Immobilization and characterization of cellulase on concanavalin A (Con A)-layered calcium alginate beads

Abstract

Cellulase has been immobilized on hybrid concanavalin A (Con A)-layered calcium alginate–starch beads. Immobilized cellulase retained about 82% of its activity. Con A was extracted from jack bean and the obtained crude protein was characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis. The immobilized beads showed high mechanical and storage stability; immobilized cellulase retained 100% and 85% activity at 4°C and 30°C, respectively, over one month. The immobilized cellulase retained about 70% of its activity after five cycles of use. The immobilized cellulase retained 70% activity after 120-min exposure to 60°C, whereas the soluble form only retained about 20%, showing that immobilization improved thermal stability. Surface morphology and elemental analysis of immobilized cellulase were examined using scanning electron microscope equipped with energy-dispersive X-ray. Based on the enzyme stability and reuse, this method of immobilization is both convenient and cheap.

Keywords::

• Cellulase
• immobilization
• calcium alginate
• bioaffinity
• concanavalin A

Acknowledgements

The authors gratefully acknowledge the funding support by the University Grants Commission (UGC), India under Basic Scientific Research (BSR) scheme, grant no: F.7.288/2009 (BSR). The authors would also like to acknowledge United Alacrity Pvt. Ltd, Chennai, India for providing cellulase.

Declaration of interest: The authors report no declarations of interest. The authors alone are responsible for the content and writing of the paper.