Virtual screening, activity evaluation, and stability of pancreatic lipase inhibitors in the gastrointestinal degradation of nattokinase.

ABSTRACT: Nattokinase is an alkaline serine protease secreted by natto during fermentation. Despite its good thrombolytic effect, it is intolerant to gastrointestinal conditions and is easily digested and degraded into polypeptides, oligopeptides, and amino acids. However, whether these peptides inhibit fat-digesting enzymes and other biological activities remains unknown. To explore the bioactivity of peptides produced through nattokinase degradation, nattokinase was subjected to simulated digestion in the gastrointestinal tract, and 41 small peptides were obtained through the enzymolysis of gastric enzymes, pancreases, and chymotrypsin. Four pancreatic lipase (PL) inhibitory peptides (SW, ASF, GAY, and PGGTY) were selected based on their activity scores, water solubility, and toxicity predictions.

SUBMITTER: Yang L 

PROVIDER: S-EPMC10835311 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature