Affordable Access

SiO2 microparticles with carbon nanotube-derived mesopores as an efficient support for enzyme immobilization

Authors
  • kumar, a
  • park, g d
  • patel, s k s
  • kondaveeti, s
  • otari, s
  • anwar, z
  • kalia, v c
  • singh, y
  • kim, s c
  • cho, b k
  • sohn, jung hoon
  • kim, d r
  • kang, y c
  • lee, j k
Publication Date
Jan 23, 2019
Source
KRIBB Repository
Keywords
License
Unknown
External links

Abstract

Novel mesoporous SiO2 microparticles were synthesized by spray pyrolysis using multiwalled carbon nanotubes (MCNTs) as a template. The synthesized multicompartment structure with uniform pores of 12.0 nm was used to immobilize lipase from Thermomyces lanuginosus. The total surface area of mesoporous SiO2 microparticles prepared from silica colloidal solution was increased by 26-folds compared to that of dense SiO2 particles (494 vs 19.0 m2 g?1, respectively). Mesoporous SiO2 particles showed 236% higher protein loading for lipase, than dense SiO2 particles. The maximum velocity (Vmax) and catalytic efficiencies of immobilized lipase were 3.80 and 5.90 folds higher than that of free enzyme. Contact angle analysis revealed increased hydrophobicity of the mesoporous particles, which is advantageous for lid opening at the active center, and increased activity after immobilization. We next developed a lipase/SiO2/glassy carbon electrode (GCE) biosensors. Cyclic voltammetric results showed linear responses of the lipase/SiO2/GCE bioelectrode towards tributyrin (50?300 mg dL?1) as a surface-limited reaction in Tris-HCl buffer. After 12 repetitive uses, dense SiO2- and mesoporous SiO2-bound lipase retained 74.2 and 95.4% of its original activities, respectively. Thus, given their desirable characteristics and industrial utility, greatly porous SiO2 particles may provide an excellent support for enzyme immobilization in biosensor development or biocatalysis in organic media.

Report this publication

Statistics

Seen <100 times