Abstract
Structural changes, textural properties in Tilapia surimi myofibrillar protein during gelation were studied by Raman spectroscopy. The change in the amide I (1600-1700 cm-1) region indicated that the decrease in a-helices content accompanied by increase in ß-sheet and random coil after heating. The conformation of S-S bond was observed in the Raman spectrum near 500-600 cm-1 in the samples of 30-40 oC incubation temperature which produce textural profile with high gel strength. Intensity of the band near 758 cm-1 as well as a slight decrease in I853/I826 ratio when the heat increase 60-70 oC showed that the hydrophobic interaction was involved in the heat-induced gelation of surimi protein.
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