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Please use this identifier to cite or link to this item: http://eprint.iitd.ac.in/handle/2074/1030

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dc.contributor.authorRoy, Ipsita-
dc.contributor.authorGupta, Munishwar N-
dc.identifier.citationJournal of Chromatography A, 950(1-2), 131-137en
dc.description.abstractPullulanase 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
dc.format.extent112897 bytes-
dc.titlePurification of a bacterial pullulanase on a fluidized bed of calcium alginate beadsen
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