Warner, N.; Osojnik Črnivec, I.G.; Rana, V.K.; Cruz, M.; Scherman, O.A. A Platform Approach to Protein Encapsulates with Controllable Surface Chemistry. Molecules2022, 27, 2197.
Warner, N.; Osojnik Črnivec, I.G.; Rana, V.K.; Cruz, M.; Scherman, O.A. A Platform Approach to Protein Encapsulates with Controllable Surface Chemistry. Molecules 2022, 27, 2197.
Warner, N.; Osojnik Črnivec, I.G.; Rana, V.K.; Cruz, M.; Scherman, O.A. A Platform Approach to Protein Encapsulates with Controllable Surface Chemistry. Molecules2022, 27, 2197.
Warner, N.; Osojnik Črnivec, I.G.; Rana, V.K.; Cruz, M.; Scherman, O.A. A Platform Approach to Protein Encapsulates with Controllable Surface Chemistry. Molecules 2022, 27, 2197.
Abstract
The encapsulation of proteins into core-shell structures is a widely utilised strategy for controlling protein stability, delivery and release. Despite the recognised utility of these microstructures, however, core-shell fabrication routes are often too costly or poorly scalable to allow for industrial translation. Furthermore, many scalable routes rely upon emulsion-techniques implicating denaturing or environmentally harmful organic solvents. Herein, we investigate core-shell protein encapsulation through single-feed, aqueous spray drying: a cheap, industrially ubiquitous particle-formation technology in the absence of organic solvents. We show that an excipient’s preference for the surface of the spray dried particle is well-predicted by its hydrodynamic diameter (Dh) under relevant feed buffer conditions (pH and ionic strength) and that the predictive power of Dh is improved when measured at the spray dryer outlet temperature compared to room temperature (R2 = 0.64 vs. 0.59). Lastly, we leverage these findings to propose an adaptable design framework for fabricating core-shell protein encapsulates by single-feed aqueous spray drying.
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
