| Authors: | Kunjukunju, Sangeetha; Roy, Abhijit; Shekhar, Sudhanshu; Kumta, Prashant N. |
| Title: | Cross-linked enzyme aggregates of alginate lyase: A systematic engineered approach to controlled degradation of alginate hydrogel |
| Type: | Journal Article |
| Publisher: | International Journal of Biological Macromolecules
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| Year: | 2018 |
| Volume: | 115 |
| Issue: | |
| Start Page: | 176-184 |
| End Page: | |
| DOI: | 10.1016/j.ijbiomac.2018.03.110 |
| WEB-link: | http://www.sciencedirect.com/science/article/pii/S0141813018303465 |
| Abstract: | An enzyme aggregate of alginate lyase (EC 4.2.2.3) 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 40ýC. The CLEA-AL has good stability in nonpolar organic solvents and is thermally stable up to 50ýC 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.
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| Keywords: | Enzyme immobilization |
| File: | (1476K) |
