Ephemeral gels, called Enzgels, successively undergo sol-gel and then gel-sol transition under the action of two antagonistic enzymes, transglutaminase and protease. Molecular and macroscopic properties of Enzgels are directly dependent on the enzymatic activities and their ratios. This work studies the characteristics of Enzgels according to the specificity of three different proteases: thermolysin, trypsin, and collagenase. The experiments are conducted using three types of gelatin networks, one created only by triple helices, one only by covalent bonds, and the last network by both triple helices and covalent bonds. Rheology and polarimetry measurements show that the evolution of Enzgels is directly dependent on the specificity of the protease used. Moreover, gelatin network conformation has different influences according to this proteolytic specificity. Collagenase is not very sensitive to gelatin conformation, whereas trypsin is very limited by the presence of covalent bonds. This study considerably expands the knowledge of Enzgel properties.