The aim of this work was to produce wonderful cola protein hydrolysate fractions with in vitro antioxidant properties coupled with blood pressure-reducing ability when orally administered to spontaneously hypertensive rats (SHRs). Wonderful cola protein isolate (WCI) was hydrolyzed with pancreatin to produce a hydrolysate (WCH), which was subjected to ultrafiltration separation using 1, 3, 5, and 10 kDa molecular weight cut-off membranes to obtain <1, 1–3, 3–5 and 5–10 kDa peptide fractions, respectively. The <1 and 1–3 kDa fractions had higher contents of arginine when compared to the 3–5 and 5–10 kDa peptides. The WCH and <1 kDa peptide fraction had significantly (p < 0.05) better DPPH radical scavenging (55–67%) and metal chelation (83–93%) activities but lower hydroxyl radical scavenging power (10–32%) than the WCI (46, 46 and 63%, respectively). The <1 kDa had significantly (p < 0.05) higher in vitro inhibition (80%) of angiotensin converting enzyme (ACE) activity while the 5–10 kDa was the most active inhibitor (90%) of renin activity. All peptide fractions so produced had better systolic and diastolic blood pressure-lowering effects than WCH and WCI. However, the <1 kDa fraction produced significantly (p < 0.05) stronger systolic (−33 mmHg) and diastolic (−30 mmHg) blood pressure reductions 6 h after oral gavage to SHRs. Thus, wonderful cola proteins contain encrypted bioactive peptides that may be used to formulate antioxidant and antihypertensive products.