Antisolvent micronization of BSA using supercritical mixtures carbon dioxide + organic solvent |
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| Affiliation: | 1. Department of Chemical Engineering, National Chung Hsing University, No. 250, Kuokuang Rd, Taichung 402, Taiwan, ROC;2. Department of Nutrition, China Medical University, No. 91, Hsueh-Shih Rd, Taichung 404, Taiwan, ROC;3. Department of Food Science and Biotechnology, National Chung Hsing University, No. 250, Kuokuang Rd, Taichung 402, Taiwan, ROC;4. Department of Materials Engineering, National Chung Hsing University, No. 250, Kuokuang Rd, Taichung 402, Taiwan, ROC;5. Biotechnology Center, National Chung Hsing University, No. 250, Kuokuang Rd, Taichung 402, Taiwan, ROC;1. Department of Chemical Engineering and Food Technology, Faculty of Sciences, University of Cádiz International Excellence Agrifood Campus (CeiA3), 11510, Puerto Real, Cádiz, Spain;2. Aix Marseille Univ., CNRS, Centrale Marseille, M2P2, Marseille, France;1. Department of Industrial Engineering, University of Salerno, Via Giovanni Paolo II, 132, 84084, Fisciano, Italy;2. Department of Civil, Chemical and Environmental Engineering (DICCA), University of Genoa, Via Opera Pia 15, 16145, Genova, Italy |
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| Abstract: | In this work, expanded liquid antisolvent (ELAS) process has been used to micronize bovine serum albumin (BSA) solubilized in water. Carbon dioxide mixtures with ethanol, acetone or isopropyl alcohol, at expanded liquid conditions, have been used as the antisolvent. The effect of process parameters, such as the kind of co-antisolvent and the organic co-antisolvent/water/carbon dioxide mole fraction on the morphology and dimensions of the precipitates, was studied. Changing co-antisolvent and operating conditions, we obtained nanoparticles (with a mean diameter of about 60 nm ± 10 nm), sub-microparticles (with a mean diameter of 470 nm ± 130 nm), microparticles (with a mean diameter of 0.93 μm ± 0.37 μm) and expanded microparticles with an empty core (with a mean diameter of about 9 μm ± 5 μm). Fourier transform infrared analysis on BSA powders revealed that, using acetone as co-antisolvent, no modifications of the protein secondary structure were induced by ELAS processing. |
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| Keywords: | Expanded liquid antisolvent process Hydrosoluble proteins Bovine serum albumin Supercritical fluids |
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