https://digitalcommons.unl.edu/cgi/viewcontent.cgi?article=1214&context=foodsciefacpub

Food processing and allergenicity

Food protein functionality: A comprehensive approach

Background Food allergy is one of the major health concerns worldwide that has been increasing at an alarming rate in recent times. Foods undergo various processing steps before consumption that could affect conformation of food proteins, their digestion and thereby allergenicity. Scope and approach This review summarizes the effect of various processing methods on structural changes of major food allergens and how these changes affect their digestibility as well as allergenicity. This information could be a base line for selecting suitable food processing parameters for management of food allergies. Key findings and conclusions Most physical processes (heat, pressure, radiation, and ultrasound) affect conformational epitopes (destroy, mask or expose) of food proteins by altering their secondary and tertiary structures whereas the linear/sequential epitopes are affected mainly through bio-chemical (fermentation and enzymatic hydrolysis) treatments. Processing may also influence the interaction of food proteins with other ingredients via Maillard reaction and give rise to formation of new allergenic compound (neo-allergens). Processing induced changes to food proteins can largely affect their susceptibility to gastrointestinal digestion, absorption kinetics and consequently their allergenic response to immune system. Therefore, allergenic potential of food proteins may be minimized by selecting appropriate parameters during processing. Allergenicity of certain food proteins can also be modulated through optimized formulation with other food matrices. However, depending on the method of processing, intensity of treatment and molecular characteristics of allergen food proteins, allergenicity can be increased, decreased or remain unaltered.

Effect of processing on conformational changes of food proteins related to allergenicity

Following a request from the Food Safety Authority of Ireland, the EFSA Panel on Dietetic Products, Nutrition and Allergies (NDA Panel) was asked to deliver a scientific opinion on the evaluation of allergenic foods and food ingredients for labelling purposes In view of the request, the NDA Panel decided to update its previous opinions relative to food ingredients or substances with known allergenic potential listed in Annex IIIa of 2003/89/EC, as amended These include cereals containing gluten, milk and dairy products, eggs, nuts, peanuts, soy, fish, crustaceans, molluscs, celery, lupin, sesame, mustard and sulphites The opinion relates to immunoglobulin (Ig)E- and non-IgE-mediated food allergy, to coeliac disease and to adverse reactions to sulphites in food, and it does not address non-immune-mediated adverse reactions to food It includes information on the prevalence of food allergy in unselected populations, proteins identified as food allergens, cross-reactivities, the effects of food processing on the allergenicity of foods and ingredients, methods for the detection of allergens and allergenic foods, doses observed to trigger adverse reactions in sensitive individuals and risk assessment methodologies that have been used to derive individual and population thresholds for selected allergenic foods

Scientific Opinion on the evaluation of allergenic foods and food ingredients for labelling purposes

The scientific evidence for the role of milk protein-derived bioactive peptides in humans: a review

The effect of heat treatment on the antigenicity of α-lactalbumin (α-LA) and β-lactoglobulin (β-LG) in whey protein isolate (WPI) was investigated at temperatures in the range of 50–120°C for times from 0.5 to 30 min. The antigenicity was determined by an indirect competitive enzyme-linked immunosorbent assay. The heat denaturation of α-LA and β-LG was revealed by SDS-PAGE electrophoresis. The antigenicity of α-LA and β-LG increased with increasing temperature from 50 to 90°C and the highest antigenicity of α-LA and β-LG was detected at 90°C. However, above 90°C the antigenicity of both proteins showed a remarkable decrease. When treated at 120°C for 20 min, the antigenicity of α-LA decreased below the initial value of the untreated sample. The antigenicity of α-LA and β-LG in WPI can be decreased at certain heat temperature and time.

Effect of heat treatment on the antigenicity of bovine α-lactalbumin and β-lactoglobulin in whey protein isolate

BACKGROUND: Maillard reaction can modify functional properties of proteins. Bovine α-lactalbumin (α-LA) is often supplemented to the new generation of infant formulae, but it is considered to be a main allergen. However, there is little information on the effect of Maillard reaction on α-LA antigenicity. The objective of this study was to investigate the influence of Maillard reaction on the antigenicity of α-LA in conjugates of whey protein isolate (WPI) with glucose under different conditions of protein/sugar weight ratio (0.17–7.83), temperature (40–60 °C) and time (24–120 h) using response surface methodology.



RESULTS: Conjugation of WPI with glucose markedly reduced the antigenicity of α-LA. This reduction in antigenicity could be controlled by regulating the three independent variables weight ratio, temperature and time. A model of optimal reaction conditions for lower antigenicity of α-LA was established. According to the model, the minimum antigenicity of α-LA was achieved at 52.8 °C, 78 h and 5.96:1 WPI/glucose weight ratio. WPI/glucose weight ratio had the greatest effect on the antigenicity of α-LA, while reaction temperature influenced α-LA antigenicity to a lesser extent.



CONCLUSION: Well-controlled Maillard reaction between WPI and glucose is an efficient method to reduce α-LA antigencity. Copyright © 2009 Society of Chemical Industry

Influence of Maillard reaction conditions on the antigenicity of bovine α-lactalbumin using response surface methodology

Whey proteins are widely used as food material, but their functional properties are affected by processing conditions, in which Maillard reaction commonly occurs. The objective of this study was to investigate the effects of reaction conditions (saccharide rate (SR), setting time and setting temperature) on the functional properties of conjugates of whey protein isolates (WPI) - chitosan oligosaccharide (COS), which were produced by Maillard reaction. Response surface methodology (RSM) was used in this study, models for solubility, heat stability (HS), emulsifying activity (EA) and emulsifying stability (ES) of WPI-COS were established. Results indicated that the solubility of WPI-COS was 98.8 % at 29.8 % SR, 17.4 h, 46.7 °C; the heat stability of WPI-COS was 92.95 % at 27.2 % SR, 18.1 h, 48.7 °C; the EA of WPI-COS was 1.87 at 25.3 % SR, 20.0 h, 46.1 °C; the ES of WPI-COS was 13.28 min at 32.5 % SR, 12.0 h, 35.0 °C and setting temperature was the major factor affecting EA and ES while SR was the major factor affecting solubility and heat stability. Conditions were optimized for the preparation of WPI-COS to obtain improved functional properties.

Effects of Maillard reaction conditions on the functional properties of WPI chitosan oligosaccharide conjugates

Effects of pH, temperature and enzyme-to-substrate ratio on the antigenicity of whey protein hydrolysates prepared by Alcalase

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Effect of heat treatment on the antigenicity of bovine α-lactalbumin and β-lactoglobulin in whey protein isolate

Influence of Maillard reaction conditions on the antigenicity of bovine α-lactalbumin using response surface methodology

Effects of Maillard reaction conditions on the functional properties of WPI chitosan oligosaccharide conjugates

Effects of pH, temperature and enzyme-to-substrate ratio on the antigenicity of whey protein hydrolysates prepared by Alcalase