FT-IR and Raman spectroscopies determine structural changes of tilapia fish protein isolate and surimi under different comminution conditions.
Food Chem
; 226: 156-164, 2017 Jul 01.
Article
em En
| MEDLINE
| ID: mdl-28254007
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 ß-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.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Análise Espectral Raman
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Tilápia
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Espectroscopia de Infravermelho com Transformada de Fourier
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Proteínas de Peixes
Limite:
Animals
Idioma:
En
Ano de publicação:
2017
Tipo de documento:
Article