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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 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.