Design of an immobilized preparation of catalase from Thermus thermophilus to be used in a wide range of conditions.

摘要: Abstract Crude extracts from Thermus thermophilus strains HB8 and HB27 with catalase activity were obtained. Activity measurements in the presence of azide suggested that Mn-catalase may be responsible for these activities, which was successfully stabilised by multipoint immobilization onto highly activated glyoxyl or glutaraldehyde agarose, while on poorly supports did not stabilize enzyme. The most stable preparation obtained using T. immobilized agarose (compared to derivatives strain). However, stability enzyme depended concentration, suggesting dissociation subunits could playing a key role inactivation preparation. SDS–PAGE this derivative confirmed some protein covalently attached support. In order avoid release supernatant, preparations crosslinked dextran aldehyde. Using partially oxidized dextrans, full stabilization quaternary structure enzymes achieved without severe detrimental effects activity. optimally stabilized derivative, dilution have any effect Thermal optimal studied at different pH values organic cosolvents, reaching half-lives 7 days 50% acetonitrile dioxane 40 °C. Thus, biocatalysts are very robust, capable functioning wide range conditions.