tPapain from ripe fruit and from papaya latex was characterised, in comparison with stem bromelain, under wine-likeconditions, with the aim to evaluate their applicability for white wine stabilization.Papains proteolytic activity was investigated, in McIlvaine buffer toward different synthetic peptide substratesand Bz-Phe-Val-Arg-pNA appeared the most suitable one for detecting proteolytic effect at wine average minimumpH (3.2). Kinetic parameters estimated in McIlvaine (as reference) and in tartaric buffer (mimicking wine medium),indicated a good hydrolytic activity toward selected substrate, at wine average minimum pH value (3.2) in spite ofethanol presence, in both mediums. Papain from latex showed a significantly higher and stable catalytic activityrespect to fruit papain and stem bromelain, retaining after 7 days, about 50% of its initial activity.