Novel thermally and mechanically stable hydrogel for enzyme immobilization of penicillin G acylase via covalent technique
?-Carrageenan hydrogel crosslinked with protonated polyethyleneimine (PEI+) and glutaraldehyde (GA) was prepared and evaluated as a novel biocatalytic support for covalent immobilization of penicillin G acylase (PGA). The method of modification of the carrageenan biopolymer is clearly illustrated us...
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| Format: | Journal Article |
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John Wiley and Sons Inc
2008
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| Online Access: | http://hdl.handle.net/20.500.11937/48366 |
| _version_ | 1848758089221668864 |
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| author | Elnashar, Magdy Yassin, M. Kahil, T. |
| author_facet | Elnashar, Magdy Yassin, M. Kahil, T. |
| author_sort | Elnashar, Magdy |
| building | Curtin Institutional Repository |
| collection | Online Access |
| description | ?-Carrageenan hydrogel crosslinked with protonated polyethyleneimine (PEI+) and glutaraldehyde (GA) was prepared and evaluated as a novel biocatalytic support for covalent immobilization of penicillin G acylase (PGA). The method of modification of the carrageenan biopolymer is clearly illustrated using a schematic diagram and was verified by FTIR, elemental analysis, DSC, and INSTRON using the compression mode. Results showed that the gels' mechanical strength was greatly enhanced from 3.9 kg/cm2 to 16.8 kg/cm 2 with an outstanding improvement in the gels thermal stability. It was proven that, the control gels were completely dissolved at 35°C, whereas the modified gels remained intact at 90°C. The DSC thermogram revealed a shift in the endothermic band of water from 62 to 93°C showing more gel-crosslinking. FTIR revealed the presence of the new functionality, aldehydic carbonyl group, at 1710 cm-1 for covalent PGA immobilization. PGA was successfully immobilized as a model industrial enzyme retaining 71% of its activity. The enzyme loading increased from 2.2 U/g (control gel) to 10 U/g using the covalent technique. The operational stability showed no loss of activity after 20 cycles. The present support could be a good candidate for the immobilization of industrial enzymes rich in amino groups, especially the thermophilic ones. © 2008 Wiley Periodicals, Inc. |
| first_indexed | 2025-11-14T09:38:26Z |
| format | Journal Article |
| id | curtin-20.500.11937-48366 |
| institution | Curtin University Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-14T09:38:26Z |
| publishDate | 2008 |
| publisher | John Wiley and Sons Inc |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | curtin-20.500.11937-483662017-09-13T14:20:16Z Novel thermally and mechanically stable hydrogel for enzyme immobilization of penicillin G acylase via covalent technique Elnashar, Magdy Yassin, M. Kahil, T. ?-Carrageenan hydrogel crosslinked with protonated polyethyleneimine (PEI+) and glutaraldehyde (GA) was prepared and evaluated as a novel biocatalytic support for covalent immobilization of penicillin G acylase (PGA). The method of modification of the carrageenan biopolymer is clearly illustrated using a schematic diagram and was verified by FTIR, elemental analysis, DSC, and INSTRON using the compression mode. Results showed that the gels' mechanical strength was greatly enhanced from 3.9 kg/cm2 to 16.8 kg/cm 2 with an outstanding improvement in the gels thermal stability. It was proven that, the control gels were completely dissolved at 35°C, whereas the modified gels remained intact at 90°C. The DSC thermogram revealed a shift in the endothermic band of water from 62 to 93°C showing more gel-crosslinking. FTIR revealed the presence of the new functionality, aldehydic carbonyl group, at 1710 cm-1 for covalent PGA immobilization. PGA was successfully immobilized as a model industrial enzyme retaining 71% of its activity. The enzyme loading increased from 2.2 U/g (control gel) to 10 U/g using the covalent technique. The operational stability showed no loss of activity after 20 cycles. The present support could be a good candidate for the immobilization of industrial enzymes rich in amino groups, especially the thermophilic ones. © 2008 Wiley Periodicals, Inc. 2008 Journal Article http://hdl.handle.net/20.500.11937/48366 10.1002/app.28379 John Wiley and Sons Inc restricted |
| spellingShingle | Elnashar, Magdy Yassin, M. Kahil, T. Novel thermally and mechanically stable hydrogel for enzyme immobilization of penicillin G acylase via covalent technique |
| title | Novel thermally and mechanically stable hydrogel for enzyme immobilization of penicillin G acylase via covalent technique |
| title_full | Novel thermally and mechanically stable hydrogel for enzyme immobilization of penicillin G acylase via covalent technique |
| title_fullStr | Novel thermally and mechanically stable hydrogel for enzyme immobilization of penicillin G acylase via covalent technique |
| title_full_unstemmed | Novel thermally and mechanically stable hydrogel for enzyme immobilization of penicillin G acylase via covalent technique |
| title_short | Novel thermally and mechanically stable hydrogel for enzyme immobilization of penicillin G acylase via covalent technique |
| title_sort | novel thermally and mechanically stable hydrogel for enzyme immobilization of penicillin g acylase via covalent technique |
| url | http://hdl.handle.net/20.500.11937/48366 |