Gong Pin, Yue Shan, Wang Jie, Xu Ke, Yang Wenjuan, Li Nan, Wang Jing, Zhao Yanni, Chen Fuxin, Guo Yuxi
School of Food science and Engineering, Shaanxi University of Science and Technology, Xi'an 710021, China; School of Biological and Pharmaceutical Sciences, Shaanxi University of Science and Technology, Xi'an 710021, China; Xi' an Key Laboratory of Precision Nutrition and Functional Product Innovation, Shaanxi University of Science and Technology, Xi'an 710021, China.
School of Food science and Engineering, Shaanxi University of Science and Technology, Xi'an 710021, China; School of Biological and Pharmaceutical Sciences, Shaanxi University of Science and Technology, Xi'an 710021, China; Xi' an Key Laboratory of Precision Nutrition and Functional Product Innovation, Shaanxi University of Science and Technology, Xi'an 710021, China.
Int J Biol Macromol. 2025 Mar;295:139562. doi: 10.1016/j.ijbiomac.2025.139562. Epub 2025 Jan 7.
This study investigates the effects of ultrasound synergistic pH shift modification on the structural and functional properties of Hericium erinaceus (HE) proteins. The modification resulted in significant changes in the molecular structure of HE proteins, including increased solubility (49.69 % at pH 1.5 and 61.30 % at pH 12.5), enhanced surface hydrophobicity (from 721.00 to 3377.00), and the exposure of free sulfhydryl groups, which rose from 9.3 μmol/g in the control to 19.9 μmol/g at pH 12.5. The modification also led to a reduction in particle size, improving oil-holding capacity and foaming properties, with foaming stability increasing from 10.5 % to 60.3 % at pH 12.5. Furthermore, the emulsification activity was significantly enhanced (187.5 % at pH 12.5). Rheological analysis revealed that ultrasound-modified proteins exhibited improved flow stress and gelation properties, with a shear recovery rate of 65.71 %. In 3D printing applications, the modified HE proteins demonstrated better printability, structural stability, and mechanical integrity, attributed to the enhanced molecular interaction and gelation properties. These findings suggest that ultrasound-assisted pH shift modification effectively alters the structure and functionality of HE proteins, making them suitable for use as a versatile raw material in food applications, particularly in 3D food printing.
本研究考察了超声协同pH值变化修饰对猴头菇（HE）蛋白结构和功能特性的影响。该修饰导致HE蛋白分子结构发生显著变化，包括溶解度增加（在pH 1.5时为49.69%，在pH 12.5时为61.30%）、表面疏水性增强（从721.00增至3377.00）以及游离巯基暴露，其含量从对照中的9.3 μmol/g增至pH 12.5时的19.9 μmol/g。该修饰还导致粒径减小，提高了持油能力和起泡性能，在pH 12.5时起泡稳定性从10.5%提高到60.3%。此外，乳化活性显著增强（在pH 12.5时为187.5%）。流变学分析表明，经超声修饰的蛋白表现出改善的流动应力和凝胶化特性，剪切恢复率为65.71%。在3D打印应用中，修饰后的HE蛋白表现出更好的可打印性、结构稳定性和机械完整性，这归因于增强的分子相互作用和凝胶化特性。这些发现表明，超声辅助pH值变化修饰有效地改变了HE蛋白的结构和功能，使其适合作为食品应用中的通用原料，特别是在3D食品打印中。
