@article{LI2025, 
author = {Feifan LI and Xiaojun CHI and Yang QIN and Lingjin BU and Yuhang SHI},
title = {Isolation Optimization and Mucoadhesion Analysis of B-Hordein},
year = {2025},
journal = {Food Science},
volume = {46},
number = {19},
pages = {79-88},
keywords = {B-hordein, pectin, selective binding behavior, component isolation, mucoadhesion},
url = {https://www.sciopen.com/article/10.7506/spkx1002-6630-20250421-167},
doi = {10.7506/spkx1002-6630-20250421-167},
abstract = {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.}
}