Whey allergens: Influence of nonthermal processing treatments and their detection methods

Abstract

Whey and its components are recognized as value-added ingredients in infant formulas, beverages, sports nutritious foods, and other food products. Whey offers opportunities for the food industrial sector to develop functional foods with potential health benefits due to its unique physiological and functional attributes. Despite all the above importance, the consumption of whey protein (WP) can trigger hypersensitive reactions and is a constant threat for sensitive individuals. Although avoiding such food products is the most successful approach, there is still a chance of incorrect labeling and cross-contamination during food processing. As whey allergens in food products are cross-reactive, the phenomenon of homologous milk proteins of various species may escalate to a more serious problem. In this review, nonthermal processing technologies used to prevent and eliminate WP allergies are presented and discussed in detail.These processing technologies can either enhance or mitigate the impact of potential allergenicity. Therefore, the development of highly precise analytical technologies to detect and quantify the existence of whey allergens is of considerable importance. The present review is an attempt to cover all the updated approaches used for the detection of whey allergens in processed food products.Immunological and DNA-based assays are generally used for detecting allergenic proteins in processed food products. In addition, mass spectrometry is also employed as a preliminary technique for detection. We also highlighted the latest improvements in allergen detection toward biosensing strategies particularly immunosensors and aptasensors.

Linear Epitopes Play an Important Role in the Immunoglobulin G (IgG)/Immunoglobulin E (IgE)-Binding Capacity of Scy p 4

“…5 Besides, the immunoglobulin G (IgG)/ IgE-binding capacity of food allergens was reduced by highpressure, ultrasonic, and irradiation treatment as a result of the secondary structure being changed and non-covalent bonds being destroyed. 11 The structure and activity of allergen are closely related. 12 Chemical denaturants were used to study the conformation−activity relation of protein.…”

“…Previous studies have found that the enzyme cross-linking reaction and Maillard reaction could reduce the immunoreactivity of Scy p 4, which is due to Scy p 4 being modified to change its structure . Besides, the immunoglobulin G (IgG)/IgE-binding capacity of food allergens was reduced by high-pressure, ultrasonic, and irradiation treatment as a result of the secondary structure being changed and non-covalent bonds being destroyed . The structure and activity of allergen are closely related .…”

Purification, Expression, and Characterization of Sarcoplasmic Calcium Binding Protein: A Novel Allergen of Portunus trituberculatus

“…Heat and acid-alkali are important factors that induce structural variations of allergic proteins during food processing, like boiling, roasting, fermentation, and others. 34,35 The thermal and pH resistance of P. trituberculatus SCP were assessed with rSCP through immunologic approaches. The rSCP retained main bonds and strong immunoreactivity in normal conditions, yet partially degraded at extreme conditions (temperature >80 °C and pH 1−2).…”

“…Heat and acid-alkali are important factors that induce structural variations of allergic proteins during food processing, like boiling, roasting, fermentation, and others. , The thermal and pH resistance of P. trituberculatus SCP were assessed with rSCP through immunologic approaches.…”

CRISPR‐Cas‐based detection for food safety problems: Current status, challenges, and opportunities

“…Additionally, detection of allergens is also a possible application of the CRISPR‐Cas system. Currently, immunological and DNA‐based analyses are commonly used to detect allergenic proteins in foods (Khan et al., 2021). Mass spectrometry and aptamer‐based biosensors have also been used as preliminary techniques for detection.…”