Journal
FOOD CHEMISTRY
Volume 226, Issue -, Pages 156-164Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2017.01.068
Keywords
FT-IR spectroscopy; Raman spectroscopy; Fish protein isolate; Surimi; Chopping conditions
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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 degrees C for 18 min compared to samples chopped at 5 degrees C for 6 min. Results indicated both hydrophobic interactions and disulfide bonds were significantly enhanced during gelation. FPI and surimi gels prepared at 25 degrees C for 18 min exhibited higher beta-sheet contents and more chemical bonds such as hydrophobic interactions and disulfide bonds than those at 5 degrees 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. (C) 2017 Elsevier Ltd. All rights reserved.
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