Ribonucleoprotein (RNP) bodies that exhibit liquid-like internal dynamics facilitate processes such as rRNA transcription and processing, while RNP bodies with gel- or solid-like dynamics (e.g., P-bodies and stress granules) facilitate processes such as mRNA storage. Recently, it has been shown that bacterial RNA degradosomes can assemble into phase-separated condensates called bacterial ribonucleoprotein bodies (BR-bodies). In Caulobacter crescentus, BR-bodies are dynamic and exhibit liquid-like properties, consistent with their mRNA degradation activity. However, under cell stress, the number of BR-bodies increases significantly to give C. crescentus cells a fitness advantage. Furthermore, upon entrance into the stationary phase, an increased number of BR-bodies correlates with a slowdown in the mRNA decay rate. These results raise the question of whether BR-bodies can facilitate mRNA storage. Here, we use bulk fluorescence imaging and live-cell single-molecule tracking to probe the dynamics of the ribonuclease RNase E, the central scaffold of the BR-body. We found that during stationary phase, BR-bodies are stable for longer have a longer compared to exponential phase. Consistent with these results, the residence time of RNase E in BR-bodies in stationary phase cells is at least two orders of magnitude longer than in exponential phase cells. Finally, we measured the size and abundance of BR-bodies during both growth stages and found that during stationary phase, BR-bodies are smaller and more abundant, which suggests that the condensate phase is not conducive to fusion. Together, our data shows an increased stability of RNAse E in the stationary phase, which may indicate a gel or solid phase transition. Furthermore, we anticipate our single-molecule measurements will provide a foundation for probing the mechanical properties of subcellular compartments in living bacteria.