Exploring acid deamidation’s effects on cereal proteins, highlighting improved solubility, digestibility, and structural changes for enhanced nutritional value.

Deamidation treatment is a method of protein modification. After deamidation, the physical, chemical and nutritional properties of the protein will change. This experiment studied the effect of acid deamidation treatment on the in vitro digestibility of rice, wheat, and corn protein, and explored deamidation from the aspects of protein solubility, surface hydrophobicity, sulfhydryl and disulfide bond content, and ultrastructure and other physical and chemical properties. Mechanism of action affecting in vitro digestibility. The test results show that as the degree of deamidation increases, the mutual conversion between sulfhydryl groups and disulfide bonds of rice protein, wheat protein and corn protein is not obvious (P<0.05), and the contents of the two remain basically unchanged; the three cereals The solubility of the protein gradually increases under the conditions of the optimal pH of pepsin of 1.5 and the optimal pH of trypsin of 7; the surface hydrophobicity of the protein gradually decreases with the increase of deamidation degree; the in vitro digestibility also changes from the original 66.5% to 66.5%, respectively. 79.5% and 78.5% increased to 79.5%, 89.0%, and 89.2%. The ultrastructure changed from the original dense aggregation to porous and loose, which is more conducive to protein digestion.

Study Overview: Examining Acid Deamidation on Cereal Proteins

Deamidation treatment, a method of protein modification, has drawn considerable attention in the realm of food science due to its impact on the physical, chemical, and nutritional properties of proteins. This professional discourse delves into an experimental study examining the effects of acid deamidation on the in vitro digestibility of proteins derived from rice, wheat, and corn. By exploring several key aspects—protein solubility, surface hydrophobicity, sulfhydryl and disulfide bond content, and ultrastructure—the research provides valuable insights into the mechanism by which deamidation influences protein digestibility.

Stability of Sulfhydryl and Disulfide Bonds Post-Deamidation

The study meticulously investigated the changes in physical and chemical properties resulting from acid deamidation treatment. Notably, the results indicated that the degree of deamidation does not significantly alter the interconversion between sulfhydryl groups and disulfide bonds in rice, wheat, and corn proteins (P<0.05). This observation suggests that the content of these chemical groups remains essentially unchanged post-deamidation, challenging previous assumptions about the role of these bonds in protein digestibility.

Enhanced Solubility and Its Significance for Protein Digestibility

Further examination revealed a gradual increase in the solubility of the proteins from the three cereals under optimal pH conditions for pepsin (pH 1.5) and trypsin (pH 7). This finding is of paramount importance, as enhanced solubility is closely linked to improved digestibility, suggesting that deamidation facilitates a more efficient breakdown of proteins by digestive enzymes.

Reduction in Surface Hydrophobicity Through Deamidation

Moreover, the study observed a consistent decrease in surface hydrophobicity with an increase in deamidation degree. This alteration in hydrophobicity is crucial because it influences protein interactions and stability, potentially making proteins more accessible to digestive enzymes.

Significant Improvements in In Vitro Protein Digestibility

In terms of in vitro digestibility, the research presented compelling evidence that deamidation markedly improves the digestibility of rice, wheat, and corn proteins. Specifically, digestibility values increased from 66.5%, 79.5%, and 78.5% to 79.5%, 89.0%, and 89.2%, respectively. Such improvements in digestibility are significant, highlighting deamidation’s potential to enhance the nutritional value of cereal proteins.

Alterations in Protein Ultrastructure Favoring Digestion

A critical aspect of this study is the examination of changes in the ultrastructure of proteins post-deamidation. The transition from a dense aggregation to a more porous and loose structure indicates a profound alteration in the physical makeup of the proteins, making them more amenable to enzymatic action and thereby facilitating digestion.

Conclusion: The Potential of Deamidation in Food Science

In conclusion, this comprehensive study sheds light on the multifaceted impacts of acid deamidation treatment on cereal proteins, revealing significant enhancements in solubility, digestibility, and structural properties. These findings underscore the potential of deamidation as a promising approach to improving the nutritional quality and functionality of plant-based proteins. As the demand for sustainable and nutritious food sources continues to grow, such innovations in food science are pivotal, offering new avenues for enhancing the health benefits of plant-derived proteins.

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Original research was done by Long Pei

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