Abstract
N-Succinyl amino acids (N-Suc-AAs) are increasingly recognized for their potential as taste-active compounds. However, research into the green synthesis, taste-enhancing properties, and mechanisms of N-succinyl-L-leucine (N-Suc-Leu) remains limited. This study employed an enzymatic synthesis method, catalyzed by protamex and pancreatin, to produce N-Suc-Leu, with its structure confirmed. Multiple sensory techniques demonstrated that N-Suc-Leu markedly enhanced the umami, saltiness, and kokumi intensity, and prolonged the duration of umami by 25%. Sigmoid curve analysis further revealed the synergistic enhancement of N-Suc-Leu on the perceptions of umami and saltiness. Molecular docking and dynamics simulations revealed that N-Suc-Leu could bind with T1R1, T1R3, TMC4, and CaSR, enhancing the sensations of saltiness, umami, and kokumi, and bound closely to these receptors without altering their overall conformation. These findings offered a systematic explanation of the potential and mechanism of enzymatically synthesized N-Suc-Leu in enhancing taste and provided novel insights into potential strategies for the development and innovation of taste enhancers and food flavors.
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