RESUMEN
The acquisition of high quality lyophilized IgY products, characterized by an aesthetically pleasing visage, heightened stability, and a marked preservation of activity, constitutes an indispensable pursuit in augmenting the safety and pragmatic utility of IgY. Within this context, an exploration was undertaken to investigate an innovative modality encompassing microwave freeze-drying (MFD) as a preparatory methodology of IgY. Morphological assessments revealed that both cryogenic freezing and subsequent MFD procedures resulted in aggregation of IgY, with the deleterious influence posed by the MFD phase transcending that of the freezing phase. The composite protective agent comprised of trehalose and mannitol engendered a safeguarding effect on the structural integrity of IgY, thereby attenuating reducing aggregation between IgY during the freeze-drying process. Enzyme-linked immunosorbent assay (ELISA) outcomes demonstrated a discernible correlation between IgY aggregation and a notable reduction in its binding affinity towards the pertinent antigen. Comparative analysis vis-à-vis the control sample delineated that when the trehalose-to-mannitol ratio was upheld at 1:3, a two-fold outcome was achieved: a mitigation of the collapse susceptibility within the final product as well as a deterrence of IgY agglomeration, concomitant with an elevated preservation rate of active antibodies (78.57 %).
Asunto(s)
Inmunoglobulinas , Manitol , Trehalosa , Congelación , Trehalosa/farmacología , Trehalosa/química , Manitol/química , Liofilización/métodosRESUMEN
The preparation of egg yolk powder (EYP) with excellent solubility and high retention of active IgY is of great significance for increasing the added value and promoting the application of EYP. A new method of preparing EYP by microwave-assisted freeze-drying (MFD) was researched. Confocal laser scanning microscopy results demonstrated that the supplementation of excipients (sucrose, trehalose, and maltodextrin) could inhibit lipoproteins aggregation in egg yolk induced by freezing. Scanning electron microscopy indicated that drying further damaged the structure of lipoproteins in EYP, leading to lipid separation from it. FTIR and fluorescence spectra confirmed this finding, indicating that excipients enhance protein stability. Compared with conventional freeze-drying (FD), EYP prepared by MFD, particularly that containing excipients, had higher solubility (63 g/100 g), active antibody retention rate and shorter drying time. Therefore, excipients can significantly improve the solubility and stability of EYP and the retention rate of active IgY.