The response surface methodology (RSM) and central composite design (CCD) technique were used to optimize the three key process parameters (i.e., pressure, temperature and holding time) of the high-hydrostatic-pressure (HHP) processing either standalone or combined with moderate thermal processing to modulate molecular structures of β-lactoglobulin (β-Lg) and α-lactalbumin (α-La) with reduced human IgE-reactivity. The RSM model derived for HHP-induced molecular changes of β-Lg determined immunochemically showed that temperature (temp), pressure (p) and the interaction between temperature and time () had statistically significant effects ( < 0.05). The optimal condition defined as minimum (β-Lg specific) IgG-binding derived from the model was 505 MPa at 56 °C with a holding time of 102 min (R of 0.81 and -value of 0.01). The validation carried at the optimal condition and its surrounding region showed that the model to be underestimating the β-Lg structure modification. The molecular change of β-Lg was directly correlated with HHP-induced dimerization in this study, which followed a quadratic equation. The β-Lg dimers also resulted in the undetectable human IgE-binding.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8394912PMC
http://dx.doi.org/10.3390/foods10081741DOI Listing

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