The influence of two common cooking methods, grilling and baking, on chemical composition, water retention, fat retention, cooking yield, diameter reduction, expressible water, color and mechanical texture of tilapia (Oreochromis niloticus) fish burgers was investigated. Texture analyses were performed using a Warner-Bratzler test. The fish burger had a softer texture with a lower shear force than other meat products reported in the literature. There were no significant differences in proximate composition, diameter reduction, fat retention and expressible water between the grilled and oven-baked fish burgers. Cooking methods did not affect the cooking times and cooking rates. Warner-Bratzler parameters and color were significantly influenced by the cooking method. Grilling contributed to a shear force and work of shearing increase due to the lower cooking yield and water retention. Raw burgers had the highest L* (69.13 ± 0.96) and lowest b* (17.50 ± 0.75) values. Results indicated that baking yielded a product with better cooking characteristics, such as a desired softer texture with lower shear values (4.01 ± 0.54) and increased water retention (95.82 ± 0.77). Additionally, the baked fish burgers were lighter (higher L*) and less red (lower a*) than the grilled ones.

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This study focussed on the evaluation of thermal denaturation at three different stages during soy protein isolation and the effect of subunit composition on the formation of heat-induced soy protein gels. Soy protein isolates (SPI) were prepared from 12 high protein lines, Harovinton variety and 11 derived null-lines which lacked specific glycinin (11S) and b-conglycinin (7S) protein subunits. Protein denaturation during SPI processing was monitored by differential scanning calorimetry (DSC). The results showed that hexane extraction of oil from soybean flours at 23°C or 105°C did cause changes in protein conformation. Rheological measurements showed that lines with different subunit compositions and 11S:7S ratio had distinctive gelation temperatures and resulted in gels with different network structures. All lines formed particulate gels at 11% protein. The 11S:7S ratio was not correlated to final stiffness, measured as the storage modulus G 0 , of SPI gels. Lower gelation temperatures were usually observed for 7S-rich lines. The absence of A3 and the combination of A1, A2 and A4 subunits of 11S fraction may suggest the formation of stiffer gels. A more detailed study of the frequency dependence of G 0 for the various networks formed also indicated that differences in subunit composition influenced the network structures.