Phospholipid-templated silica nanocapsules as efficient polyenzymatic biocatalysts.

Solid polyenzymatic biocatalysts have been designed by combining two immobilized enzymes, the first one allowing the in situ generation of H(2)O(2) from air and the second one performing an oxidation reaction. The in situ H(2)O(2) generation system is based on the reaction of glucose with air using a glucose oxidase (GOx). The optimization of the encapsulation of GOx into phospholipids-templated silica capsules (NPS) was performed. A bienzymatic system made of GOx and horseradish peroxidase (HRP) was studied. Optimal conditions for the activity of the GOx/HRP bienzymatic system have been determined for both homogeneous and heterogeneous conditions. The encapsulation in NPS materials increases the stability of both enzymes. The performance of the encapsulated bienzymatic GOx/HRP system in the model reaction of 4-aminoantipyridine with phenol is similar when the enzymes are immobilized separately in two NPS or coencapsulated in the same NPS. An excess of peroxidase compared to GOx ([HRP]/[GOx] = 5-10) is necessary to obtain the optimal activity. To show the potentiality of bienzymatic systems in real applications, HRP has been replaced by hemoglobin, which is known for its ability to oxidize polycyclic aromatic hydrocarbons (PAH) pollutants through a pseudoperoxidase pathway. A larger excess of Hb compared to GOx ([Hb]/[GOx] = 1000) was necessary to obtain the maximum PAH removal, as Hb is not a real peroxidase as HRP but a hemoprotein with some pseudoperoxidase activity. In opposite to real enzymes, the immobilization of Hb by adsorption in mesoporous silica is preferable as its encapsulation. Therefore, the bienzymatic system made of GOx encapsulated in NPS and Hb adsorbed in mesoporous silica has been used for the removal of 11 PAH from water. This heterogeneous bienzymatic system allows 64% of PAH removal from water using simple air as oxidant.

Modified SBA-15 mesoporous silica for heavy metal ions remediation.

N-Propylsalicylaldimino-functionalized SBA-15 mesoporous silica was prepared, characterized and used as an adsorbent for heavy metal ions. The organic-inorganic hybrid material was obtained using successive grafting procedures of SBA-15 silica with 3-aminopropyl-triethoxysilane and salicylaldehyde, respectively. For comparison an amorphous silica gel was functionalized using the same procedure. The structure and physicochemical properties of the materials were characterized by means of elemental analysis, X-ray diffraction (XRD), nitrogen adsorption-desorption, thermogravimetric analysis and FTIR spectroscopy. The organic functional groups were successfully grafted on the SBA-15 surfaces and the ordering of the support was not affected by the chemical modification. The behavior of the grafted solids for the adsorption of heavy metals ions from aqueous solutions was investigated. The hybrid materials showed high adsorption capacity and high selectivity for copper ions. Other ions, such as nickel, zinc, and cobalt were adsorbed by the modified SBA-15 material. The adsorbent can be regenerated by acid treatment without altering its properties.

A new mesoporous micelle-templated silica route for enzyme encapsulation.

A new mesoporous micelle-templated silica (MTS) route for enzyme encapsulation is presented. The pore structure is given by a new association oflecithin (double chain surfactant) and dodecylamine as cosurfactant. To enhance and to well protect the enzyme activity, lactose was loaded in the synthesis. The mixed-micelles give after the addition of tetraethyl orthosilicate a well-ordered mesoporous material with a spongelike rigid structure stable after calcination at 550 degrees C. The size of the pores lies between 30 and 40 A, matching well with the size of the lipases. The activity of this heterogeneous catalyst was tested in the hydrolysis of the ethylthiodecanoate. These new biocatalysts were very active, more than hydrophobic sol-gel materials and commercially available sol-gel encapsulated lipase. This new MTS synthesis route allows one to encapsulate in one-step various enzymes, even those that are very fragile.