Controlling the aggregation propensity and thereby digestibility of allergens by Maillardation as illustrated for cod fish parvalbumin

Journal of Bioscience and Bioengineering

Volumn 111, Issue 2, 2011, Pages 204-211

  De Jongh, Harmen H J ^a   Taylor, Steve L ^b   Koppelman, Stef J ^b,c  

^a TOP INSTITUTE FOOD AND NUTRITION   (Netherlands)

^b UNIVERSITY OF NEBRASKA LINCOLN   (United States)

^c HAL Allergy   (Netherlands)

Author keywords

Allergen; Digestibility; Maillardation; Protein aggregation; Thermodynamics

Indexed keywords

AGGREGATION KINETICS; AGGREGATION PROCESS; AGGREGATION PROPENSITY; ALLERGEN; ALLERGIC RESPONSE; AMBIENT CONDITIONS; CALCIUM BINDING; CIRCULAR DICHROISM; COD FISH; DENATURATION PROCESS; DENATURATION TEMPERATURES; DENATURED STATE; DIGESTIBILITY; EFFECTIVE TOOL; FOOD CONSUMPTION; FREE ENERGY CHANGE; GLUCOSYLATION; HEAT CAPACITIES; HEAT-TREATED MATERIALS; LYSINE RESIDUES; MAILLARDATION; PARVALBUMIN; PROTEIN AGGREGATION; PROTEIN SURFACE; SCATTERING TECHNIQUES; SHAPE AND SIZE;

AGGLOMERATION; ALLERGIES; AMINO ACIDS; ANTIGENS; DENATURATION; DICHROISM; FOOD SUPPLY; GLUCOSE; HYDROPHOBICITY; SLOW LIGHT; THERMODYNAMICS;

PROTEINS;

ALLERGEN; GLUCOSE; LYSINE; PARVALBUMIN; PEPSIN A;

ARTICLE; CALCIUM BINDING; CIRCULAR DICHROISM; DENATURATION; DIGESTION; ENVIRONMENTAL TEMPERATURE; FISH; FLUORESCENCE ANALYSIS; HEAT TREATMENT; HYDROPHOBICITY; LIGHT SCATTERING; NONHUMAN; PROTEIN FOLDING; PROTEIN STRUCTURE;

ALLERGENS; ANIMALS; CALORIMETRY, DIFFERENTIAL SCANNING; CIRCULAR DICHROISM; GADIFORMES; HOT TEMPERATURE; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MAILLARD REACTION; PARVALBUMINS; PROTEIN DENATURATION; PROTEIN FOLDING; SEAFOOD; SPECTROMETRY, FLUORESCENCE; THERMODYNAMICS;

EID: 78951484854     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2010.09.015     Document Type: Article

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