A metabolomics approach to commercial protease enzyme hydrolysis of gourami meat.

The enzymatic hydrolysis of fish proteins has gained increasing attention to enhance nutritional quality and generate bioactive peptides with functional properties. In this study, we investigated the metabolomic consequences of gourami (Osphronemus goramy) meat hydrolysis using two commercial proteases, papain and bromelain. Hydrolysis was conducted over 0-240 min, and the resulting metabolites were profiled using ultra-performance liquid chromatography coupled with high-resolution mass spectrometry (UPLC-HRMS). Multivariate statistical analyses revealed a clear separation of hydrolysates by enzyme type and reaction time. Bromelain treatment induced more extensive proteolysis, yielding diverse array of amino acids, dipeptides (Valylproline, Leu-Gly-Pro), vitamins (pantothenic acid, biotin sulfone), and lipid derivatives (arachidonic acid, 2-hexenoyl carnitine). In contrast, papain hydrolysates were enriched in targeted bioactive peptides such as Tyr-Tyr, Trp-Phe, and Val-Tyr, known for antioxidant and angiotensin-converting enzyme (ACE) inhibitory activity. These findings highlight enzyme-specific biochemical pathways during fish protein hydrolysis and demonstrate how metabolomics can guide hydrolysate's tailored production.