Linked Life Data

16961324

Source:http://linkedlifedata.com/resource/pubmed/id/16961324

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2006-9-11
pubmed:abstractText
Lipases from Candida rugosa (CRL) and lipase isoforms A and B from Candida antarctica (CAL-A and CAL-B) were adsorbed on aminated supports in the presence of detergents to have individual lipase molecules. Then, one fraction was washed to eliminate the detergent, and both preparations were treated with glutaraldehyde. The presence of detergent during the cross-linking of the lipases to the support permitted an increase in the recovered activity (in some instances, even by a 10-fold factor). This activity was higher even than that exhibited by the just adsorbed lipases, suggesting that it was not a result of some protective effect of the detergent in the enzyme activity during glutaraldehyde chemical modification. Moreover, the enantioselectivity of the different enzyme preparations was very different if the glutaraldehyde was offered in the presence or in the absence of detergent, in some cases increasing the E value (even by a 7-fold factor in the case of CAL-A in the hydrolysis of (+/-)-2-hydroxy-4-phenylbutyric acid ethyl ester), in other cases even inverting the enantio preference (e.g., in the case of CRL). The irreversible chemical inhibition of the enzyme that was immobilized and cross-linked with glutaraldehyde in the presence of detergents was more rapid than that in the other preparations (by more than a 10-fold factor). This experiment reveals an exposition degree of the active serine in the preparation cross-linked with the support in the presence of detergent that is higher than that in the other preparations. The results suggested that different enzyme structures were "stabilized" by the glutaraldehyde treatment if performed in the presence or in the absence of detergent, and that, in the presence of detergent, a form of the lipase with the serine residue more exposed to the medium and much more active could be obtained. This strategy seems to be of general use to improve the lipase activity to be used in macroaqueous media.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1525-7797
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2610-5
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Glutaraldehyde cross-linking of lipases adsorbed on aminated supports in the presence of detergents leads to improved performance.
pubmed:affiliation
Departamento de Biocatálisis, Instituto de Catálisis -CSIC, Campus UAM, Cantoblanco, Madrid, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't