High pressure (HP, 200, 400, and 600 MPa)- and heat (60, 80, and 100 °C)-induced gelation, aggregation, and structural conformations of rapeseed protein isolate (RPI) were characterized using gel permeation–size-exclusion chromatography, differential scanning calorimetry, and circular dichroism (CD) techniques. HP treatments significantly (p < 0.05) increased the content of soluble protein aggregates and surface hydrophobicity of RPI. In contrast, heat treatments at 80 and 100 °C led to significant (p < 0.05) decreases in the amount of soluble protein aggregates. At pressure treatment of 200 MPa, there was a significant (p < 0.05) increase in free sulfhydryl group content of RPI, whereas 400- and 600-MPa treatments as well as temperature treatments (60–100 °C) caused significant decreases. Protein denaturation temperature was increased by about 6 °C by HP and heat treatments. The far-UV CD spectra revealed increases in α-helix content of RPI after HP treatments with 400 MPa producing the most increase. Near-UV data showed that HP and heat treatments of RPI led to increasing interactions among the aromatic amino acids (evidence of protein aggregation), and between aromatic amino acids and the hydrophilic environment, which indicates protein unfolding. Least gelation concentration of RPI was significantly (p < 0.05) reduced by HP and heat treatments, but HP-treated RPI produced gels with better textural properties (hardness increased from ~7.7 to 81.1 N, while springiness increased from ~0.37 to 0.99). Overall, pressure treatments (200–600 MPa) were better than heat treatments (60–100 °C) to modify the structure and improve gelation properties of RPI.
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Funding for this work was provided through the National Key Technology Research and Development Program of Jiangsu Province, China (project no. SBE201130495). The research program of Dr. R.E. Aluko is funded by the Natural Sciences and Engineering Research Council of Canada (NSERC) through a Discovery Grant.
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He, R., He, HY., Chao, D. et al. Effects of High Pressure and Heat Treatments on Physicochemical and Gelation Properties of Rapeseed Protein Isolate. Food Bioprocess Technol 7, 1344–1353 (2014). https://doi.org/10.1007/s11947-013-1139-z
- Rapeseed protein isolate
- High pressure treatment
- Heat treatment
- Differential scanning calorimetry
- Circular dichroism