Abstract
Prolamin-based particles loaded with bioactive molecules have attracted widespread attention from scientists due to their novel properties in chemistry, physics, and biology. In the self-assembly process of biopolymer-based nanocapsules, noncovalent interactions are the main driving forces for reducing bulk materials to the nanoscale and controlling the release of bioactive molecules. This article reviews the types of interaction forces, binding strength, binding active sites, molecular orientation, and binding affinity that affect the release profile of bioactive molecules during the preparation of protein stabilizer particles. Different preparation formulations, the use of different biopolymers, the inherent nature of the loaded bioactive molecules, and external factors (including pH, biopolymer concentration, temperature, salt, ultrasonication, and atmospheric cold plasma treatment) lead to different types and strengths of intra- and intermolecular interactions. Strategies, such as pH, ultrasonication, and atmospheric cold plasma, to change the protein conformation are key to improving the binding strength between proteins and bioactive substances or stabilizers. This review provides some guidance for scientists and technicians dedicated to improving loading efficiency, delaying release, enhancing colloidal stability, and exploring the binding behavior among proteins, stabilizers, and bioactive molecules.
Published Version
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
