Dairy Science Department, South Dakota State University, Brookings, SD 57007, USA.
Dairy Science Department, South Dakota State University, Brookings, SD 57007, USA; Dairy Foods R&D, Land O'Lakes, Inc., Arden Hills, MN 55126, USA.
Food Chem. 2017 May 15;223:114-120. doi: 10.1016/j.foodchem.2016.12.013. Epub 2016 Dec 9.
Whey protein isolate (WPI) solutions (12.8%w/w protein) were treated with varying concentrations of HO in the range of 0-0.144 HO to protein ratios (HTPR) by the addition of the required quantity of HO and deionized water. The samples were analyzed for heat stability, rheological properties, denaturation level of β-lactoglobulin (β-LG) and α-lactalbumin (α-LA). The samples treated with HO concentration >0.072 (HTPR) showed significant improvement in the heat stability, and decreased whey protein denaturation and aggregation. The WPI solution treated with HO (>0.072 HTPR) remained in the liquid state after heat treatment at 120°C, whereas the control samples formed gel upon heat treatment. Detailed analysis of these samples suggested that the improvement in the heat stability of HO treated WPI solution was attributed to the significant reduction in the sulfhydryl-disulfide interchange reaction during denaturation of β-LG and α-LA.
乳清蛋白分离物 (WPI) 溶液（12.8%w/w 蛋白质）通过添加所需量的 HO 和去离子水，用 HO 在 0-0.144 HO 与蛋白质比例（HTPR）范围内处理不同浓度的 HO。对样品的热稳定性、流变性能、β-乳球蛋白（β-LG）和α-乳白蛋白（α-LA）的变性水平进行了分析。HO 浓度 >0.072（HTPR）处理的样品显示出热稳定性显著提高，并且乳清蛋白变性和聚集减少。在 120°C 热处理后，用 HO（>0.072 HTPR）处理的 WPI 溶液保持液态，而对照样品在热处理时形成凝胶。对这些样品的详细分析表明，HO 处理的 WPI 溶液热稳定性的提高归因于β-LG 和 α-LA 变性过程中巯基-二硫键交换反应的显著减少。
