Publication | Closed Access
Microencapsulation of proteins by rapid expansion of supercritical solution with a nonsolvent
167
Citations
27
References
2000
Year
Ethylene GlycolMacromolecular ChemistryEngineeringSupercritical Fluid ChromatographyBiofabricationChemistryProtein RefoldingPolymersMacromolecular EngineeringProtein FoldingRapid ExpansionBiochemical EngineeringNew Method—rapid ExpansionSupercritical SolutionDissolved PolymerPolymer ChemistryBiophysicsMicro-encapsulationBiopolymersBiomolecular EngineeringSupercritical Co2Macromolecular SciencePolymer ScienceProtein EngineeringMedicine
Abstract A new method—rapid expansion from supercritical solution with a nonsolvent (RESS‐N)—is reported for forming polymer microparticles containing proteins such as lysozyme (from chicken egg white) and lipase (from Pseudomonas cepacia). A suspension of protein in CO 2 containing a cosolvent and dissolved polymer is sprayed through a nozzle to atmospheric pressure. The polymers are poly(ethylene glycol) (PEG4000; MW = 3,000, PEG6000; MW = 7,500, PEG20000; MW = 20,000), poly(methyl methacrylate) (PMMA; MW = 15,000), poly(L‐lactic acid) (PLA; MW = 5,000), poly(DL‐lactide‐co‐glycolide) (PGLA; MW = 5,000) and PEG–poly(propylene glycol) (PPG)–PEG triblock copolymer (MW = 13,000). The solubilities of these polymers in CO 2 increase significantly with low‐molecular‐weight alcohols as cosolvents. The particles do not tend to agglomerate after expansion, since the pure cosolvent is a nonsolvent for the polymer. The structure and morphology of the microcapsules were investigated by TEM, SEM, and optical microscopy. The thickness of the polymer coating about the protein, as well as the mean particle diameter and particle‐size distribution, could be controlled by changing the feed composition of the polymer.
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