Masticatory or M-MyHC (Myosin Heavy Chain) is a myosin subunit isoform with expression restricted to muscles derived from the first branchial arch, such as jaw closer muscles, with pronounced inter-species variability. Only sparse information is available on the contractile properties of muscle fibers expressing M-MyHC (M fibers). In this study we characterized M fibers isolated from the jaw closer muscles (temporalis and masseter) of two species of domestic carnivores, the cat and the dog, in comparison with fibers expressing slow or fast (2A, 2X and 2B) isoforms. In each fiber, during maximally calcium-activated contractions at 12°C, we determined isometric specific tension (Po), unloaded shortening velocity (Vo) with the slack test protocol and the rate constant of tension redevelopment (k_TR) after a fast shortening-relengthening cycle. At the end of the mechanical experiment, we identified MyHC isoform composition of each fiber with gel electrophoresis. Electrophoretic migration rate of M-MyHC was similar in both species. We found that in both species the kinetic parameters Vo and k_TR of M fibers were similar to those of 2A fibers, whereas Po values were significantly greater than in any other fiber types. The similarity between 2A and M fibers and the greater tension development of M fibers were confirmed also in mechanical experiments performed at 24°C. Myosin concentration was determined in single fibers and found not different in M fibers compared to slow and fast fibers, suggesting that the higher tension developed by M fibers does not find an explanation in a greater number of force generators. Thus, the specific mechanical characteristics of M fibers might be attributed to a diversity in cross bridge kinetics.