Fig. 4: Co-immobilization of enzyme and cell by NKCOF-141 and characterizations. | Nature Communications

Fig. 4: Co-immobilization of enzyme and cell by NKCOF-141 and characterizations.

From: Co-immobilization of whole cells and enzymes by covalent organic framework for biocatalysis process intensification

Fig. 4

a Schematic illustration and reconstructed 3D CLSM image of FITC-INU-NH2&E-NH2@NKCOF-141. The 3D top view (b) and the 3D side view (c) CLSM images of FITC-INU-NH2&E-NH2@NKCOF-141. d CLSM images of the FITC-INU-NH2&E-NH2@NKCOF-141 at a series of focal planes measured every 0.2 μm along the Z-axis. The cells were labeled with propidium iodide (red). Scale bar: 0.5 µm. Each experiment was repeated independently three times with similar results (n = 3). e The catalytic activity of immobilized INU-NH2&E-NH2 in different materials, and co-immobilized systems were loaded with ~ 4 mg of cells and 1 mg of enzyme. f Stability of INU-NH2&E-NH2 and INU-NH2&E-NH2@NKCOF-141 after treatment in heat (60 °C) for 20 min, methanol for 40 min and ethanol for 30 min, and 15 mg mL−1 chymotrypsin for 30 min. g Recyclability of INU-NH2&E-NH2@NKCOF−141, in which the initial content of D-allulose was set as 100%. All error bars mean ± s.d. received from three independent experiments (n = 3). Source data are provided as a Source Data file.

Back to article page