Abstract: Enzymatic cross-linking of protein-encapsulated oil particles by complex coacervation. A complex coacervate of oil particles, each encapsulated in a protein shell, is stabilized by gelling the protein shell and is subsequently enzymatically cross-linked to form thermostable capsules of about 100-300 microns. The preferred enzyme is transglutaminase, and the reaction is performed at pH 7 to achieve the optimal cross-linking rate. The transglutaminase-catalyzed cross-linking reaction takes place with the complex coacervate maintained at a temperature in the range of about 5° C.-10° C. to maintain the structural stability of the complex coacervate.

Abstract: Enzymatic cross-linking of protein-encapsulated oil particles by complex coacervation. A complex coacervate of oil particles, each encapsulated in a protein shell, is stabilized by gelling the protein shell and is subsequently enzymatically cross-linked to form thermostable capsules of about 100-300 microns. The preferred enzyme is transglutaminase, and the reaction is performed at pH 7 to achieve the optimal cross-linking rate. The transglutaminase-catalyzed cross-linking reaction takes place with the complex coacervate maintained at a temperature in the range of about 5.degree. C.-10.degree. C. to maintain the structural stability of the complex coacervate.

Abstract: A method for preparing microcapsules which comprises:dispersing a hydrophobic oily liquid containing a pre-wall former in a continuous aqueous phase, the aqueous phase containing a chain extender which comprises a water soluble polyfunctional compound capable of reacting with the pre-wall former upon dispersion of the hydrophobic oily liquid in the continuous aqueous phase; andforming capsule walls around the droplets of the hydrophobic oily liquid in the continuous aqueous phase.