In terms of maximum extractable catalytic activity, sucrose synthase is the predominant sucrolytic enzyme in developing cotyledons of faba bean (Vicia faba L.). Although acid invertase activity is extremely low, there is significant activity of alkaline invertase, the majority of which is extractable only with high concentrations of NaCl. Calculations of potential activity in vivo indicate that alkaline invertase is the predominant sucrolytic enzyme from 50 days after anthesis onward. However, at almost all stages of cotyledon development analyzed, the maximum extractable catalytic activities of both enzymes is in excess of the actual rate of starch deposition. Two forms of alkaline invertase were identified in developing cotyledons. The major form has been purified to homogeneity, and antibodies have been raised against it. The native protein has a molecular mass of about 238 [plus or minus] 4.5 kD. It is apparently a homotetramer (subunit molecular mass 53.4 [plus or minus] 0.9 kD). The enzyme has a pH optimum of 7.4, an isoelectric point of 5.2, and a Km[sucrose] of 10 mM and is inhibited by Tris (50% inhibition at 5 mM) and fructose (30% inhibition at 10 mM). Bean alkaline invertase is a [beta]-fructofuranosidase with no significant activity against raffinose, stachyose, trehalose, maltose, or lactose.