Wuyi　rock　tea　residue　is　rich　in　protein,　making　them　a　valuable　protein　source　for　producing　angiotensin　I-converting　enzyme　(ACE)　inhibitory　peptides.　In　the　present　research,　five　novel　ACE　inhibitory　peptides　were　isolated　and　identified　from　protein　hydrolysate　of　Wuyi　rock　tea　residue　using　Sephadex　G-15,　reversed　phase　high-performance　liquid　chromatography　(RP-HPLC),　and　quadrupole　time-of-flight　mass　spectrometry.　The　peptide　sequences　were　identified　as　FPFPRPP,　PPPRGP,　PFPRPPH,　LGHPW　and　LKFPDF,　with　IC50　values　ranged　from　0.271　mg/mL　to　1.018　mg/mL,　with　FPFPRPP　demonstrating　the　strongest　activity.　As　indicated　by　the　Lineweaver–Burk　plot,　FPFPRPP　was　a　mixed-type　inhibitor　against　ACE.　Molecular　docking　studies　further　confirmed　that　FPFPRPP　forms　five　hydrogen　bonds　with　residues　near　the　active　sites　of　ACE,　with　a　binding　energy　of　−10.5　kcal/mol.　Functional　assay　in　human　umbilical　vein　endothelial　cells　(HUVECs)　showed　that　FPFPRPP　significantly　upregulated　nitric　oxide　production　and　downregulated　reactive　oxygen　species　and　endothelin-1　levels　induced　by　angiotensin　II,　indicating　its　potential　antihypertensive　effect.　These　findings　highlight　Wuyi　rock　tea　residue　as　a　promising　source　of　ACE　inhibitory　peptides　and　suggest　FPFPRPP　could　be　developed　as　a　functional　food　ingredient　with　possible　applications　in　hypertension　management.　©　2025　The　Authors