The objective of this study was the research of novel and inexpensive sources of polysaccharides degrading enzymes such as amylases and glucanases from local plants in order to justify their biotechnological applications. The isolation of two l3-amylases and an endo-1,3-ß-D-glucanase was reached using common protein purification methods such as buffer extraction, ammonium sulfate fractionation, ionexchange and gel filtration chromatographies. The methods used were simple and easily reproducible, suggesting the possibilfty of large-scale production. ln the crude extract of Curculigo pilosa tuber, only ß-amylase was detected as starch degrading enzyme and its activity was approximately 282 Uig of fresh material. The enzyme was purified 100 fold with 38 % yield and giving a final specifie activity of 4860 U/mg of the purified protein. The enzyme was determined to be a monomer protein of 64 kDa molecular mass, its isoelectric point was about 4.2 and it was shown to be thermostable enzyme possessing the ability to hydrolyze raw starches. ln the bulb of G/adiolus klattianus both a-amylase and ß-amylase activities have been detected. However, the ß-amylase was the major starch degrading enzyme (92 %), and its activity was about 440 U/g of fresh materia/, value similar with that of the l3-amylase from barley malt (400-500 UIg). The enzyme was isolated (47 fold) from the bulb by the mean of simple purification techniques and partially characterized. The final purification recovery was up to 75 % giving a specifie activity of 2360 U/mg. The enzyme is a dimeric protein with a molecular mass of 72 kDa. The crude extract of the leaves of Boscia senegalensis contained a multienzymic complex of polysaccharide degrading enzymes. Activities of a-amylase, ß-amylase, 13-(1 ~3, 1~)-exo-glucanase and ß-(1 ~3)-endo-glucanase were respectively equal to 15; 207, 11 and 35 U/g of fresh plant materia/. The endo-1,3-ß-D-glucanase (EC: 3.1.1.39), a cell wall degrading enzyme, has been purified. The typical yield of the purification was 57 % with 203 purification fold and a final specifie activity of 549.2 U/mg. The enzyme is a basic protein (pl 10.3), no glycosilated and was able to hydrolyze soluble substrate (laminarin), insoluble substrate (yeast cell wall 13-glucan) as weil as to inhibit the growth of living yeast ce/ls (Saccharomyces cerevisiae). These properties may be related to the traditional use of this species for cereal protection against microbial or insect invasions. Polysaccharide degrading enzymes such as amylases and glucanases are nowadays at the center of food process engineering, evolving enormous applications in biotechnology. These enzymes are especially used in the production of improved nutritive value foods (weaning flour), high maltose-containing syrup and in brewery. The isolated and characterized enzymes in the present work, especially the 13amylases could be used for sorghum beer manufacture to improve its value, because the malted sorghum lacks this enzyme. It could be one way to improve the economical value of a local products widely consumed in whole West African area. Furthermore this could be also a way to enhance the value of novel sources of amylases and glucanases from local higher plants. In addition, more purified and low cost enzymes will have interesting future for biotechnological applications such as genetic engineering, enzyme immobilization and analytical purposes.