The commercial value of Peruvian hake (Merluccius gayi peruanus) meat is low because of its soft texture. This study investigated the major factor contributing to the gel-forming ability of Peruvian hake surimi by comparing the effects of endogenous protease activity and parasitic infection. Heat-induced gels could not be obtained at 50 °C-90 °C. Surimi with severe parasitic infection showed a stronger gel-forming ability. The endogenous protease activities were the main factor influencing the Peruvian hake meat proteolysis and contributed to the low gel-forming ability, rather than parasitic infection. Specifically, endogenous cysteine proteases played an essential role in protein degradation and low gel-forming ability. Moreover, endogenous transglutaminase was also shown to be involved in the gel-forming ability upon heating at 40 °C. These results suggested that Peruvian hake meat could be used as a raw material of frozen surimi for fish gel by inhibiting the activity of endogenous proteases.

This study aimed to investigate the effect of pea protein isolate (PPI) on the functional, instrumental and textural quality parameters of duck meat batters (DMB). Ground duck breast meat was mixed with different concentrations of PPI (0%, 3%, 6% or 9%, w/w) to prepare DMB. The color, cooking yield, water-holding capacity, water distribution and migration, rheological properties and texture profile of the DMB were evaluated. The results showed that the L* value of the gel decreased and the b* value increased with the increasing pea protein addition. The cooking yield and water-holding capacity showed a gradual increase, but the difference was not significant (p > 0.05). Compared with the control, the storage modulus (G′) and loss modulus (G″) were higher at the beginning and at the end and increased with the addition of pea protein, which was in accordance with the Fourier series relationship. The hardness, chewiness and gumminess of the gels gradually increased; on the contrary, the springiness and cohesiveness first increased and then decreased, respectively, reaching a maximum value of 0.96 and 0.81 when the addition amount reached 6%. Adding pea protein to the gels not only increased the area of immobilized water but also decreased the area of free water, thus improving the water-holding capacity of the batters. Therefore, pea protein can promote the formation of a stable and elastic network structure of duck meat batters.

The effect of pH and ionic strength (μ) on the extraction capacity of myofibrillar proteins from Jumbo squid mantle muscle along with the addition of isoascorbic acid (IA) in its gel-forming ability (GFA) were evaluated. The results indicate that μ had a greater impact (p < 0.05) than pH on the extraction of muscle myofibrillar proteins. The effectiveness of IA, as the precursor of dehydro-isoascorbic acid (DIA), on the oxidation of sulfhydryl groups (-SH) to disulfide bonds (-SS-) of extracted proteins at 0.6 μ was also evaluated. During the sol-gel transition the -SH groups initially present in the protein system decreased (p < 0.05) due to the combined effect of heat treatment (90 °C/30 min) and the addition of IA; however, the oxidative effect of IA reduced (p < 0.05) the GFA of Jumbo squid muscle proteins. Results also indicated that NaCl at 2.8% rather than at 2.5% during gel preparation significantly (p < 0.05) improves its GFA.

The optimal conditions for the preparation of glucose-conjugated chicken myofibrillar proteins (Mfs) via the Maillard reaction, presenting strong antioxidant activity against hydroxyl radicals (･OH) and high solubility in low ionic strength medium, were sought using random-centroid optimization (RCO). Four parameters of temperature, relative humidity (RH), reaction time, and glucose-to-Mfs mixing ratio, were examined, resulting in a total of 24 vertices. Evaluations were carried out relatively to each individual vertex, and the optimal preparatory conditions to obtain the highest antioxidant activity were determined as follows: temperature of 52 °C, RH of 38%, reaction time of 6.79 h, and a glucose to Mfs mixing ratio of 11.7 (w/w). The resulting glucose-conjugated chicken Mfs gained thermal gel-forming ability and its ･OH averting capacity reached 9.7 ± 0.7 μmol of gallic acid equivalent/g of protein.Abbreviations: GA: gallic acid; HORAC: hydroxyl radical averting capacity; IC50: half-maximal inhibitory concentration; 2-ME, 2-mercaptoethanol; Mfs: myofibrillar proteins; MHC: myosin heavy chain; ･OH: hydroxyl radical; PAGE: polyacrylamide gel electrophoresis; RCO: random-centroid optimization; RH: relative humidity; RLU: relative light units; SDS: sodium dodecyl sulfate; SEM: scanning electron microscope; SS: disulfide.

A protein concentrate from giant squid (Dosidicus gigas) was produced under acidic conditions and its functional-technological capability evaluated in terms of its gel-forming ability, water holding capacity and colour attributes. Technological functionality of the concentrate was compared with that of squid muscle and a neutral concentrate. Protein-protein aggregates insoluble at high ionic strength (I=0.5M), were detected in the acidic concentrate as result of processing with no preclusion of its gel-forming ability during the sol-to-gel thermal transition. Even though washing under acidic condition promoted autolysis of the myosin heavy chain, the acidic concentrate displayed an outstanding ability to gel giving samples with a gel strength of 455 and 1160gcm at 75% and 90% compression respectively, and an AA folding test grade indicative of high gel strength, elasticity, and cohesiveness. The process proved to be a good alternative for obtaining a functional protein concentrate from giant squid muscle.