81606-79-3 Purity
97%
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Bibi S, et al. Colloids and Surfaces A: Physicochemical and Engineering Aspects, 2026, 734, 139389.
This case study describes the experimental application of bromelain as a surface modifier to regulate protein corona formation on selenium nanoparticles (SeNPs). Uniform SeNPs (~50 nm) were synthesized via chemical reduction using sodium selenite and ascorbic acid, followed by bromelain functionalization to obtain BR-SeNPs with identical hydrodynamic diameters. To investigate corona formation, SeNPs and BR-SeNPs (0.2 g/L) were incubated with bromelain at graded concentrations (0.2-12 g/L) in phosphate-buffered saline (pH 7.4) for 24 h to form soft coronas, while subsequent centrifugation enabled isolation of hard coronas. Time-dependent adsorption was evaluated over 1-24 h at an optimized bromelain concentration. Quantification of unbound bromelain in supernatants enabled adsorption isotherm and kinetic analysis. Circular dichroism spectroscopy assessed structural integrity of adsorbed bromelain, while serum stability assays evaluated colloidal behavior. This experimental approach demonstrates bromelain's effectiveness in modulating corona architecture and enhancing nanoparticle stability for biomedical nanocarrier design.
Chen W-H, et al. Biomedicine & Pharmacotherapy, 2025, 190, 118376.
In this study, bromelain, a protease enzyme from pineapple stem, was applied to investigate its vascular protective effects by enhancing nitric oxide (NO) bioavailability in endothelial cells (ECs). Intracellular NO production was quantified using Griess's assay, while protein expressions of eNOS, AMPK, and autophagy-related markers were assessed by western blotting. Intracellular Ca²⁺ levels and L-arginine content were measured using conventional assay kits. Mechanistic studies employed pharmacological inhibitors targeting bradykinin receptor B2 (B2R) and TRPV1 to delineate the signaling pathway. Bromelain cleaved kininogen to release bradykinin, activating the B2R-TRPV1-Ca²⁺-AMPK-eNOS axis and autophagy-urea cycle-L-arginine pathway, synergistically increasing NO synthesis. In vivo, Matrigel plug assays demonstrated bromelain-induced angiogenesis, which was attenuated by inhibition of B2R, TRPV1, eNOS, or autophagy, highlighting the enzyme's experimental utility in cardiovascular research.
Jeong O, et al. Vaccine, 2026, 75, 128235.
Bromelain was applied to optimize the extraction of hemagglutinin (BHA) from cell culture-derived influenza viruses, including A/H3N2 (A/Texas/50/2012) and B/Victoria (B/Brisbane/60/2008) strains. Inactivated virus was first concentrated via ultracentrifugation and quantified using the Bradford assay. For neuraminidase (NA) depletion, A/H3N2 virus was treated with EDTA, 2-mercaptoethanol, and sequential bromelain digestion, whereas B/Victoria virus required trypsin pre-treatment prior to bromelain incubation. Post-digestion, ultracentrifugation separated bromelain-released BHA from residual viral proteins, and the supernatant was concentrated using molecular weight cutoff spin filters. NA removal was confirmed by SDS-PAGE, and final BHA preparations were concentrated 20-fold for sucrose gradient ultracentrifugation. This method enabled high-yield, highly purified BHA suitable for antiserum production, demonstrating bromelain's critical role in selective enzymatic cleavage and protein purification in viral antigen preparation.
Chelminiak-Dudkiewicz D, et al. Materials & Design, 2026, 261, 115374.
Bromelain nanoflowers (BNFs) were synthesized by incubating 2 mg bromelain with phosphate buffer (pH 7.4) and Cu(II) sulfate at 4 °C for 48 h, followed by centrifugation and drying at 30 °C. These BNFs were integrated into a chitosan-laminarin (CS-Lam) sponge crosslinked with 10 wt% dialdehyde laminarin. Polysaccharides were dissolved in 1 % acetic acid, combined, and stirred for 1 h at room temperature. Mannich base (0.2 g, dissolved in water/DMSO 30:70) was added and stirred for 1 h, followed by incorporation of 0.3 g BNFs. The mixture was cast in 96-well plates, frozen at -20 °C for 24 h, and freeze-dried at -54 °C under 0.05 mBar for 48 h, yielding a porous, functionalized sponge. This methodology demonstrates precise enzymatic functionalization and crosslinking for potential biomedical applications.
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