Open AccessTHE CHANGES OF PROTEIN STRUCTURE IN TILAPIA SURIMI DURING GELATION BY RAMAN SPECTROSCOPY
Author(s) -
Do Thi Yen
Publication year - 2018
Publication title -
vietnam journal of science and technology/science and technology
Language(s) - English
Resource type - Journals
eISSN - 2815-5874
pISSN - 2525-2518
DOI - 10.15625/2525-2518/55/5a/12197
Subject(s) - raman spectroscopy , random coil , myofibril , chemistry , tilapia , crystallography , analytical chemistry (journal) , fish <actinopterygii> , chromatography , circular dichroism , biochemistry , fishery , biology , optics , physics
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.