Document Detail


Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein.
MedLine Citation:
PMID:  20205191     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Crosslinking enzymes are frequently used in bioprocessing of dairy products. The aim of this study was to examine the effects of enzymatic crosslinking on IgE binding, allergenicity and digestion stability of beta-casein (CN). beta-CN was crosslinked by transglutaminase, tyrosinase, mushroom tyrosinase/caffeic acid and laccase/caffeic acid. The IgE binding to beta-CN was compared in vitro by CAP inhibition assay, ELISA inhibition as well as ex vivo by basophil activation assay. Crosslinked CNs were digested by simulated gastric fluid for 15 and 60 min and obtained digests analyzed for their ability to inhibit IgE binding by CAP inhibition assay and SDS-PAGE. The ability of crosslinked CNs to activate basophils was significantly reduced in seven patients in the case of CN crosslinked by laccase and moderately reduced in the case of tyrosinase/caffeic acid crosslinked CN (in two cow's milk allergy patients tested with different allergen concentrations). The response to various crosslinked CNs differed individually among patients' sera tested by ELISA inhibition assay. The presence of caffeic acid hampered digestion by pepsin, and this effect was most pronounced for the tyrosinase/caffeic acid crosslinked CN. The laccase/caffeic acid and mushroom tyrosinase/caffeic acid had the highest potential in mitigating IgE binding and allergenicity of the beta-CN out of all investigated enzymes. The presence of a small phenolic compound also increased digestion stability of beta-CN.
Authors:
Dragana Stanic; Evanthia Monogioudi; Ercili Dilek; Jelena Radosavljevic; Marina Atanaskovic-Markovic; Olga Vuckovic; Lantto Raija; Maija Mattinen; Johanna Buchert; Tanja Cirkovic Velickovic
Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Molecular nutrition & food research     Volume:  54     ISSN:  1613-4133     ISO Abbreviation:  Mol Nutr Food Res     Publication Date:  2010 Sep 
Date Detail:
Created Date:  2010-09-08     Completed Date:  2011-01-27     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101231818     Medline TA:  Mol Nutr Food Res     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  1273-84     Citation Subset:  IM    
Affiliation:
Department of Chemistry, Institute of Chemistry, Technology and Metallurgy, University of Belgrade, Belgrade, Serbia.
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MeSH Terms
Descriptor/Qualifier:
Adolescent
Allergens / chemistry,  immunology*,  metabolism*
Basophil Degranulation Test
Caffeic Acids / metabolism
Caseins / chemistry,  immunology*,  metabolism*
Child, Preschool
Digestion*
Enzyme-Linked Immunosorbent Assay
Food Handling / methods
Humans
Immunoglobulin E / immunology,  metabolism
Kinetics
Laccase / metabolism
Milk Hypersensitivity / blood,  immunology*
Monophenol Monooxygenase / metabolism
Polymerization
Protein Hydrolysates / chemistry,  immunology*,  metabolism
Transglutaminases / metabolism
Chemical
Reg. No./Substance:
0/Allergens; 0/Caffeic Acids; 0/Caseins; 0/Protein Hydrolysates; 331-39-5/caffeic acid; 37341-29-0/Immunoglobulin E; EC 1.10.3.2/Laccase; EC 1.14.18.1/Monophenol Monooxygenase; EC 2.3.2.13/Transglutaminases

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


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