Entrapment of Lipases in Hydrophobic Sol-Gel-Materials: Efficient Heterogeneous Biocatalysts in Aqueous Medium

Synthesis ◽  
2000 ◽  
Vol 2000 (06) ◽  
pp. 781-783 ◽  
Author(s):  
Manfred T. Reetz ◽  
Regina Wenkel ◽  
David Avnir
2003 ◽  
Vol 345 (67) ◽  
pp. 717-728 ◽  
Author(s):  
Manfred T. Reetz ◽  
Patrick Tielmann ◽  
Wolfgang Wiesenhöfer ◽  
Werner Könen ◽  
Albin Zonta

2014 ◽  
Vol 77 (11) ◽  
pp. 1799-1806 ◽  
Author(s):  
M.J. Juan-Díaz ◽  
M. Martínez-Ibáñez ◽  
M. Hernández-Escolano ◽  
L. Cabedo ◽  
R. Izquierdo ◽  
...  
Keyword(s):  

2014 ◽  
Vol 87 (6) ◽  
pp. 761-766 ◽  
Author(s):  
O. A. Kamanina ◽  
D. G. Fedoseeva ◽  
T. V. Rogova ◽  
O. N. Ponamoreva ◽  
I. V. Blokhin ◽  
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2012 ◽  
Vol 15 (6) ◽  
pp. 986-989 ◽  
Author(s):  
Mohammed Rafiq Hussain Siddiqui ◽  
Abdulaziz Ibrahim Al-Wassil ◽  
Abdullah Mohmmed Al-Otaibi ◽  
Refaat Mohamad Mahfouz

Author(s):  
Ludivine van den Biggelaar ◽  
Patrice Soumillion ◽  
Damien P. Debecker

ω-Transaminases have been immobilized on macrocellular silica monoliths and used as heterogeneous biocatalysts in a continuous flow mode enantioselective transamination reaction. The support was prepared by a sol-gel method based on emulsion-templating. The enzyme was immobilized on the structured silica monoliths both by adsorption, and by covalent grafting using amino-functionalized silica monoliths and glutaraldehyde as a coupling agent. A simple reactor set-up based on the use of a heat-shrinkable Teflon tube is presented and successfully used for the continuous flow kinetic resolution of a chiral amine, 4-bromo-α-methylbenzylamine. The porous structure of the supports ensures effective mass transfer and the reactor works in the plug flow regime without preferential flow paths. When immobilized in the monolith and used in the flow reactor, transaminases retain their activity and their enantioselectivity. The solid biocatalyst is also shown to be stable both on stream and during storage. These essential features pave the way to the successful development of an environmentally friendly process for chiral amines production.


2014 ◽  
Vol 239 ◽  
pp. 233-241 ◽  
Author(s):  
Kristiany Moreira Diniz ◽  
Felipe Augusto Gorla ◽  
Emerson Schwingel Ribeiro ◽  
Marcela Betta Olimpio do Nascimento ◽  
Rodrigo José Corrêa ◽  
...  

Author(s):  
Ludivine van den Biggelaar ◽  
Patrice Soumillion ◽  
Damien P. Debecker

ω-Transaminases have been immobilized on macrocellular silica monoliths and used as heterogeneous biocatalysts in a continuous flow mode enantioselective transamination reaction. The support was prepared by a sol-gel method based on emulsion templating. The enzyme was immobilized on the structured silica monoliths both by adsorption, and by covalent grafting using amino-functionalized silica monoliths and glutaraldehyde as a coupling agent. A simple reactor set-up based on the use of a heat-shrinkable Teflon tube is presented and successfully used for the continuous flow kinetic resolution of a chiral amine, 4-bromo-α-methylbenzylamine. The porous structure of the supports ensures effective mass transfer and the reactor works in the plug flow regime without preferential flow paths. When immobilized in the monolith and used in the flow reactor, transaminases retain their activity and their enantioselectivity. The solid biocatalyst is also shown to be stable both on stream and during storage. These essential features pave the way to the successful development of an environmentally friendly process for chiral amines production.


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