Characterization and application of a sterol esterase immobilized on polyacrylate epoxy-activated carriers (Dilbeads™)

Abstract

The sterol esterase from the ascomycete Ophiostoma piceae was immobilized on novel polyacrylate-based epoxy-activated carriers (Dilbeads TM). Six supports with particle sizes between 120-165 m were prepared varying the composition of monomers, crosslinkers and porogens. Their surface areas and porosities were determined by N 2 adsorption and mercury intrusion porosimetry. The pore volumes ranged from 0.63 to 1.32 cm 3 /g, but only Dilbeads TM RS and NK had narrow pore size distributions (with maxima at 33.5 and 67.0 nm, respectively). The distribution of the enzyme in the support was studied by fluorescence confocal microscopy. The immobilized esterase on Dilbeads TM TA showed a significant pH and thermal stability and was assayed in the continuous hydrolysis of cholesteryl esters-present in the pulp industry process waters- .

Advanced characterization of immobilized enzymes as heterogeneous biocatalysts

“…Soaking the support with liquid of comparable refractive index is a possible solution to enable direct measurements also in such cases [12,62,63]. Evidence from CLSM studies on the interaction of proteins with chromatographic supports can be translated almost directly to enzyme immobilization [50,62,[71][72][73][74][75][76][77][78][79][80][81][82][83]. Relationships between the dynamics of protein adsorption and the external and internal geometrical features of the support were established [84][85][86].…”

Fungi and Their Enzymes for Pitch Control in the Pulp and Paper Industry

“…Fungal sterol esterases can be produced by heterologous expression in industrial hosts and the recombinant enzymes have been characterized (Calero-Rueda et al 2009;Kontkanen et al 2006a) and immobilized to increase their enzyme stability (Torres et al 2008). The effects of a recombinant sterol esterase from M. albomyces on the extractives of TMP water (Table 17.3) as well as on the properties of derived paper sheets were evaluated and compared with Resinase A2X (Kontkanen et al 2006b).…”

Immobilisation of horseradish peroxidase on Eupergit®C for the enzymatic elimination of phenol

“…pH 7.0) mainly if a former mild physical adsorption between the protein and the support has been promoted [13]. Several research works has studied the immobilisation of enzyme onto epoxy-activated supports remarking the improvement in the stability of the support towards pH, temperature and storage time [14][15][16].…”