posted on 2015-10-30, 14:23authored byNoreldeen Hassan. Abdallah, Miriam. Schlumpberger, Darragh Gaffney, John P. Hanrahan, Joseph M. Tobin, Edmond MagnerEdmond Magner
The activity and stability of Candida antartica lipase B (CALB) and cytochrome c immobilised on to, SBA-15 and a porous spherical silicate material (PPS), were examined. The materials possess similar pore diameters but have different morphologies, pore volumes and surface areas. CALB exhibited higher catalytic activity and stability on SBA-15 when compared to PPS, while cytochrome c showed similar catalytic activity on both materials. The activity of CALB immobilised on SBA-15 was retained (95%) after 7 uses, while CALB immobilised on PPS retained only 43% activity. Such changes can be mainly ascribed to the different physical properties (pore volume, surface area and pore shape) of the supports.
Funding
Using the Cloud to Streamline the Development of Mobile Phone Apps
Journal of Molecular Catalysis B: Enzymatic108, pp. 82-88
Publisher
Elsevier
Note
peer-reviewed
Other Funding information
IRC, SFI, HEA
Rights
This is the author’s version of a work that was accepted for publication in Journal of Molecular Catalysis B: Enzymatic . Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Journal of Molecular Catalysis B: Enzymatic, 108, pp. 82-88, http://dx.doi.org/10.1016/j.molcatb.2014.06.007