Literature DB >> 29671483

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

Phuong T Dang, Hy G Le, Vinh-Thang Hoang, Hoa T H Tran, Canh D Dao, Kien T Nguyen, Giang H Le, Quang K Nguyen, Tuyen V Nguyen, Tuan A Vu.   

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.

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

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Year:  2017        PMID: 29671483     DOI: 10.1166/jnn.2017.12632

Source DB:  PubMed          Journal:  J Nanosci Nanotechnol        ISSN: 1533-4880


  1 in total

1.  Affinity-binding immobilization of D-amino acid oxidase on mesoporous silica by a silica-specific peptide.

Authors:  Miaomiao Wang; Wenjing Qi; Hongping Xu; Huimin Yu; Shuliang Zhang; Zhongyao Shen
Journal:  J Ind Microbiol Biotechnol       Date:  2019-07-09       Impact factor: 3.346

  1 in total

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