Center for Food Safety and Applied Nutrition, Food and Drug Administration, Laurel, MD.
Joint Inst. for Food Safety and Applied Nutrition, Univ. of Maryland, College Park, MD.
J Food Sci. 2019 Aug;84(8):2357-2363. doi: 10.1111/1750-3841.14712. Epub 2019 Jul 30.
Peanut allergic consumers rely on food package labels to avoid foods containing peanut. The inadvertent presence of peanut in foods due to cross-contact can be fatal if ingestion of such food leads to an allergic reaction. Analytical methods are available to detect undeclared peanut in foods. However, depending on the type of food matrix and food processing parameters, method performance can be adversely affected due to reduction in the extraction efficiency of peanut proteins. Temperature and probe sonication were used as a preincubation treatment for peanut flour slurries to assess their effect on the total peanut protein solubility from raw, light-roasted, and dark-roasted peanut flours. The effect of these treatments on the immunoreactivity of peanut allergens (Ara h 1, Ara h 2, Ara h 3, and Ara h 6) was determined by an indirect enzyme-linked immunosorbent assay using antibodies raised against these individual peanut proteins. Preincubation at 50 °C did not significantly improve the peanut protein solubility, whereas an increase in protein solubility was observed when light- and dark-roasted peanut flour slurries were preincubated at 90 °C or sonicated. The immunoreactivity of peanut allergens varied depending on the degree of peanut flour roasting and type of preincubation treatment. Overall, the immunoreactivity of peanut allergens from most peanut flour slurries was unaffected when preincubated at 50 °C for up to 60 min or sonicated with a probe for up to 5 min, whereas preincubation at 90 °C resulted in a time-dependent reduction in immunoreactivity of peanut allergens. Sonication treatment may improve peanut protein extraction without markedly affecting their immunoreactivity. PRACTICAL APPLICATION: Extraction of peanut proteins is vital for developed analytical methods to estimate peanut allergens in foods. The manuscript describes the effect of two different temperatures (50 and 90 °C) and probe-type sonication on peanut protein solubility. The findings suggest sonication can improve peanut protein solubility without markedly affecting their immunoreactivity.
花生过敏消费者依赖食品包装标签来避免食用含花生的食物。如果食用含有花生的食物导致过敏反应，由于交叉接触而无意中存在的花生可能是致命的。现已有分析方法可用于检测食品中未申报的花生。然而，由于花生蛋白提取效率降低，取决于食品基质的类型和食品加工参数，方法性能可能会受到不利影响。温度和探针超声处理被用作花生粉糊的预孵育处理，以评估它们对生、轻度烘烤和重度烘烤花生粉中总花生蛋白溶解度的影响。通过针对这些个别花生蛋白的抗体的间接酶联免疫吸附测定法，确定这些处理对花生过敏原（Ara h 1、Ara h 2、Ara h 3 和 Ara h 6）的免疫反应性的影响。预孵育在 50°C 时并未显著提高花生蛋白溶解度，而当轻度和重度烘烤花生粉糊在 90°C 下预孵育或超声处理时，蛋白溶解度增加。花生过敏原的免疫反应性取决于花生粉烘烤程度和预孵育处理类型的不同而变化。总体而言，当在 50°C 下预孵育长达 60 分钟或用探头超声处理长达 5 分钟时，大多数花生粉糊中的花生过敏原的免疫反应性不受影响，而在 90°C 下预孵育则导致花生过敏原的免疫反应性随时间呈下降趋势。超声处理可能会改善花生蛋白的提取，而不会明显影响其免疫反应性。实际应用：提取花生蛋白对于开发分析方法来估计食品中的花生过敏原至关重要。本文描述了两种不同温度（50 和 90°C）和探针式超声处理对花生蛋白溶解度的影响。研究结果表明，超声处理可以提高花生蛋白的溶解度，而不会明显影响其免疫反应性。
