TY  - JOUR
AU  - LI, Feifan
AU  - CHI, Xiaojun
AU  - QIN, Yang
AU  - BU, Lingjin
AU  - SHI, Yuhang
PY  - 2025
TI  - Isolation Optimization and Mucoadhesion Analysis of B-Hordein
JO  - Food Science
SN  - 1002-6630
SP  - 79
EP  - 88
VL  - 46
IS  - 19
AB  - 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.
UR  - https://doi.org/10.7506/spkx1002-6630-20250421-167
DO  - 10.7506/spkx1002-6630-20250421-167