Here, potential physicochemical and techno‐functional properties of the albumen protein recovered from over‐salted albumen by an effective acid‐aided pH‐shift process (POA) were tested in comparison with the fresh albumen (FA) and albumen protein recovered from fresh albumen by acid‐aided pH‐shift process (PFA). POA contained 66.73% protein and 11.30% sodium (dry basis). Surface hydrophobicities of PFA and POA were higher than FA (P < 0.05), whereas the reactive sulfhydryl content of FA was higher than PFA and POA (P < 0.05). PFA had the highest whiteness followed by POA and FA, respectively. Single endothermic peak in DSC thermogram was found at 86.86, 89.67 and 98.96 °C for FA, PFA and POA, respectively. Long‐term salting impaired the solubility, viscosity, emulsifying activity and gelation but not for foaming of albumen protein isolate. FA can be softly gelled with continuously packed structure, whereas PFA and POA underwent agglutination to form white clot suspension with spongy network.

中文翻译：

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盐腌过的鸭蛋（Anas platyrhucus）蛋白的酸辅助pH转换蛋白分离物的理化和技术功能特性

在这里，与新鲜蛋白（FA）和从新鲜蛋白回收的蛋白相比，通过有效的酸辅助pH转换过程（POA）测试了从盐分过高的蛋白回收的蛋白的潜在物理化学和技术功能特性。通过酸辅助pH转换过程（PFA）。POA包含66.73％的蛋白质和11.30％的钠（干基）。PFA和POA的表面疏水性高于FA（P  <0.05），而FA中的反应性巯基含量高于PFA和POA（P <0.05）。PFA的白度最高，其次是POA和FA。在FA，PFA和POA的DSC温度图中，单个吸热峰分别位于86.86、89.67和98.96°C。长期加盐会损害溶解度，粘度，乳化活性和胶凝作用，但不会使蛋白分离物起泡。FA可以软凝胶成连续堆积的结构，而PFA和POA则经过凝集形成具有海绵状网络的白色凝块悬浮液。