Related Experiment Video
Updated: May 6, 2026
Efficient Purification of Elastin-Like Polypeptides (ELPs) from E. coli Using an Organic Solvent-based Extraction and Precipitation Method
Published on: January 9, 2026
Extraction methods dictate pumpkin seed protein structure and thereby govern the linear and nonlinear rheological
Fei Su1, Zhitong Zhou2, Jingru Wu1
1Science Center for Future Foods, Jiangnan University, Wuxi 214122, China; School of Food Science and Technology, Shandong Agricultural University, Tai'an 271018, China.
Abstract:
This study prepared PSPI using mild extraction (PSPI1) and conventional alkaline extraction-isoelectric precipitation (PSPI2), respectively. The omission of the isoelectric precipitation step during mild extraction preserved the native protein conformation, as the acid precipitation process caused loss of soluble albumins. Consequently, PSPI1 significantly reduced interfacial tension relative to PSPI2. In terms of HIPEs, PSPI1 exhibited better HIPEs formation ability and smaller droplet size. Furthermore, rheological analysis revealed that PSPI1-HIPEs exhibited elevated apparent viscosity and higher storage moduli under identical pH conditions, while demonstrating optimal oral lubricity at pH 3.0. However, large amplitude oscillatory shear (LAOS) indicated enhanced deformation resistance in PSPI2-HIPEs at pH 6.0, which may be associated with low solubility and the aggregation of undissolved protein particles, thereby contributing to a stronger bulk network. In conclusion, mild extraction could preserve the native protein conformation of PSPI, thereby enhancing the performance of HIPEs and offering perspectives for alternative protein development.
