Linked Life Data

18292248

Source:http://linkedlifedata.com/resource/pubmed/id/18292248

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2008-2-22
pubmed:abstractText
This study evaluates the use of high pressure to enhance pepsin hydrolysis of beta-lactoglobulin (beta-LG). The protein was subjected to high pressure before and during the proteolytic process. Analysis of remnant beta-LG, identification of the peptides produced, and evaluation of antigenicity (binding to commercial antibodies) and binding to IgE of allergic patients' sera were conducted in the hydrolysates. The results showed that the application of high pressure before the enzyme treatment slightly improved the proteolytic process but did not reduce the antigenicity or IgE binding of the hydrolysates. The application of high pressure during the enzymatic treatment enhanced the production of large intermediate fragments that were further proteolysed to smaller fragments as proteolysis proceeded for longer periods. At 400 MPa, all the intact protein was removed in minutes, simultaneously decreasing its antigenicity and serum IgE binding properties. However, for considerable reduction of the antigenicity and IgE binding of beta-LG, extending the incubation time with the enzyme was needed to reduce the amount of potentially allergenic intermediate peptides. Changes of beta-LG under pressure at acidic pH are discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1525-3198
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
91
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
928-38
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Proteolytic pattern, antigenicity, and serum immunoglobulin E binding of beta-lactoglobulin hydrolysates obtained by pepsin and high-pressure treatments.
pubmed:affiliation
Instituto de Fermentaciones Industriales, Consejo Superior de Investigaciónes Científicas, Madrid, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't