Increase of stability of oleate hydratase by appropriate immobilization technique and conditions

摘要: The enzymatic hydration of oleic acid, one the most abundant natural unsaturated fatty acids, into 10-hydroxystearic acid (10HSA) represents a subject considerable scientific and practical interest. Commercial application process requires, however, stabilization reuse biocatalyst. Recombinant oleate hydratase (OHase) from Elizabethkingia meningoseptica expressed in Escherichia coli was purified immobilized for first time by different immobilization strategies. Among tested methods, yields higher than 90% recovered activities up to 30% were achieved covalent binding onto chitosan magnetic composites. resulting biocatalysts have been characterized detail terms stability reusability. thermal enhanced after immobilization. OHase preserved 40% initial activity at 50 °C, while native enzyme completely inactivated. Immobilization resulted radical improvement operational OHase, as covalently bound 75% five reuses.