Enzymatic hydrolysis of inulin by an immobilized extremophilic inulinase from the halophile bacterium Alkalibacillus filiformis
| Autor: | Ali Sharafi, Somaye Imanparast, Shahla Rezaei, Salar Sadeghian-Abadi, Mehdi Mogharabi-Manzari, Y Amanzadeh, Mohammad Ali Faramarzi, Mahsa Yousefi-Mokri |
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| Rok vydání: | 2019 |
| Předmět: |
Immobilized enzyme
Glycoside Hydrolases Inulin Oligosaccharides 010402 general chemistry 01 natural sciences Biochemistry Ferric Compounds Analytical Chemistry chemistry.chemical_compound Extremophiles Bacterial Proteins Enzymatic hydrolysis Enzyme Stability Inulinase Magnetite Nanoparticles Bacillaceae Ethanol precipitation Chromatography 010405 organic chemistry Chemistry Hydrolysis Organic Chemistry Substrate (chemistry) Fructose General Medicine Cobalt Chromatography Ion Exchange Enzymes Immobilized 0104 chemical sciences Ultrafiltration (renal) |
| Zdroj: | Carbohydrate research. 483 |
| ISSN: | 1873-426X |
| Popis: | Bacterial inulinases are the key enzymes in the enzymatic hydrolysis of inulin and production of fructooligosaccharides (FOSs) and high fructose syrup (HFS). An extremophilic inulinase was purified from Alkalibacillus filiformis using 80% ethanol precipitation, ultrafiltration, and Q-Sepharose anion exchange chromatography. The purified inulinase was highly active in a wide range of pH, temperature, chemical reagents, and NaCl concentrations. The enzyme immobilization on cobalt ferrite magnetic nanoparticles (CoFe 2 O 4 MNPs) was carried out by carrier binding method with covalent linkage and showed improved stability and reusability within a broad temperature and pH range, compared with the free enzyme. Using free and immobilized inulinases from A. filiformis , 122 g L −1 and 160 g L −1 fructose with 61% and 80% conversion, respectively, were obtained, with inulin as the substrate. The enzymatic properties, such as notable stability under extreme conditions, make the inulinase from A. filiformis a promising candidate for related biotechnological applications. |
| Databáze: | OpenAIRE |
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