Abstract
Tilapia proteins refined by pH shift and water washing were chopped under various comminution conditions and their structural changes were investigated using Fourier transform infrared (FT-IR) and Raman spectroscopies. Both techniques revealed the degree of unfolding in protein structure increased when fish protein isolate (FPI) and surimi were chopped at 25 °C for 18 min compared to samples chopped at 5 °C for 6 min. Results indicated both hydrophobic interactions and disulfide bonds were significantly enhanced during gelation. FPI and surimi gels prepared at 25 °C for 18 min exhibited higher β-sheet contents and more chemical bonds such as hydrophobic interactions and disulfide bonds than those at 5 °C for 6 min. Results suggested that controlling comminution is important to improve gel qualities in FPI and surimi from tropical fish like tilapia. Moreover, FT-IR and Raman spectroscopies are useful complementary tools for elucidating the change in the structure of protein during comminution and gelation.
Original language | English |
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Pages (from-to) | 156-164 |
Number of pages | 9 |
Journal | Food Chemistry |
Volume | 226 |
DOIs | |
Publication status | Published - 2017 Jul 1 |
Externally published | Yes |
Keywords
- Chopping conditions
- Fish protein isolate
- FT-IR spectroscopy
- Raman spectroscopy
- Surimi
ASJC Scopus subject areas
- Analytical Chemistry
- Food Science
- Medicine(all)