Polyacrolein/mesoporous silica nanocomposite: Synthesis, thermal stability and covalent lipase immobilization

被引:25
作者
Motevalizadeh, Seyed Farshad [1 ,2 ]
Khoobi, Mehdi [1 ,2 ]
Shabanian, Meisam [1 ,2 ]
Asadgol, Zahra [3 ,4 ]
Faramarzi, Mohammad Ali [3 ,4 ]
Shafiee, Abbas [1 ,2 ,5 ]
机构
[1] Univ Tehran Med Sci, Fac Pharm, Dept Med Chem, Tehran 14176, Iran
[2] Univ Tehran Med Sci, Pharmaceut Sci Res Ctr, Tehran 14176, Iran
[3] Univ Tehran Med Sci, Fac Pharm, Dept Pharmaceut Biotechnol, Tehran 14176, Iran
[4] Univ Tehran Med Sci, Biotechnol Res Ctr, Tehran 14176, Iran
[5] Univ Tehran, Ctr Excellence Biothermodynam, Tehran, Iran
基金
美国国家科学基金会;
关键词
Composite materials; Nanostructures; Polymers; Thermal properties; Electron microscopy; Biomaterials; ENZYME IMMOBILIZATION; MESOPOROUS SILICA; MEMBRANES; MCM-41; MICROSPHERES;
D O I
10.1016/j.matchemphys.2013.08.016
中图分类号
T [工业技术];
学科分类号
08 ;
摘要
In this work, new polyacrolein/MCM-41 nanocomposites with good phase mixing behavior were prepared through an emulsion polymerization technique. Mesoporous silica was synthesized by in situ assembly of tetraethyl orthosilicate (TEOS) and cetyl trimethyl ammonium bromide (CTAB). The structure and properties of polyacrolein containing nanosized MCM-41 particle (5 and 10 wt%), were investigated by Fourier transform infrared spectroscopy (FTIR), X-ray diffraction, Dynamic light scattering (DLS), scanning electron microscopy (SEM), transmission electron microscopy (TEM), N-2 adsorption techniques, and thermogravimetric (TGA) analyses. The SEM images from the final powder have revealed good dispersion of the MCM-41 nanoparticles throughout polymeric matrix with no distinct voids between two phases. The results indicated that the thermal properties of the nanocomposite were enhanced by addition of MCM-41. Thermomyces lanuginosa lipase (TLL) was used as a model biocatalyst and successfully immobilized with polyacrolein and the nanocomposite via covalent bonds with the aldehyde groups. The activity between free enzyme, polyacrolein, and MCM-41 nanocomposite (10 wt%)-immobilized TLL was compared. The immobilized lipase with the nanocomposite shows better operational stability such as pH tolerance, thermal and storage stability. In addition, the immobilized lipase with the nanocomposite can be easily recovered and retained at 74% of its initial activity after 15 time reuses. (C) 2013 Elsevier B.V. All rights reserved.
引用
收藏
页码:76 / 84
页数:9
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