Linked Life Data

20865388

Source:http://linkedlifedata.com/resource/pubmed/id/20865388

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2010-9-24
pubmed:abstractText
While biocatalysts show tremendous potential for the industrial production of fine chemicals, their integration into large-scale processes has been slow. One of the main reasons for slow acceptance in industry is the inherent instability of the enzymes. Recent developments in bioengineering have shed some light on methods of improving enzyme stability. One method that has been used for many decades, successfully to varying degrees, has been the immobilization of enzymes. To this regards, silica gels have attracted much attention because of the ease of surface functionalization, high surface areas, mechanical and thermal stability, and resistance to both chemical and biological attack. We have previously shown the immobilization of invertase on silica gels with high immobilized activity and significantly improved stability. Here, we provide greater details on the methods for effecting the immobilization.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1940-6029
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
679
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
49-66
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Enzyme stabilization and immobilization by sol-gel entrapment.
pubmed:affiliation
Department of Chemical and Biomolecular Engineering, University of Maryland, College Park, MD, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural