Identification of Novel Umami Peptides from Yeast Protein through Enzymatic, Sensory, and In Silico Approaches

This study aimed to rapidly develop
novel umami peptides using
yeast protein as an alternative protein source. Yeast protein hydrolysates
exhibiting pronounced umami intensity were produced using flavorzyme
under optimum conditions determined via a sensory-guided response
surface methodology. Six out of 2138 peptides predicted to possess
umami taste by composite machine learning and assessed as nontoxic,
nonallergenic, water-soluble, and stable using integrated bioinformatics
were screened as potential umami peptides. Sensory evaluation results
revealed these peptides exhibited multiple taste attributes (detection
threshold: 0.37 ± 0.10–1.1 ± 0.30 mmol/L), including
umami. In light of the molecular docking outcomes, it is inferred
that hydrogen bond, hydrophobic, and electrostatic interactions enhanced
the theoretically stable binding of peptides to T1R1/T1R3, with their
contributions gradually diminishing. Hydrophilic amino acids within
T1R1/T1R3, especially Ser, may play a particularly pivotal role in
binding with umami peptides. Future research will involve establishing
heterologous cell models expressing T1R1 and T1R3 to delve into the
cellular physiology of umami peptides. Peptide sequences (FADL, LPDP,
and LDIGGDF) also had synergistic saltiness-enhancing effects; to
overcome the limitation of not investigating the saltiness enhancement
mechanism, comprehensive experiments at the molecular and cellular
levels will also be conducted. This study offers a rapid umami peptide
development framework and lays the groundwork for exploring yeast
protein taste compounds.