Present study ascribe multifunctional characterstics of moth bean bioactive peptides obtained by enzymatic hydrolysis of seed proteins. Alcalase derived protein hydrolysates were further subjected to fractionation by ultrafiltration and gel filtration chromatography. Moth bean peptide (MBP) fractions of < 3 kDa was characterised for in vitro antihypertensive, antioxidant, antidiabetic, antiproliferative, DNA damage inhibition and antibiofilm activities. It reports high ACE-inhibition activity (IC50 =9.51 µg/mL) and exhibit significant stability on a wide range of pH, temperature, and gastrointestinal proteases. The peptide fraction displayed noteworthy DPPH radical-scavenging activity (IC50 =155.05 µg/mL), ABTS radical-scavenging activity (IC50 =158.88 µg/mL), and Fe2+ chelating activity (IC50 =71.59 µg/mL). Additionally, it showed inhibition against α-amylase (IC50 =126.90 µg/mL) and α-glucosidase (IC50 =121.69 µg/mL). Further, peptide fraction effectively inhibited the growth of carcinoma breast cells MCF-7 (IC50 =46.93 µg/mL). It showed protective effects against DNA damage. Moreover, MBP fraction significantly restricted the biofilm formation of Pseudomonas aeruginosa (IC50 =86.45 µg/mL). Overall, the MBP fraction provides value addition to moth bean protein for its use in nutraceutical formulations.