TY - CONF
T1 - Immobilization of biomolecules on soluble and insoluble polymers.
AU - Rollett, Alexandra
AU - Schneider, Konstantin
AU - Fischer, Roland
AU - Marold, Annemarie
AU - Flock, Teresa
AU - Guebitz, George
AU - Schroeder, Marc.
N1 - M1 - Copyright (C) 2017 American Chemical Society (ACS). All Rights Reserved.
CAPLUS AN 2009:301735(Conference; Meeting Abstract; Computer Optical Disk)
PY - 2009
Y1 - 2009
N2 - Coupling of biomols. onto appropriate polymers provides several advantages concerning activity, stability, recovering and sepn. In this study, various coupling techniques, different polymers and combinations of oxidoreductases with relevant substrates were investigated. Substrate specificities of laccase were tuned by chem. modification with methoxypolyethylene glycol. Biocatalytic properties of the conjugates were adjusted varying activation strategies and mol. wt. (750-5,000) of the attached polymer. Further, laccase was covalently immobilized onto insol. carriers with high efficiency and excellent recovery of activity (higher 90%). Vice versa also laccase substrates were immobilized onto silica gel as carrier. Diverse coupling strategies were elaborated, using linkers (e.g. thiol, amino, epoxy groups). Covalent coupling was confirmed by TLC and NMR anal. on low mol. wt. reaction partners. Various combinations of immobilized enzymes and/or substrate were tested in applications like org. synthesis (of UV-stabilizers), food processing (removal of off-flavors) biodegrdn. processes (elimination of explosives), and detection (biosensor for antioxidants). [on SciFinder(R)]
AB - Coupling of biomols. onto appropriate polymers provides several advantages concerning activity, stability, recovering and sepn. In this study, various coupling techniques, different polymers and combinations of oxidoreductases with relevant substrates were investigated. Substrate specificities of laccase were tuned by chem. modification with methoxypolyethylene glycol. Biocatalytic properties of the conjugates were adjusted varying activation strategies and mol. wt. (750-5,000) of the attached polymer. Further, laccase was covalently immobilized onto insol. carriers with high efficiency and excellent recovery of activity (higher 90%). Vice versa also laccase substrates were immobilized onto silica gel as carrier. Diverse coupling strategies were elaborated, using linkers (e.g. thiol, amino, epoxy groups). Covalent coupling was confirmed by TLC and NMR anal. on low mol. wt. reaction partners. Various combinations of immobilized enzymes and/or substrate were tested in applications like org. synthesis (of UV-stabilizers), food processing (removal of off-flavors) biodegrdn. processes (elimination of explosives), and detection (biosensor for antioxidants). [on SciFinder(R)]
M3 - Poster
SP - CELL-067
ER -