Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/10397
Share/Export:
logo share SHARE logo core CORE BASE
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE
Title

Proteolytic pattern, antigenicity, and serum immunoglobulin E binding of ß-Lactoglobulin hydrolysates obtained by pepsin and high-pressure treatments

AuthorsChicón, Rosa; López-Fandiño, Rosina CSIC ORCID ; Alonso, Elena; Belloque, Josefina CSIC ORCID
KeywordsMilk whey protein
Allergens
High pressure
Proteolysis
Issue DateMar-2008
PublisherAmerican Dairy Science Association
CitationJournal of Dairy Science 91(3): 928-938 (2008)
AbstractThis study evaluates the use of high pressure to enhance pepsin hydrolysis of β-lactoglobulin (β-LG). The protein was subjected to high pressure before and during the proteolytic process. Analysis of remnant β-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 β-LG, extending the incubation time with the enzyme was needed to reduce the amount of potentially allergenic intermediate peptides. Changes of β-LG under pressure at acidic pH are discussed.
Description11 pages.-- PMID: 18292248 [PubMed].
Interpretive summary available at: http://jds.fass.org/cgi/data/91/3/928/DC1/1
Publisher version (URL)http://dx.doi.org/10.3168/jds.2007-0657
URIhttp://hdl.handle.net/10261/10397
DOI10.3168/jds.2007-0657
ISSN0022-0302
Appears in Collections:(IFI) Artículos

Show full item record
Review this work

SCOPUSTM   
Citations

53
checked on May 27, 2022

WEB OF SCIENCETM
Citations

46
checked on May 22, 2022

Page view(s)

383
checked on May 27, 2022

Google ScholarTM

Check

Altmetric

Dimensions


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.