This is a continuation of previous immobilization studies with an extracellular amylase from the exo-1 mutant of Neurospora crassa. This mutant is characterized by hyperproduction of amylases and invertase. The exo-1 amylase is easily immobilized on agarose supports. Here were compared different matrices with different crosslink concentration: 4 BCL and 10 BCL agarose gels for the production of glyoxyl-agarose derivatives. The 4BCL exhibits lower crosslink degree than 10BCL agarose, thus, in this case, possible diffusion problems of the starch across the supports could be reduced. Also were tested two epoxy supports for amylase immobilization, using Eupergit and Sephabeads supports. The activities of the different derivatives obtained, on two substrates - maltose and starch – were compared. Either glyoxyl agarose support prepared with 4BCL or 10BCL agarose had diffusion problems when the starch substrate was used to measure the immobilization course, and the 10BCL derivative was detached when thermal stability studies were carried out. Eupergit derivatives were better than Sephabeads preparations. In a comparison between two of the best derivatives (glyoxyl 10BCL and Eupergit derivates) both of them were stable at 60ºC, maintaining 100% of activity for up to 12 hours, while the soluble amylase preserved only about 12% of initial activity. These two exo-1 amylase derivatives exhibited differences when the temperature of incubation was 70ºC. At 70ºC the glyoxyl 10BCL amylase derivative was more thermally stable, preserving about 30% of initial activity.