteolysis of fish gels was not inhibited by HPP when incubated at 60 °C. The results obtained suggest differences in the mechanisms of protein aggregation for pressure- and heat-induced fish gels.

Session 89B, Aquatic Food Products: Surimi, gels and by-products
2:00 PM - 5:30 PM, Tuesday PM Room Hall I-2

2005 IFT Annual Meeting, July 15-20 - New Orleans, Louisiana