Tuning Immobilized Enzyme Features by Combining Solid-Phase Physicochemical Modification and Mineralization.

ABSTRACT: Lipase B from Candida antarctica (CALB) and lipase from Thermomyces lanuginosus (TLL) were immobilized on octyl agarose. Then, the biocatalysts were chemically modified using glutaraldehyde, trinitrobenzenesulfonic acid or ethylenediamine and carbodiimide, or physically coated with ionic polymers, such as polyethylenimine (PEI) and dextran sulfate. These produced alterations of the enzyme activities have, in most cases, negative effects with some substrates and positive with other ones (e.g., amination of immobilized TLL increases the activity versus p-nitro phenyl butyrate (p-NPB), reduces the activity with R-methyl mandate by half and maintains the activity with S-isomer). The modification with PEI increased the biocatalyst activity 8-fold versus

SUBMITTER: Guimaraes JR 

PROVIDER: S-EPMC9658946 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature