Deng Xiang-Yu, Hao Man, Yang Jie, Sun Gui-Jin, Li Ying-Qiu, Wang Chen-Ying, Liang Yan, Mo Hai-Zhen
Shangdong Key Laboratory of Healthy Food Resources Exploration and Creation, School of Food Science and Engineering, Qilu University of Technology (Shandong Academy of Sciences), Jinan, China.
School of Architecture and Chemical Engineering, Heze Vocational College, Heze, China.
J Sci Food Agric. 2025 Aug 12. doi: 10.1002/jsfa.70119.
Lotus seed protein, as a plant protein, has high nutritional and functional value but limited gelation ability. So, the structure and gelation properties of lotus seed protein gel (LSPG) treated using ultrasound were investigated. Structural properties were analyzed through surface hydrophobicity, free sulfhydryl groups, electrophoresis, Fourier transform infrared spectroscopy and intermolecular forces. Gelation properties were evaluated through rheology, water-holding capacity (WHC), texture and scanning electron microscopy (SEM).
Hydrophobic interactions and disulfide bonds played crucial roles in LSPG formation. Surface hydrophobicity of LSP increased from 484.3 to 1601 AU, but free sulfhydryl content of LSPG decreased from 1.35 (control) to 0.62 μmol g (300 W) with increasing ultrasound power (0-300 W). SDS-PAGE analysis showed that LSPG had eight distinct protein bands of 24, 28, 34, 53, 57, 62, 70 and 140 kDa, of which that at 28 kDa was dominant. Ultrasound treatment did not alter protein subunit composition. Additionally, a shift in secondary structure was observed, with an increase in β-sheet content from 22.21% to 23.48% and a decrease in α-helix content from 28.07% to 26.16%. Observation using SEM indicated that ultrasound-treated LSPG microstructure became denser and more uniform than control. Ultrasound treatment also enhanced the textural properties and WHC of LSPG. Among ultrasound powers of 60, 120, 180, 240 and 300 W, the highest storage modulus (1.61 × 10 Pa), hardness (2556.1 g), chewiness (2129.9), springiness (0.983), cohesiveness (0.864) and WHC (96.2%) were at 180 W.
This study provides a theoretical basis for applying LSPG in food processing. © 2025 Society of Chemical Industry.
莲子蛋白作为一种植物蛋白，具有较高的营养价值和功能价值，但凝胶化能力有限。因此，研究了超声处理对莲子蛋白凝胶（LSPG）结构和凝胶化特性的影响。通过表面疏水性、游离巯基、电泳、傅里叶变换红外光谱和分子间作用力分析结构特性。通过流变学、持水能力（WHC）、质地和扫描电子显微镜（SEM）评估凝胶化特性。
疏水相互作用和二硫键在LSPG形成中起关键作用。随着超声功率（0 - 300W）增加，LSP的表面疏水性从484.3增加到1601 AU，但LSPG的游离巯基含量从1.35（对照）降至0.62μmol g（300W）。SDS - PAGE分析表明，LSPG有24、28、34、53、57、62、70和140 kDa的八条明显蛋白带，其中28 kDa处的条带占主导。超声处理未改变蛋白质亚基组成。此外，观察到二级结构发生变化，β - 折叠含量从22.21%增加到23.48%，α - 螺旋含量从28.07%降至26.16%。SEM观察表明，超声处理的LSPG微观结构比对照更致密、更均匀。超声处理还增强了LSPG的质地特性和WHC。在60、120、180、240和300W的超声功率中，最高储能模量（1.61×10 Pa）、硬度（2556.1g）、咀嚼性（2129.9）、弹性（0.983）、内聚性（0.864）和WHC（96.2%）出现在180W。
本研究为LSPG在食品加工中的应用提供了理论依据。© 2025化学工业协会。
