Back to Search
Start Over
Immobilization of glucosyltransferase from Erwinia sp. using two different techniques.
- Source :
-
Journal of biotechnology [J Biotechnol] 2012 Apr 15; Vol. 158 (3), pp. 137-43. Date of Electronic Publication: 2012 Jan 24. - Publication Year :
- 2012
-
Abstract
- Two different techniques of glucosyltransferase immobilization were studied for the conversion of sucrose into isomaltulose. The optimum conditions for immobilization of Erwinia sp. glucosyltransferase onto Celite 545, determined using response surface methodology, was pH 4.0 and 170 U of glucosyltransferase/g of Celite 545. Using this conditions more than 60% conversion of sucrose into isomaltulose can be obtained. The immobilization of glucosyltransferase was also studied by its entrapment in microcapsules of low-methoxyl pectin and fat (butter and oleic acid). The non-lyophilized microcapsules of pectin, containing the enzyme and fat, showed higher glucosyltransferase activity, compared with lyophilized microcapsules containing enzyme plus fat, and also lyophilized microcapsules containing enzyme without fat addition. The non-lyophilized microcapsules of pectin containing the glucosyltransferase and fat, converted 30% of sucrose into isomaltulose in the first batch. However the conversion decreased to 5% at the 10th batch, indicating inactivation of the enzyme.<br /> (Copyright © 2012 Elsevier B.V. All rights reserved.)
- Subjects :
- Capsules
Hydrogen-Ion Concentration
Isomaltose chemical synthesis
Isomaltose chemistry
Pectins chemistry
Bacterial Proteins chemistry
Diatomaceous Earth chemistry
Enzymes, Immobilized chemistry
Erwinia enzymology
Glucosyltransferases chemistry
Isomaltose analogs & derivatives
Sucrose chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1873-4863
- Volume :
- 158
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Journal of biotechnology
- Publication Type :
- Academic Journal
- Accession number :
- 22306307
- Full Text :
- https://doi.org/10.1016/j.jbiotec.2012.01.012