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Please use this identifier to cite or link to this item:
http://hdl.handle.net/2074/1030
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Full metadata record
| DC Field | Value | Language |
|---|
| contributor.author | Roy, Ipsita | - |
| contributor.author | Gupta, Munishwar N | - |
| date.accessioned | 2005-12-22T07:11:50Z | - |
| date.available | 2005-12-22T07:11:50Z | - |
| date.issued | 2002 | - |
| identifier.citation | Journal of Chromatography A, 950(1-2), 131-137 | en |
| identifier.uri | http://eprint.iitd.ac.in/dspace/handle/2074/1030 | - |
| description.abstract | Pullulanase from Bacillus acidopullulyticus was purified on a packed bed and a fluidized bed of calcium alginate beads. The binding of enzyme activity to the medium was found to follow Langmuir isotherm pattern. The maximum binding capacity was 1476 U ml−1 matrix and the dissociation constant was 142 U ml−1. The dynamic binding capacities at 5% breakthrough in the packed and fluidized beds were 472 U ml−1 and 644 U ml−1, respectively. In the packed bed as well as the fluidized bed, an activity recovery of more than 95% with fold purification in the range of 46–59 was observed. The elution with a competitive inhibitor, viz. maltose, and high-fold purification indicate an affinity-based process. The purification process worked equally well with columns of bed volumes of 3.8 and 10 ml. | en |
| format.extent | 112897 bytes | - |
| format.mimetype | application/pdf | - |
| language.iso | en | en |
| subject | Pullulanase | en |
| subject | Enzymes | en |
| title | Purification of a bacterial pullulanase on a fluidized bed of calcium alginate beads | en |
| type | Article | en |
| Appears in Collections: | Chemistry
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| File |
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Size | Format |
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| purroy2002.pdf | | 110Kb | Adobe PDF | View/Open |
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