Isolation Optimization and Mucoadhesion Analysis of B-Hordein
2025
LI Feifan, CHI Xiaojun, QIN Yang, BU Lingjin, SHI Yuhang
This study characterized the selective complex coacervation between hordein and pectin to confirm the selective binding behavior of different hordein components in order to develop a low-cost, readily scalable protein isolation method. Besides, the isolation of B-hordein was optimized and the adhesion properties of different components were also evaluated. The results demonstrated that B-hordein, the major component of hordein, preferentially bound to two types of pectin to form coacervates. High-methoxyl pectin (HMP) exhibited weaker binding affinity to B-hordein, as evidenced by the fact that the supernatant of the complex system contained a significant amount of B-hordein. In contrast, low-methoxyl pectin (LMP) showed stronger binding affinity to B-hordein. Protein spectrum analysis revealed that high-purity B-hordein could be obtained by collecting the coacervates from the Hordein/LMP1:1 system. Adjusting the pH enabled the secondary separation of B-hordein from LMP in the coacervates, with a B-hordein recovery of 65.29%. Meanwhile, B-hordein-based composites exhibited the best adhesion performance. This study provides a theoretical foundation for promoting the development of protein isolation technologies.
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