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Honey is a highly consumed natural product, not only for its taste and nutritional value, but also for its health benefits. Owing to characteristics that are essentially or exclusively related to the specific region or particular local environment and flora, honey can be classified as a premium product generally perceived as a high-quality and valued product because of its desirable flavor and taste. Consequently, honey has been a target of adulteration through inappropriate/fraudulent production practices and mislabeling origin. Globally, authentication of honey covers 2 main aspects: the production, with main issues related to sugar syrup addition, filtration, thermal treatment, and water content; and the labeled origin (geographical and/or botanical) and "organic" provenance. This review addresses all those issues, focusing on the approaches to detect the different types of honey adulteration. Due to the complex nature of honey and to the different types of adulteration, its authentication has been challenging and prompted the development of several advanced analytical approaches. Therefore, an updated, critical, and extensive overview on the current and advanced analytical methods targeting markers of adulteration/authenticity, including nontarget fingerprint approaches will be provided. The most recent advances on molecular, chromatographic, and spectroscopic methodologies will be described, emphasizing their pros and cons for the identification of botanical and geographical origins.

Cow milk allergy is one of the most common food allergies in early childhood and often persists through adult life, forcing an individual to a complete elimination diet. Milk proteins are present in uncounted food products, such as cheese, yogurt, or bakery item, exposing allergic persons to a constant threat. Many efforts have been made to overcome this global problem and to improve the life quality of allergic individuals. First, proper and reliable food labeling is fundamental for consumers, but the verification of its compliance is also needed, which should rely on accurate and sensitive analytical methods to detect milk allergens in processed foods. At the same time, strategies to reduce milk allergenicity, such as immunotherapy or the use of food processing techniques to modify allergen structure, have to be extensively studied. Recent research findings on the applicability of food processing, such as heat treatment, fermentation, or high pressure, have revealed great potential in reducing milk allergenicity. In this review, significant research advances on cow milk allergy are explored, focusing on prevalence, diagnosis, and therapy. Molecular characterization of cow milk allergens and cross-reactivity with other nonbovine milk species are described, as well as the effects of processing, food matrix, and digestibility on milk allergenicity. Additionally, analytical methods for the detection of milk allergens in food are described, from immunoassays and mass spectrometry methods for protein analysis to real-time polymerase chain reaction for DNA analysis.

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Species identification in meat products has grown in interest in recent years since these foodstuffs are susceptible targets for fraudulent labelling. In this work, a real-time PCR approach based on SYBR Green dye was proposed for the quantitative detection of pork meat in processed meat products. For the development of the method, binary meat mixtures containing known amounts of pork meat in poultry meat were used to obtain a normalised calibration model from 0.1 to 25% with high linear correlation and PCR efficiency. The method revealed high specificity by melting curve analysis, being successfully validated through its application to blind meat mixtures, which confirmed its adequacy for pork meat determination. The fully applicability of the method was further demonstrated in commercial meat products, allowing verification of labelling compliance and identification of meat species in processed foods.

Olive fruits at the green, cherry and black stages were used to investigate the structural and microstructural changes in tissues during ripening. Scanning electron microscopy (SEM) tissue fracture of green olives resulted in cell wall breakage of epicarp and mesocarp cells. Tissue fracture resulted in fewer broken cells in cherry than in green olives and even less in black olive tissues. Cell separation occurred in the middle lamella region in some of the cells of the cherry fruit and in most of the black olive cells. Solubilization and loss of pectic polysaccharides, mainly the arabinan moiety, and glucuronoxylans occurred in the green to cherry stages. The pulp cell wall constituent polysaccharides, pectic polysaccharides, cellulose, glucuronoxylans and xyloglucans, were degraded and/or solubilized at the cherry to black ripening stages. The resultant depolymerization of the pectic polymers, especially those of the middle lamella region, was consistent with the progressive cell separation at the different ripening stages by SEM. This showed that partial solubilization of pectic, hemicellulosic and cellulosic polysaccharides within the cell wall matrix weakened the cell wall structures, preventing the breaking of cells when the tissues were fractured.

Key determinants for the development of an allergic response to an otherwise 'harmless' food protein involve different factors like the predisposition of the individual, the timing, the dose, the route of exposure, the intrinsic properties of the allergen, the food matrix (e.g. lipids) and the allergen modification by food processing. Various physicochemical parameters can have an impact on the allergenicity of animal proteins. Following our previous review on how physicochemical parameters shape plant protein allergenicity, the same analysis was proceeded here for animal allergens.We found that each parameter can have variable effects, ranging on an axis from allergenicity enhancement to resolution, depending on its nature and the allergen. While glycosylation and phosphorylation are common, both are not universal traits of animal allergens. High molecular structures can favour allergenicity, but structural loss and uncovering hidden epitopes, can also have a similar impact. We discovered that there are important knowledge gaps in regard to physicochemical parameters shaping protein allergenicity both from animal and plant origin, mainly because the comparability of the data is poor. Future biomolecular studies of exhaustive, standardized design together with strong validation part in the clinical context, together with data integration model systems will be needed to unravel causal relationships between physicochemical properties and the basis of protein allergenicity.

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