Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2002-5-6
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9673
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
950
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
131-7
pubmed:dateRevised
2009-1-15
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Purification of a bacterial pullulanase on a fluidized bed of calcium alginate beads.
pubmed:affiliation
Chemistry Department, Indian Institute of Technology, Hauz Khas, New Delhi.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't