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Updated: Mar 6, 2026
Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
Published on: September 12, 2019
FT-IR and Raman spectroscopies determine structural changes of tilapia fish protein isolate and surimi under
Yuka Kobayashi1, Steven G Mayer2, Jae W Park1
1Oregon State University Seafood Research and Education Center, 2001 Marine Drive #253, Astoria, OR 97103, USA.
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 18min compared to samples chopped at 5°C for 6min. Results indicated both hydrophobic interactions and disulfide bonds were significantly enhanced during gelation. FPI and surimi gels prepared at 25°C for 18min exhibited higher β-sheet contents and more chemical bonds such as hydrophobic interactions and disulfide bonds than those at 5°C for 6min. 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.
