Assessment of bioactive compound variations and in-vitro and in-vivo antioxidant activity in edible fresh and processed Bambusa nutans shoot through FTIR, GC/MS and HPLC analyses.

This study explores the impact of processing techniques on the bioactive composition and antioxidant properties of Bambusa nutans shoots, an underutilized superfood. Boiling resulted in a significant reduction of total phenols (39.52%), flavonoid (8.07%), and tannin (27.77%). Conversely, fermentation increased total phenols (25.92%), tannin (34.72%), and phytosterol (75.39%). Antioxidant activities were notably higher in fermented-shoots, as indicated by DPPH and FRAP assays, and in-vivo experiments demonstrated increased GSH (31.85%) and decreased LPO levels (11.12%) post-administration of fermented-shoots extract. Spectral analysis revealed an increased diversity of compounds in fermented shoots, with GC/MS identifying hexadecane-1-ol in significantly higher proportions and 11 characteristic bands in FTIR spectra. HPLC analysis demonstrated changes in phenolic acids and flavonoid content, with fermentation enhancing 3,4,5-trihydroxybenzoic acid, 4'-hydroxycinnamic acid, benzene-1,2-diol, and luteolin contents. This study underscores the dynamic nature of B. nutans shoots, highlighting the potential for enhanced bioactivity and antioxidant properties through fermentation, offering promising avenues for culinary and pharmaceutical developments.

Proteomic response of mouse pituitary gland under heat stress revealed active regulation of stress responsive proteins.

The mapping of tissue proteomes can identify the molecular regulators and effectors of their physiological activity. However, proteomic response of a mammalian tissue against heat stress (HS) particularly of the pituitary gland has not yet been resolved. The proteomic response of the mouse pituitary gland against HS at 40oC was evaluated by iTRAQ. We found that, HS actively regulates stress-related proteins. Among 375 differentially expressed proteins, 26 up and 46 downregulated proteins were found as stress responsive proteins. Two proteins belonging to the HSP70 and one to HSP90 family were found upregulated. Meanwhile, the expression of HSP90α (Cytosolic), HSP60, and HSP84b were observed to be downregulated. A neuroprotective enzyme Nmnat3 was observed to be significantly upregulated. Three proteins related to the intermediate filament (IF) proteins (lamins, vimentin and keratins) were also found to be upregulated. We reported, an association between the IF proteins and HSPs as a biological marker of HS. The expression of Apo A-IV was upregulated and might be one explanation for low food intake during HS. Our findings indicated that, differentially expressed proteins might be played important roles in combating HS.