Linked Life Data

19554325

Source:http://linkedlifedata.com/resource/pubmed/id/19554325

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2009-11-5
pubmed:abstractText
The operational stabilities of nitrilases from Aspergillus niger K10 and Fusarium solani O1 were examined with 4-cyanopyridine as the substrate in continuous-stirred membrane reactors (CSMRs). The former enzyme was fairly stable at 30 degrees C with a deactivation constant (k (d)) and enzyme half-life of 0.014 h(-1) and 50 h, respectively, but the latter exhibited an even higher stability characterized by k (d) = 0.008 h(-1) and half-life of 87 h at 40 degrees C. Another advantage of this enzyme was its high chemoselectivity, i.e., selective transformation of nitriles into carboxylic acids, while the amide formed a high ratio of A. niger K10 nitrilase product. High conversion rates (>90%) were maintained for about 52 h using the nitrilase from F. solani O1 immobilized in cross-linked enzyme aggregates (CLEAs). The purity of isonicotinic acid was increased from 98% to >99.9% by using two CSMRs connected in series, the first one containing the F. solani O1 nitrilase and the second the amidase from Rhodococcus erythropolis A4 (both enzymes as CLEAs), the amidase hydrolyzing the by-product isonicotinamide.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1432-0614
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
85
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
277-84
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Continuous hydrolysis of 4-cyanopyridine by nitrilases from Fusarium solani O1 and Aspergillus niger K10.
pubmed:affiliation
Department of Chemistry, Chemical Engineering and Materials, University of l'Aquila, Monteluco di Roio, 67040 l'Aquila, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't