Exploring how enzymatic deamidation enhances rice protein’s functionality through molecular structural changes, impacting solubility, thermal stability, and food application potential.

The significant improvement in functional properties of rice protein after enzymatic deamidation is related to changes in its molecular microstructure. The changes in the ultrastructure, intermolecular forces and degree of polymerization of rice glutenin molecules after deamidation were studied through scanning electron microscopy (SEM) analysis, disulfide bond content determination and differential scanning calorimetry (DSC). The results show that the ultrastructure of rice gluten particles gradually loosens as the degree of deamidation increases; after deamidation, some intramolecular disulfide bonds are rapidly reduced, but enzymatic deamidation will not affect the disulfide bonds within the peptide chain; DSC spectrum Analysis showed that protein thermal stability and degree of polymerization were reduced after deamidation.

Introduction: The Significance of Rice Protein Enhancement

The exploration of methods to improve the functional properties of plant-based proteins is pivotal in addressing the growing demand for sustainable and nutritious food sources. This study focuses on rice protein, a critical component of global food security, and investigates how enzymatic deamidation influences its functional characteristics by altering its molecular microstructure. The comprehensive analysis utilizes scanning electron microscopy (SEM), disulfide bond content determination, and differential scanning calorimetry (DSC) to provide insights into the structural modifications and their implications on protein functionality.

Methodology: Investigating Structural Changes

Rice protein, particularly rice glutenin, plays a significant role in the nutritional and textural properties of rice-based products. However, its potential is often limited by inherent structural constraints. Enzymatic deamidation emerges as a transformative process that modifies the amino acid side chains of proteins, thereby altering their physicochemical properties. This study meticulously examines the effects of enzymatic deamidation on the ultrastructure, intermolecular forces, and degree of polymerization of rice glutenin molecules.

Findings: Ultrastructure and Disulfide Bond Alterations

SEM analysis reveals that the ultrastructure of rice gluten particles undergoes significant loosening with increasing degrees of deamidation. This structural relaxation potentially enhances the protein’s solubility and interaction with other molecules, facilitating improved functionality in food applications. The investigation into disulfide bond content unveils that enzymatic deamidation leads to a rapid reduction in some intramolecular disulfide bonds, impacting the protein’s functional behavior while preserving its primary structure and nutritional value.

Implications: Thermal Stability and Polymerization

DSC spectrum analysis further elucidates the impact of deamidation on protein thermal stability and degree of polymerization. The findings indicate a reduction in both attributes post-deamidation, pointing to a more flexible and less aggregated protein structure. This modification may enhance the protein’s heat sensitivity and its ability to integrate into food systems requiring thermal processing.

Conclusion: Enhancing Plant-Based Protein Functionality

In conclusion, the study provides compelling evidence that enzymatic deamidation significantly improves the functional properties of rice protein by inducing changes in its molecular microstructure. These findings not only deepen our understanding of protein structural dynamics but also highlight the potential of enzymatic deamidation as a novel approach to improving the functional attributes of plant-based proteins, offering a promising avenue for enhancing the quality and sustainability of food products in an increasingly plant-forward global diet.

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Original research was done by Liu Yongle, Wang Faxiang, Zhou Xiaoling, Li Xianghong, Yu Jian, Wang Jianhui

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