In　this　study,　we　attempted　to　prepare　novel　angiotensin　I-converting　enzyme　inhibitory　(ACEI)　peptides　from　Tie　Guanyin　tea　residue　protein　(TTRP).　Different　proteases　were　used　to　hydrolyze　TTRP　to　prepare　ACEI　peptides,　neutral　protease　and　alkaline　protease　hydrolysates　exhibited　higher　ACEI　activity　and　was　chosen　in　further　hydrolysis　treatment.　Response　surface　methodology　(RSM)　was　used　to　optimize　the　enzymatic　condition,　and　the　results　indicated　that　the　optimal　conditions　of　enzymatic　hydrolysis　were:　4%　(w/v)　of　TTRP　in　water　was　hydrolyzed　with　3500　U/g　neutral　protease　at　50　degrees　C　and　pH　6.5　for　2.5　h　in　the　first　step　and　then　with　5000　U/g　alkaline　protease　at　50　degrees　C　and　pH　10.0　for　3　h　in　the　second　step.　Under　the　optimum　condition,　the　ACE　inhibitory　rate　of　the　final　products　was　88.45%　+/-　0.45%　at　the　concentration　of　1.0　mg/mL.　Moreover,　ACEI　peptides　derived　from　TTRP　showed　good　stability　under　different　temperatures,　pHs,　metal　ions　and　gastrointestinal　digestion.　These　results　indicated　that　the　TTRP　has　potential　to　be　used　for　preparing　ACEI　peptides.