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Immobilization of Human Carbonic Anhydrase on Gold Nanoparticles Assembled onto Amine/Thiol-Functionalized Mesoporous SBA-15 for Biomimetic Sequestration of CO 2

2011; American Chemical Society; Volume: 27; Issue: 10 Linguagem: Inglês

10.1021/la105029h

1520-5827

Mari Vinoba, Kyoung Soo Lim, Si Hyun Lee, Soon Kwan Jeong, M. Alagar,

Enzyme Catalysis and Immobilization

A biocatalyst was synthesized by immobilizing human carbonic anhydrase onto gold nanoparticles assembled over amine/thiol-functionalized mesoporous SBA-15. The physicochemical properties of the functionalized mesoporous SBA-15 were obtained by XRD, BET, FE SEM, HR TEM, EDS, and zeta potential analysis. The biocatalytic performance was studied for para-nitrophenyl acetate (p-NPA) hydrolysis. The kinetic parameters Km were found to be 22.35 and 27.75 mM, and Kcat/Km values were 1514.09 and 1612.25 M−1 s−1 for HCA immobilized on gold nanoparticles assembled on amine/thiol-functionalized mesoporous SBA-15 (HCA/Au/APTES/SBA-15 and HCA/Au/MPTES/SBA-15), respectively. These HCA/Au/APTES/SBA-15 and HCA/Au/MPTES/SBA-15 were investigated for biocatalytic hydration of CO2 and its precipitation as CaCO3. The amount of CaCO3 precipitated over HCA/Au/MPTES/SBA-15 was nearly the same as that precipitated over free HCA. Storage stability and reusability studies suggested that HCA/Au/MPTES/SBA-15 retained its activity even after 20 days storage at 25 °C and 20 recycling runs. The present results demonstrate that HCA/Au/MPTES/SBA-15 and HCA/Au/APTES/SBA-15 are highly efficient potential nanobiocatalysts for industrial-scale CO2 sequestration.