Thus, the disturbances of gut microbiota caused by the supplementation of PF and WF can improve gut health status. In conclusion, PF and WF exposure affects the urine and plasma metabolome of rats. The effects of PF and WF in the metabolic profiles are more pronounced in the urine than in the plasma, where many fiber diet-derived metabolites were measured. The consumption of PF and WF can promote antioxidant activity and change some common systemic metabolic processes, including lipid metabolism, glycogenolysis and glycolysis metabolism, energy metabolism, protein biosynthesis, and gut microbiota metabolism. PF can also decrease bile acid metabolism. The metabolic profiles of the rats exposed to PF and WF can improve the present understanding of the metabolic status of PF and WF. This research also contributes in defining the effects of metabolic modifiers and in refining nutritional requirements to provide better nutritional support for growth and health. This study emphasizes the potential metabolomic strategy in the assessment of nutritional interventions in a mammalian system. To the best of our knowledge, this is the first study to systematically identify the expressed metabolites in urine and plasma from PF and WF supplementation. Future studies may be directed toward a mechanistic understanding on the effects of PF and WF in animal tissue intermediary metabolism. The mammalian target of rapamycin is a highly evolutionarily conserved protein kinase that plays a key role in the integration of growth factor, nutrient and energy status of the cells. mTOR R428 functions as a catalytic subunit in two distinct multiprotein complexes, mTOR complex 1 and mTORC2. mTORC1, characterized by the regulatory subunit Raptor, controls at least two regulators of protein synthesis, the 40S ribosomal protein subunit S6 kinase and the eukaryotic translation initiation factor 4E -binding protein 1, AZ 960 referred as 4E-BP1. The heterodimer of the tumor suppressor TSC2 and TSC1 represses mTORC1 signaling by acting as the GTPase-activator protein for the small G protein Rheb, a potent activator of mTORC1 signaling in its GTP-bound state. Phosphorylation of TSC2 by Akt and/or ERK/p90RSK suppresses its GTPase activating activity towards Rheb, leading to mTORC1 activation. mTORC1 is acutely and allosterically inhibited by rapamycin through binding to FKBP12. mTORC2, characterized by Rictor, is not inhibited by short-term treatment with this agent and phosphorylates several AGC protein kinases, including Akt at Ser473. The mTORC1 pathway plays a key role in insulin/ IGF receptor signaling and is aberrantly activated in many cancers, including pancreatic ductal adenocarcinoma, one of the most lethal human diseases.