Sun Xin, Vivien Chua Jialing, Le Quynh Anh, Trujillo Francisco J, Oh Mi-Hwa, Campbell Dianne E, Mehr Sam, Lee Nanju Alice
School of Chemical Engineering, University of New South Wales, Syndey, NSW 2052, Australia.
National Institute of Animal Science, Rural Development Administration, Wanju 55365, Korea.
Foods. 2021 Jul 28;10(8):1741. doi: 10.3390/foods10081741.
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.
采用响应面法(RSM)和中心复合设计(CCD)技术,对高静水压(HHP)处理单独或与适度热处理相结合的三个关键工艺参数(即压力、温度和保持时间)进行优化,以调节β-乳球蛋白(β-Lg)和α-乳白蛋白(α-La)的分子结构,降低其与人IgE的反应性。通过免疫化学方法得出的关于HHP诱导β-Lg分子变化的RSM模型表明,温度(temp)、压力(p)以及温度与时间之间的相互作用()具有统计学显著影响(<0.05)。根据该模型确定的最小(β-Lg特异性)IgG结合的最佳条件为56℃、505MPa,保持时间为102分钟(R为0.81,-值为0.01)。在最佳条件及其周边区域进行的验证表明,该模型低估了β-Lg的结构修饰。在本研究中,β-Lg的分子变化与HHP诱导的二聚化直接相关,其遵循二次方程。β-Lg二聚体也导致无法检测到与人IgE的结合。