Effects of Sulfur-Containing Amino Acids and High Hydrostatic Pressure on Structure and Gelation Properties of Sweet Potato Protein
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The structural modification and gelation properties of sweet potato protein (SPP) affected by sulfur-containing amino acids (L-cysteine or L-cystine) and high hydrostatic pressure (HHP) were investigated. Additives altered the denaturation temperature and reduced the denaturation enthalpy of SPP. Higher α-helical contents were observed in untreated or HHP-treated SPP with L-cysteine or L-cystine, while β-sheet and random coil structure unit were decreased. FTIR spectra showed a weak absorbance in HHP-treated SPP with L-cysteine and L-cystine. Storage modulus (G′) of untreated or HHP-treated SPP was enhanced by L-cysteine and L-cystine. Textural properties of SPP gels were improved by sulfur-containing amino acids and HHP, especially for L-cysteine. Decrease in T2b relaxation time and increase in A21 proportion peak area by low-field NMR suggested that water bound more closely to SPP molecules in the presence of L-cysteine and L-cystine, and more immobilized water fraction was trapped in SPP gel matrix.
Key wordsSweet potato protein High hydrostatic pressure Sulfur-containing amino acids Gelation Low-field NMR
Sweet potato protein
High hydrostatic pressure
Fourier transform infrared
Differential scanning calorimetry
Nuclear magnetic resonance relaxation
The authors received the earmarked fund from China Agriculture Research System (CARS-10-B21) and National Key R & D Program of China (2016YFE0133600).
Compliance with Ethical Standards
Conflict of Interest
The authors declare that they have no competing interests.
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