A hydrogen-terminated Si (111) surface was modified to form an aminoterminated monolayer for immobilization of streptavidin. Cleavage of an N-(omega-undecylenyl)-phthalimide covered surface using hidrazine yields an amino group-modified surface, which serves as a substrate for the attachment of biotin and subsequently streptavidin. We used surface analytical techniques to characterize the surface and to control the course of functionalization before the immobilization of streptavidin. To confirm the presence of the streptavidin Texas red on the surface two powerful techniques available in a standard biochemical laboratory are used, Fluorescence Microscopy and MALDI-TOF that allow us to detect and determine the immobilized streptavidin. This work provides an avenue for the development of devices in which the exquisite binding specificity of biomolecular recognition is directly coupled to a biosensor. In addition, we have demonstrated that MALDI-TOF and fluorescence microscopy are useful techniques for the characterization of silicon functionalized surfaces.