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Please use this identifier to cite or link to this item:
http://hdl.handle.net/2074/965
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| DC Field | Value | Language |
|---|
| contributor.author | Roy, Ipsita | - |
| contributor.author | Sastry, M S R | - |
| contributor.author | Johri, B N | - |
| contributor.author | Gupta, Munishwar N | - |
| date.accessioned | 2005-10-19T05:34:44Z | - |
| date.available | 2005-10-19T05:34:44Z | - |
| date.issued | 2000 | - |
| identifier.citation | Protein Expression and Purification, 20(2), 162–168 | en |
| identifier.uri | http://eprint.iitd.ac.in/dspace/handle/2074/965 | - |
| description.abstract | An a-amylase has been purified from the thermophilic fungus Scytalidium hermophilum. A ninefold purification was achieved in a single step using fluidized bed chromatography wherein alginate was used as the affinity matrix. There are at least two isoenzymes as shown by concanavalin A (Con A)–agarose column chromatography. The isoenzyme binding to Con A is stable for at least 3 h at 80°C in the presence of calcium ions. The isoenzymes have similar molecular weights of around 45,000 Da as shown by SDS PAGE analysis. The isoenzymes differ only slightly in their pH optima and temperature optima but the isoenzyme binding to Con A–agarose has slightly higher thermal stability. | en |
| format.extent | 1678122 bytes | - |
| format.mimetype | application/pdf | - |
| language.iso | en | en |
| subject | a-amylase | en |
| subject | fluidized bed | en |
| subject | chromatography | en |
| subject | alginate beads | en |
| subject | s. thermophilum | en |
| subject | thermostable enzymes. | en |
| title | Purification of a-amylase isoenzymes from scytalidium thermophilum on a fluidized bed of alginate beads followed by concanavalin a-agarose column chromatography | en |
| type | Article | en |
| Appears in Collections: | Chemistry
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| File |
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Size | Format |
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| roypur2000.pdf | | 1638Kb | Adobe PDF | View/Open |
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