Effect of glycation degree on the structure and digestion properties of ovalbumin: A study of amino acids and peptides release after in vitro gastrointestinal simulated digestion

Glycation can improve the functional properties of protein. However, in vitro and animal studies have shown that glycation induced lysine blockage and impaired protein digestibility. This study aimed to explore the effects of different glycation degree on the structure and digestive characteristics of ovalbumin. The results showed that glycation decreased the turbidity and hydrophobicity of the protein and changed the protein structure. Moreover, the results of in vitro simulated digestion revealed that glycation reduced the contents of essential amino acids and total amino acids after digestion. Glycation changed the amino acids and peptides release from the protein by resisting the digestion of digestive enzymes, especially trypsin. In conclusion, this work links glycation, protein digestibility, and the release of amino acids and peptides. This emphasizes the importance of the balance between improving properties and ensuring the digestibility of proteins during food processing.

Automated summary

This study investigates the effects of glycation on protein structure and digestive characteristics. The results show that glycation decreases the turbidity and hydrophobicity of protein and changes its structure. It also reduces the contents of essential amino acids and total amino acids after digestion.