One-step mild biorefinery of functional biomolecules from microalgae extracts
Autor: | Hélène Monteillet, Frans A. M. Leermakers, Rupali K. Desai, Xiaohua Li, J. Mieke Kleijn, Boelo Schuur, Michel H.M. Eppink, René H. Wijffels |
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Přispěvatelé: | Sustainable Process Technology |
Rok vydání: | 2018 |
Předmět: |
Bio Process Engineering
One-Step 02 engineering and technology Fractionation 01 natural sciences Catalysis chemistry.chemical_compound Life Science Chemical Engineering (miscellaneous) Organic chemistry VLAG Fluid Flow and Transfer Processes chemistry.chemical_classification Aqueous solution 010405 organic chemistry Chemistry Process Chemistry and Technology Biomolecule Extraction (chemistry) 021001 nanoscience & nanotechnology Biorefinery 0104 chemical sciences Chemical engineering Chemistry (miscellaneous) Emulsion Ionic liquid 0210 nano-technology Physical Chemistry and Soft Matter |
Zdroj: | Reaction chemistry & engineering, 3(2), 182-187. Royal Society of Chemistry Reaction Chemistry & Engineering, 3(2), 182-187 Reaction Chemistry & Engineering 3 (2018) 2 |
ISSN: | 2058-9883 |
Popis: | Fractionation of complex matrices such as biomass into diverse functional biomolecules without disrupting the biomolecule functionalities is a real challenge. Known separation processes are designed for the recovery of single products such as hydrophilic proteins or hydrophobic pigments, discarding the other products as waste. Here we present a concept for one-step biorefinery of hydrophobic and hydrophilic biomolecules from complex matrices using an ionic liquid-based surfactant free emulsion stabilised by microgel particles, while maintaining the product integrity. We demonstrate the process by simultaneous extraction of pigments and proteins from a microalgae extract; the hydrophobic pigments are transferred to the ionic liquid droplets and the proteins to the aqueous continuous phase. In contrast to most solvent extraction procedures, with this concept, the proteins retain their nativity, opening up an extraction pathway to fully functioning proteins while harvesting hydrophobes. A perspective towards continuous operation of this novel process is presented. |
Databáze: | OpenAIRE |
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