ENHANCING SOLUBILITY AND α-GLUCOSIDASE INHIBITION OF MANGOSTEEN PEEL EXTRACT VIA AMORPHOUS SOLID DISPERSION: A COMPARATIVE STUDY OF SOLVENT EVAPORATION AND FLUIDIZED BED DRYING METHODS

Diabetes mellitus-a disorder of glucose handling in the body-is appearing more frequently in clinic and registry alike. Public-health officials now label it as at once familiar and alarming. Among the clinical varieties, type 2 diabetes mellitus (T2DM) carries the heaviest demographic load and, perhaps not coincidentally, the bulk of research sponsorship. Most therapeutic playbooks still default to drugs that stall carbohydrate breakdown once the food reaches the intestines. At the end of that enzymatic assembly line sits the α-glucosidase molecule itself; without its action, oligosaccharides remain stranded, unprocessed. Pharmaceutical scientists have filed acarbose and miglitol under the same functional umbrella, though abdominal discomfort and spotty systemic absorption keep the prescriptions honest. The side effects have nudged inventors toward plant extracts, prodding them to browse the rainforest rather than the test-tube archive. One contender, α-mangostin from the queen-sized mangosteen fruit, nips at the enzyme but refuses to dissolve at anything resembling room temperature. Solid-dispersing it in polyvinylpyrrolidone (PVP) swaps the crystalline cage for a shapeless cloud and, by anecdotal report, boosts the apparent solubility tenfold or more. Laboratory batches usually employ flush-and-evaporate glassware, yet fluid-bed drying (FBD) is also in the mix when significance demands industrial scale. Both routes tweak the particle outline, and those subtle silhouettes end up steering bioavailability toward one wall or the other. To pin down the correlation, we decided to measure enzyme inhibition side-by-side with solubility gains from each processing strategy. Solubility experiments under controlled bulk conditions showed that solvent evaporation boosted reconcentration 2.1-fold and fluidized-bed drying raised it 1.8-fold. Enzyme inhibition tests, normalizing to final mass, revealed an IC50 value of 14.14±0.02 µg/mL. In parallel inhibition assays on -glucosidase, the plant extract outperformed commercial acarbose, recorded at 379.75±0.57 µg/mL, yet fell far short of pure quercetin, whose strength was 2.97±0.05 µg/mL. A side-by-side formulation comparison showed liquid-bed drying conserved inhibitory activity at 118.5964 g/mL, whereas the simpler evaporation method inflated that estimate to roughly 1,176.6459 g/mL. This research demonstrates that α-mangostin from the mangosteen fruit has the potential to be a stronger inhibitor of α-glucosidase enzyme than the commercial drug acarbose, although still less than the effectiveness of pure quercetin. The formulation process affects biological activity and solubility greatly. Solvent evaporation increases bioavailability more than fluid spray drying, yet diminishes enzyme inhibition effectiveness. On the other hand, fluidized bed drying retains enzyme inhibition activity much better, even though the increase in solubility is slightly lower. Thus, the formulation approach is the most important factor to consider in maximally utilizing the therapeutic potential of α-mangostin for development as natural antidiabetic drugs.