Linked Life Data

12665670

Source:http://linkedlifedata.com/resource/pubmed/id/12665670

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2003-3-31
pubmed:abstractText
Glutaryl-7-aminocephalosporanic acid (GL-7-ACA) acylase is an enzyme that converts GL-7-ACA to 7-aminocephalosporanic acid, a starting material for semisynthetic cephalosporin antibiotics. In this study, optimal conditions for the immobilization of GL-7-ACA acylase were determined by experimental observations and statistical methods. The optimal conditions were as follows: 1.1 M phosphate buffer (pH 8.3) as buffer solution, immobilization temperature of 20 degrees C, and immobilization time of 120 min. Unreacted aldehyde groups were quenched by reaction with a low-molecular-weight material such as L-lysine, glycine, and ethanolamine after immobilization in order to enhance the activity of immobilized GL-7-ACA acylase. The activities of immobilized GL-7-ACA acylase obtained by using the low-molecular-weight materials were higher than those obtained by immobilized GL-7-ACA acylase not treated with low-molecular-weight materials. In particular, the highest activity of immobilized GL-7-ACA acylase was obtained using 0.4% (v/v) ethanolamine. We also investigated the effect of sodium cyanoborohydride in order to increase the stability of the linkage between the enzyme and the support. The effect on operational stability was obvious: the activity of immobilized GL-7-ACA acylase treated with 4% (w/w) sodium cyanoborohydride remained almost 100% after 20 times of reuse.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/7-aminocephalosporanic acid, http://linkedlifedata.com/resource/pubmed/chemical/Borohydrides, http://linkedlifedata.com/resource/pubmed/chemical/Cephalosporins, http://linkedlifedata.com/resource/pubmed/chemical/Enzymes, Immobilized, http://linkedlifedata.com/resource/pubmed/chemical/Ethanolamine, http://linkedlifedata.com/resource/pubmed/chemical/Penicillin Amidase, http://linkedlifedata.com/resource/pubmed/chemical/Silica Gel, http://linkedlifedata.com/resource/pubmed/chemical/Silicon Dioxide, http://linkedlifedata.com/resource/pubmed/chemical/glutaryl-7-aminocephalosporanic acid, http://linkedlifedata.com/resource/pubmed/chemical/glutarylamidocephalosporanic acid..., http://linkedlifedata.com/resource/pubmed/chemical/sodium cyanoborohydride
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0273-2289
pubmed:author
pubmed:issnType
Print
pubmed:volume
104
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
185-98
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Immobilization of glutaryl-7-aminocephalosporanic acid acylase on silica gel and enhancement of its stability.
pubmed:affiliation
Department of Chemical and Biological Engineering, Korea University, 1 Anam-dong, Sungbuk-ku, Seoul 136-701, Korea.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't, Evaluation Studies, Validation Studies