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.