Protein digestibility and ACE inhibitory activity of fermented flours in older adults and standard gastrointestinal simulation

Consumption of essential amino acids responsible for muscle protein synthesis is important in preventing sarcopenia among older individuals. This population may experience gastrointestinal disorders that inhibit protein digestibility, making it crucial to address. Therefore, solid-state fermentation (SSF) using Pleurotus ostreatus and air drying has been suggested as a means of improving the protein digestibility of lentils and quinoa. SSF combined with air drying at 70 degrees C resulted in a slight increase in protein hydrolysis compared to unfermented samples. SSF was found to boost the proportion of small peptides to 35 %. Following digestion, SSF and drying yielded bioactive peptides of 1400 and 450 Da, with a range of 11 % to 28 %, respectively, and peptides < 190 Da making up 60 % of the total. SSF promoted valine, leucine, and isoleucine generation; however, hot air drying reduced free amino acids due to the amino acid-reducing sugar bonding but was never lower than the initial content of its unfermented counterpart. Furthermore, SSF and drying at 70 degrees C improved the release of hydrophobic amino acids (>70 mg/g dry basis) and negatively charged amino acids (>20 mg/g dry basis) in lentils during digestion. The SSF samples exhibited lower angiotensin converting enzyme (ACE) inhibitory activity, <= 35 %, compared to unfermented flours after digestion. However, the ACE inhibitory activity increased in SSF-dried samples, in part because of melanoidins generated during drying. Finally, lower values of protein digestibility and thus smaller peptides, amino acid profile, and ACE inhibitory activity of fermented flours were found in the older adult digestion model.