Immobilization of D-Amino Acid Oxidase (DAAO) Enzyme on Hybrid Mesoporous MCF, SBA-15 and MCM-41 Nanomaterial

J Nanosci Nanotechnol. 2017 Feb;17(2):947-53. doi: 10.1166/jnn.2017.12632.

Abstract

Hybrid mesoporous materials as carriers for immobilization of D-amino acid oxidase (DAAO) were prepared via three steps: (i) hydrothermal synthesis of nanoporous MCF, SBA-15 and MCM-41 powders, (ii) functionalization with 3-aminopropyltriethoxysilane (APTES) by post-synthesis grafting; and (iii) activation with glutardialdehyde. The resulting mesostructured solids were characterized by various techniques: XRD, IR, TGA-DTA and N2 adsorption–desorption (BET). The characterization results indicated that these materials still maintained their structure after functionalization. IR data and TGA-DTA analysis demonstrated the existence of amine functional groups on the surface of APTES-functionalized samples. The DAAO immobilized on these materials exhibited higher catalytic activity and stability of enzyme for conversion of cephalosporin C (CPC) as compared to those of the non-functionalized ones. The catalytic activity and stability of enzyme decreased in the order MCF > SBA-15 > MCM-41.

Keywords: MCF; SBA-15; MCM-14; Immobilization; Enzyme; DAAO; Functionalizaton.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • D-Amino-Acid Oxidase* / chemistry
  • D-Amino-Acid Oxidase* / metabolism
  • Enzyme Stability
  • Enzymes, Immobilized* / chemistry
  • Enzymes, Immobilized* / metabolism
  • Nanostructures / chemistry*
  • Porosity
  • Silicon Compounds / chemistry*
  • Silicon Dioxide / chemistry

Substances

  • Enzymes, Immobilized
  • MCM-41
  • SBA-15
  • Silicon Compounds
  • Silicon Dioxide
  • D-Amino-Acid Oxidase