Related Experiment Video
Updated: Jan 12, 2026

High-throughput, Microscale Protocol for the Analysis of Processing Parameters and Nutritional Qualities in Maize Zea mays L.
Published on: June 16, 2018
Zein-glutelin interactions and physicochemical properties of protein complex during corn post-harvest ripening
Jinying Zhu1, Jiannan Yan1, Mingzhu Zheng1
1College of Food Science and Engineering, Jilin Agricultural University, Changchun, Jilin 130118, China; National Engineering Research Center for Wheat and Corn Deep Processing, Changchun, Jilin 130118, China.
Abstract:
Proteins in corn mainly consist of zein and glutelin, existing in the form of complexes. Corn post-harvest ripening has a significant impact on the zein-glutelin interaction, which affects the structure and properties of protein complex. The changes in interaction, structure and physicochemical properties of zein-glutelin complex during corn post-ripening were investigated. The structural stability of the zein-glutelin complex was mainly maintained by hydrophobic interactions, hydrogen bonds, and disulfide bonds. After post-ripening at 15 °C for 45 days and 25 °C for 30 days, the complex protein subunits degraded, the α-helix transformed into β-sheet, and the hydrophobic interactions and disulfide bonds increased. Furthermore, both more ordered β-structure at 15 °C and higher disulfide bond at 25 °C formed protein rigid aggregates with a uniform and orderly distribution, which suggested a stronger zein-glutelin interaction, resulting in lower solubility and higher water- and oil-holding capacity of the protein complex.
More Related Videos
Related Concept Videos
Protein Folding Quality Check in the RER
Introduction to Plant Diversity

