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Cross-linked enzyme aggregates of alginate lyase: A systematic engineered approach to controlled degradation of alginate hydrogel
- Kunjukunju, Sangeetha, Roy, Abhijit, Shekhar, Sudhanshu, Kumta, Prashant N.
- International journal of biological macromolecules 2018 v.115 pp. 176-184
- alginate lyase, alginates, ammonium sulfate, catalytic activity, crosslinking, encapsulation, enzyme activity, glutaraldehyde, hydrogels, pH, solvents, storage quality, temperature, thermal stability
- An enzyme aggregate of alginate lyase (EC 126.96.36.199) from flavobactierium was prepared using ammonium sulfate. The resultant aggregates upon cross-linking with glutaraldehyde produced insoluble and catalytically active cross-linked enzyme aggregate (CLEA) enzyme. The catalytic activity and stability of the cross-linked enzyme aggregate of alginate lyase (CLEA-AL) was studied in the presence of various pH, temperatures and organic solvents. Reusability, storage stability and surface morphology of the CLEA-AL were also studied. The native enzyme and CLEA-AL exhibited maximum enzyme activity at pH of 6.3 and at a temperature of 40°C. The CLEA-AL has good stability in nonpolar organic solvents and is thermally stable up to 50°C over a period of 8h. By encapsulating CLEA-AL into alginate hydrogel, we demonstrate that alginate hydrogels can be enzymatically degraded in a controlled fashion. The results also showed that degradation of alginate hydrogel with CLEA-AL incorporated beads is slower than native enzyme and therefore, CLEA-AL can be used for controlled degradation and release of various biologics from the degrading gel.