The gut is the major interface between insect and its environment constituting a very good target to control strategies. Until recently, studies of  protein digestion in insect gut have concentrated mainly on inicial phases of protein and peptide degradation by  endopeptidase activities. However, the products of these enzymes are large peptides, which must be further degraded by aminopeptidases, carboxypeptidases and dipeptidases before absorption. Here, we are studying carboxypeptidase and dipeptidase from T. molitor larvae. Distribution studies showed that T. molitor dipeptidase and carboxypeptidase are more active in the midgut content (88% and 87% of total activity, respectively), mainly occuring in the posterior midgut (185 mU/mg and 215 mU/mg, respectively). The partial purification of T. molitor dipeptidase and carboxypeptidase was attained using a combination of four chromatographic steps: an anion-exchange chromatography in Hitrap Q XL (Amersham/Bioscience), two anion-exchange chromatographies in Resource Q (Amersham/Bioscience) and a gel filtration chromatography in Superdex 75 (Amersham/Bioscience) using an AKTA system. The yield of this process is 130% for dipeptidase and 580% to carboxypeptidase . These high yield values may result from the separation of some inhibitor naturally present in samples. The optimum pH of dipeptidase is 7.6 and its molecular mass determined by SDS-PAGE is 38.6 kDa. T. molitor dipeptidase followed simple Michaelis-Menten kinetics with a Km value of 9.7 mM and a Vmax of 68,3 mU/mL using Gly-Leu as substrate.The optimum pH of carboxypeptidase is 7.4 and its molecular mass determined by SDS-PAGE is 31.6 kDa.