2012
DOI: 10.1208/s12249-012-9794-3
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Improved Enzyme Activity and Stability in Polymer Microspheres by Encapsulation of Protein Nanospheres

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Cited by 16 publications
(14 citation statements)
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“…The HRP/MβCD powder was suspended in ethyl acetate in order to dissolve MβCD followed by sonication for 30 s. The solid protein nanoparticles were collected by centrifugation following removal of ethyl acetate containing MβCD. The formed nanoparticles were encapsulated into PLGA microspheres by s/o/w method [66]. Investigators have also prepared lyophilized HRP loaded PLGA microspheres.…”
Section: Colloidal Delivery Systemsmentioning
confidence: 99%
“…The HRP/MβCD powder was suspended in ethyl acetate in order to dissolve MβCD followed by sonication for 30 s. The solid protein nanoparticles were collected by centrifugation following removal of ethyl acetate containing MβCD. The formed nanoparticles were encapsulated into PLGA microspheres by s/o/w method [66]. Investigators have also prepared lyophilized HRP loaded PLGA microspheres.…”
Section: Colloidal Delivery Systemsmentioning
confidence: 99%
“…170 The increased size of the enzymecage complex compared with the enzyme alone can also facilitate reuse of enzymes in industry. 171 Examples of non-proteinbased nanosized cages are polymers, 172,173 polymersomes, 174,175 liposomes, 176,177 giant amphiphiles, 178 nanogels, 179 layer-by-layer structures, 180 nanodroplets, 181 nanosized metal organic frameworks (MOF), 182 silica nanoparticles 183 and other inorganic cages. 184,185 Most of these systems are especially applicable when stability is needed in extreme environments, as in the case of water-free systems, or when high (thermal) stability is required.…”
Section: Advantages Of Protein Nanoreactors Over Other Nanoreactorsmentioning
confidence: 99%
“…Encapsulation efficiency % ð Þ= mass extracted protein mass theoretical mass loading × 100 , where mass extracted protein is the mass of protein recovered per mass of PLGA microparticles after removal of PLGA via organic solvent and mass theoretical mass loading is the theoretical maximum mass of protein per mass of PLGA microparticles. Loading levels of proteins within PLGA microparticles are typically 1-10 wt% and the encapsulation efficiency using emulsion-based production can vary from 30 to 95% (Emami et al, 2009;Li, Anderson, Mehta, & Deluca, 1995;Lim, Lee, Widjaja, & Loo, 2013;Montalvo-Ortiz, Sosa, & Griebenow, 2012). The encapsulation efficiency of peptides and proteins is dependent on the physicochemical characteristic of the protein and stabilization of the primary and secondary emulsion.…”
Section: Double Emulsionmentioning
confidence: 99%