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Bartha-Vári, Judith Hajnal, et al. Periodica Polytechnica Chemical Engineering 61.1 (2017): 59-66.
Phenylalanine ammonia lyase (PcPAL) from oil palm was covalently immobilized on aminated single-walled carbon nanotubes (SwCNTNH2) to further improve the enzyme's stability in ammonia addition reactions. The SwCNTNH2 PAL obtained in this way was tested as a biocatalyst for stereoselective bioconversion in batch mode and in a continuous flow reactor.
Covalent Binding of PcPAL onto SwCNTNH2
SwCNTNH2 (20 mg) was incubated with a solution of glycerol diglycidyl ether (GDE, 32.4 mg, 0.2 mmol) in CH2Cl2 (5 mL) at room temperature overnight with shaking at 1350 rpm, with occasional sonication to avoid the formation of bundled SwCNTs. The sample was filtered on a membrane filter and then washed with CH2Cl2 (3 × 1 mL). To the resulting modified SwCNTNH2, a solution of PcPAL (2.0 mg in 1 mL 0.1 M Tris buffer, pH 8.8) was added, and the mixture was shaken at 1350 rpm at room temperature overnight. The formed biocatalyst was filtered off on a membrane filter and washed with distilled water (3 × 10 mL). The amount of immobilized PcPAL was determined by comparing the mass of PcPAL in the solution before immobilization (2.0 mg in 1 mL solution) and after immobilization (0.06 mg in a unified filtrate) using spectrophotometry using the Bradford method.
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