Enzymatic Hydrolysis of Inulin by an Immobilized Extremophilic Inulinase From the Halophile Bacterium Alkalibacillus Filiformis Publisher Pubmed



Yousefimokri M^{1, 2} ; Sharafi A² ; Rezaei S¹ ; Sadeghianabadi S¹ ; Imanparast S¹ ; Mogharabimanzari M¹ ; Amanzadeh Y¹ ; Faramarzi MA¹ Show Affiliations
Source: Carbohydrate Research Published:2019

Abstract

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 (CoFe2O4 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. © 2019 Elsevier Ltd