Abstract
SummaryThe aim of this study was to reduce the salt content of tilapia surimi using histidine without affecting gelation properties. The addition of histidine (T‐1) to low salt surimi gels increased the breaking force and deformation and resulted in the highest gel strength (458 g.cm). Expressible moisture was less in the T‐1 sample and proteolytic degradation was higher in the control sample indicating that autolysis did not occur in histidine added sample during gel setting. Protein patterns revealed cross‐linking of myosin heavy chain in gels with added histidine. Fourier transformed infrared spectra implied that histidine‐induced unfolding of proteins occurred after heating. T‐1 samples exhibited a dense and compact microstructure, whereas the control gel was loose. The results of this study show that the addition of histidine could yield high‐quality gels from tilapia surimi in low salt conditions.
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