|Title||FT-IR and Raman spectroscopies determine structural changes of tilapia fish protein isolate and surimi under different comminution conditions.|
|Publication Type||Journal Article|
|Year of Publication||2017|
|Authors||Kobayashi, Y, Mayer, SG, Park, JW|
|Date Published||2017 Jul 01|
|Keywords||Animals, Fish Proteins, Spectroscopy, Fourier Transform Infrared, Spectrum Analysis, Raman, Tilapia|
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.
|Alternate Journal||Food Chem|