TY  - JOUR
A1  - Zhang, Shuhao
A1  - Bramski, Julia
A1  - Tutus, Murat
A1  - Pietruszka, Jörg
A1  - Böker, Alexander
A1  - Reinicke, Stefan
T1  - A Biocatalytically Active Membrane Obtained from Immobilization of 2-Deoxy-D-ribose-5-phosphate Aldolase on a Porous Support
JF  - ACS applied materials & interfaces
N2  - Aldol reactions play an important role in organic synthesis, as they belong to the class of highly beneficial C-C-linking reactions. Aldol-type reactions can be efficiently and stereoselectively catalyzed by the enzyme 2-deoxy-D-ribose-5-phosphate aldolase (DERA) to gain key intermediates for pharmaceuticals such as atorvastatin. The immobilization of DERA would open the opportunity for a continuous operation mode which gives access to an efficient, large-scale production of respective organic intermediates. In this contribution, we synthesize and utilize DERA/polymer conjugates for the generation and fixation of a DERA bearing thin film on a polymeric membrane support. The conjugation strongly increases the tolerance of the enzyme toward the industrial relevant substrate acetaldehyde while UV-cross-linkable groups along the conjugated polymer chains provide the opportunity for covalent binding to the support. First, we provide a thorough characterization of the conjugates followed by immobilization tests on representative, nonporous cycloolefinic copolymer supports. Finally, immobilization on the target supports constituted of polyacrylonitrile (PAN) membranes is performed, and the resulting enzymatically active membranes are implemented in a simple membrane module setup for the first assessment of biocatalytic performance in the continuous operation mode using the combination hexanal/acetaldehyde as the substrate.
KW  - 2-deoxy-D-ribose-5-phoshphate aldolase
KW  - enzyme immobilization
KW  - enzymatically active membrane
KW  - enzyme/polymer conjugate
KW  - self-assembly
Y1  - 2019
U6  - https://doi.org/10.1021/acsami.9b12029
SN  - 1944-8244
SN  - 1944-8252
VL  - 11
IS  - 37
SP  - 34441
EP  - 34453
PB  - American Chemical Society
CY  - Washington
ER  - 
TY  - JOUR
A1  - Reinicke, Stefan
A1  - Rees, Huw C.
A1  - Espeel, Pieter
A1  - Vanparijs, Nane
A1  - Bisterfeld, Carolin
A1  - Dick, Markus
A1  - Rosencrantz, Ruben R.
A1  - Brezesinski, Gerald
A1  - de Geest, Bruno G.
A1  - Du Prez, Filip E.
A1  - Pietruszka, Jörg
A1  - Böker, Alexander
T1  - Immobilization of 2-Deoxy-D-ribose-5-phosphate Aldolase in Polymeric Thin Films via the Langmuir-Schaefer Technique
JF  - ACS applied materials & interfaces
N2  - A synthetic protocol for the fabrication of ultrathin polymeric films containing the enzyme 2-deoxy-D-ribose-5-phosphate aldolase from Escherichia coli (DERA(EC)) is presented. Ultrathin enzymatically active films are useful for applications in which only small quantities of active material are needed and at the same time quick response and contact times without diffusion limitation are wanted. We show how DERA as an exemplary enzyme can be immobilized in a thin polymer layer at the air-water interface and transferred to a suitable support by the Langmuir-Schaefer technique under full conservation of enzymatic activity. The polymer in use is a poly(N-isopropylacrylamide-co-N-2-thiolactone acrylamide) (P(NIPAAm-co-TlaAm)) statistical copolymer in which the thiolactone units serve a multitude of purposes including hydrophobization of the polymer, covalent binding of the enzyme and the support and finally cross-linking of the polymer matrix. The application of this type of polymer keeps the whole approach simple as additional cocomponents such as cross-linkers are avoided.
KW  - Langmuir-Schaefer
KW  - enzyme immobilization
KW  - 2-deoxy-D-ribose-5-phosphate aldolase
KW  - polymeric thin film
KW  - poly(N-isopropylacrylamide)
KW  - thiolactone
Y1  - 2017
U6  - https://doi.org/10.1021/acsami.6b13632
SN  - 1944-8244
VL  - 9
SP  - 8317
EP  - 8326
PB  - American Chemical Society
CY  - Washington
ER  -