Document Detail


Hydrolysis under high hydrostatic pressure as a means to reduce the binding of beta-lactoglobulin to immunoglobulin E from human sera.
MedLine Citation:
PMID:  18680946     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Cows' milk allergy is the most frequent food allergy in children, and beta-lactoglobulin (beta-Lg) is a major allergen. Milk-based hypoallergenic ingredients are manufactured by enzymatic hydrolysis, a process that could be improved by the application of high-pressure treatments. This study showed that the treatment of beta-Lg dissolved in buffer with chymotrypsin and trypsin under high pressure for relatively short times accelerated proteolysis by leading to a rapid removal of the intact protein. The rapid proteolysis of the beta-Lg substrate under pressure led to the production, in 20 min, of hydrolysates with lower immunoglobulin (Ig) G binding than those produced in 8 h (chymotrypsin) or 48 h (trypsin) at atmospheric pressure. However, those hydrolysates retained some residual IgE-binding properties that could be traced to the preferential release, during the initial stages of proteolysis, of peptides containing IgE epitopes, such as (Val-41-Lys-60), (Leu-149-Ile-162), and (Ser-21-Arg-40). The formation of these fragments was favored when proteolysis was conducted under high pressure due to the preferential hydrolysis of Arg-40 and Arg-148 by trypsin, and Tyr-42 and Leu-149 by chymotrypsin, all located at the dimer interface of beta-Lg or very close to it. Although our results do not support that trypsin and chymotrypsin under high pressure selectively address the allergenic regions of beta-Lg, it is possible to select the conditions that quickly produce hydrolysates with reduced potential allergenicity that could be used in hypoallergenic foods.
Authors:
R Chicón; J Belloque; E Alonso; P J Martín-Alvarez; R López-Fandiño
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of food protection     Volume:  71     ISSN:  0362-028X     ISO Abbreviation:  J. Food Prot.     Publication Date:  2008 Jul 
Date Detail:
Created Date:  2008-08-06     Completed Date:  2008-09-02     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7703944     Medline TA:  J Food Prot     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1453-9     Citation Subset:  IM    
Affiliation:
Instituto de Fermentaciones Industriales (CSIC), Juan de la Cierva 3, 28006 Madrid, Spain.
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MeSH Terms
Descriptor/Qualifier:
Animals
Chromatography, High Pressure Liquid
Chymotrypsin / metabolism
Epitopes
Hydrolysis
Hydrostatic Pressure*
Immunoglobulin E / immunology,  metabolism*
Lactoglobulins / immunology,  metabolism*
Milk / enzymology*,  metabolism
Milk Hypersensitivity / immunology,  prevention & control
Peptide Fragments
Time Factors
Trypsin / metabolism
Chemical
Reg. No./Substance:
0/Epitopes; 0/Lactoglobulins; 0/Peptide Fragments; 37341-29-0/Immunoglobulin E; EC 3.4.21.1/Chymotrypsin; EC 3.4.21.4/Trypsin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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