By a News Reporter-Staff News Editor at Life Science Weekly -- Fresh data on Enzymes and Coenzymes are presented in a new report. According to news originating from Tehran, Iran, by NewsRx correspondents, research stated, "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)."
Our news journalists obtained a quote from the research from the University of Tehran, "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."
According to the news editors, the research concluded: "In addition, the immobilized lipase with the nanocomposite can be easily recovered and retained at 74% of its initial activity after 15 time reuses."
For more information on this research see: Polyacrolein/mesoporous silica nanocomposite: Synthesis, thermal stability and covalent lipase immobilization. Materials Chemistry and Physics, 2013;143(1):76-84. Materials Chemistry and Physics can be contacted at: Elsevier Science Sa, PO Box 564, 1001 Lausanne, Switzerland. (Elsevier - www.elsevier.com; Materials Chemistry and Physics - www.elsevier.com/wps/product/cws_home/504097)
The news correspondents report that additional information may be obtained from S.F. Motevalizadeh, Univ Tehran, Center Excellence Biothermodynam, Tehran, Iran. Additional authors for this research include M. Khoobi, M. Shabanian, Z. Asadgol, M.A. Faramarzi and A. Shafiee (see also Enzymes and Coenzymes).
Keywords for this news article include: Iran, Asia, Tehran, Lipase, Enzymes and Coenzymes, Carboxylic Ester Hydrolases
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