Dynamics of the L-phenylalanine-d(8) has been here investigated by analyzing the H-2 NMR spin-lattice relaxation times of this selectively deuterium enriched amino acid diluted in the cesium pentadecafluorooctanoate/water (CsPFO/ H2O) lyotropic system both in the nematic (N-D(+)) and in the lamellar (L-D) phases. Information on the internal and overall molecular motions as well as on collective motions has been achieved by a global fitting procedure. The dynamic processes affecting this probe molecule reflect its particular conformational and interaction properties with respect to the lyotropic environment. The best reproduction of the experimental data is obtained by assuming free internal reorientations of the benzylic moiety, which results in diffusion constants of the same order of magnitude of the overall molecular spinning motion. Moreover, the contribution of collective motions (order director fluctuations and layer undulations) is estimated to be greater than that commonly observed by other techniques in lyotropic systems.