Ham JH, et al. Allergy Asthma Immunol Res. 2025 May;17(3):288-303. https://doi.org/10.4168/aair.2025.17.3.288

Food fraud and adulteration have been persistent issues affecting food supply chains throughout history. They intensify in parallel with the continuous growth in the global food market. Plant-based proteins, which are recognized as sustainable alternatives, face increased food fraud risks because of disparities in the cost of raw materials and complex processing methods. Despite these challenges, most efforts toward preventing food fraud and developing detection technologies have largely focused on animal-based products, with limited attention given to plant-based proteins. This comprehensive review systematically examines the characteristics of major plant protein sources and explores documented instances of food fraud (e.g., ingredient substitution, adulteration with lower-cost alternatives, and mislabeling) within this sector. Furthermore, we discuss key analytical techniques in detecting food fraud, including chromatography, DNA analysis, spectroscopy, and imaging-based approaches, examining their applications and effectiveness. A systematic literature review was conducted using structured search strategies across Scopus, Web of Science, and PubMed, covering publications from 2010 to 2025 and incorporating keywords related to plant-based proteins, food fraud, adulteration, and authentication, thereby ensuring methodological rigor and comprehensive coverage. This study provides a foundational framework to strengthen food fraud prevention strategies and uphold the integrity of the expanding plant-based protein market.

Precision fermentation (PF) yields single, well-characterized recombinant proteins, such as dairy and egg white proteins, at an industrial scale, and several products have reached the market. Numerous PF-derived proteins, including ovomucoid and β-lactoglobulin, are known allergens designed as exact structural copies of their native homologs; hence, assessments center on equivalence rather than novel hazards. Therefore, the current tiered scheme of allergen database comparison, digestibility testing, and serum immunoglobulin E binding assays is applicable. Nevertheless, residual host cell proteins, altered host-dependent enzymatic glycosylation, and process-related impurities render PF-derived products imperfect replicas, and thermal and high-pressure processing, enzymatic hydrolysis, and non-enzymatic glycation can modify linear or conformational epitopes, thereby reducing IgE binding or generating neoepitopes. Because these effects depend on structural attributes acquired during production, including folding stability, disulfide bonding, glycosylation, and proteolytic resistance, PF-derived proteins and native proteins may respond differently to identical processing. This review explores the molecular attributes acquired at each stage of PF production and the epitope changes originating during processing, reevaluates the current assessment scheme, and outlines considerations for a premarket safety framework reflecting realistic processing and consumption conditions.