Information from the abstract
This study investigated the interactions between polyphenolic compounds derived from durian fruits ( Durio zibethinus Murr.) and human serum proteins under different processing conditions, including vacuum drying, pasting, and frying, compared with fresh fruit. The polyphenolic profile was characterized using HPLC-MS/MS analysis. Differential Scanning Calorimetry (DSC) and Fourier-transform infrared spectroscopy (FTIR) were used to analyze thermal behavior and overall functional group alterations in the whole fruit matrix during processing. Spectrofluorometry analysis was used to characterize polyphenols binding affinities with human serum proteins including albumin, globulin, and fibrinogen, while the influence of protein glycation was also assessed and molecular docking was employed to provide integrated computational analysis into structural changes. Fresh durian exhibited the highest concentrations of phenolic acids, particularly gallic and cinnamic acids, whereas frying significantly reduced polyphenol levels. Vacuum drying effectively preserved major bioactive compounds, while paste processing resulted in moderate retention. Polyphenol–protein binding was reduced following protein glycation, indicating that glycation may impair the binding capacity of serum proteins under diabetic-like conditions. FTIR analyses demonstrated that minimal processing better preserves intact polyphenolic structures, whereas intensive thermal treatment induces pronounced chemical modifications. Molecular docking predicted binding of durian flavonoids to native and glycated human serum albumin, as well as fibrinogen, suggesting potential interactions with these proteins that warrant further investigation. Vacuum drying appears to be optimal strategies for maintaining the functional quality of durian products. These findings provide a basis for further studies in cellular and in vivo models.
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Related topics: Berberine and alkaloids research · Phytochemicals and Antioxidant Activities · Curcumin's Biomedical Applications
Thai researcher and institutional participation
Supeeraya Arsa · Angkana Wipatanawin · Sumitra Poovarodom · Ratiporn Haruenkit · Praphan Pinsirodom · King Mongkut's Institute of Technology Ladkrabang · Mahidol University
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