Separation of catalase fromAmsonia orientaliswith single step by aqueous two-phase partitioning system (ATPS)
| Autor: | Yonca Yuzugullu, Yonca Avcı Duman, Arda Acemi, Fazıl Özen |
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| Rok vydání: | 2016 |
| Předmět: |
0106 biological sciences
chemistry.chemical_classification Aqueous solution Chromatography biology 010405 organic chemistry Chemistry ved/biology Process Chemistry and Technology General Chemical Engineering Hydrophilic interaction chromatography ved/biology.organism_classification_rank.species Filtration and Separation Single step General Chemistry 01 natural sciences 0104 chemical sciences Enzyme Catalase 010608 biotechnology Amsonia orientalis PEG ratio biology.protein |
| Zdroj: | Separation Science and Technology. 52:691-699 |
| ISSN: | 1520-5754 0149-6395 |
| DOI: | 10.1080/01496395.2016.1253588 |
| Popis: | Catalase from Amsonia orientalis was purified by ATPS, and its efficiency was compared against hydrophobic interaction chromatography. Activity recovery and purification fold of purified catalase by ATPS were examined under varying experimental conditions. The effects of various factors such as type of phase-forming salts, (PEG) mass, with their different concentrations, pH and temperature effects on partitioning were investigated. The highest activity recovery (156%) and purification fold (8.67) of catalase were obtained in the ATPS system containing 10% (g/g) PEG4000, 15% (g/g) Na2SO4 at pH 6.0 and room temperature. In hydrophobic interaction chromatography, the enzyme has been purified 12.54-fold with 57.5% recovery. The molecular weight of catalase was determined as 75 kDa by SDS-PAGE. |
| Databáze: | OpenAIRE |
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