**1. Introduction**

Edible insects have garnered increased interest for human consumption due to their high nutritional value and low environmental impact when compared to conventional livestock. Moreover, edible insects were targeted as a potential alternative protein resource to address the problem of a global food crisis. In Western countries, mealworm (*Tenebrio molitor*) is of particular interest, being evidenced in recent years by several publications related to protein quality and the improvement of techno-functional properties [1–3]. However, recent studies described an allergenic risk that was related to the consumption of edible insects due to potential cross-reactivity with other arthropods, especially crustaceans [4–6]. Tropomyosin, arginine-kinase, but also other insect proteins, such as larval cuticle protein, myosin light, and heavy chain, as well as troponin, are potentially involved in allergenic reactions in cross-reactivity with other allergenic species (shrimp, prawn, and crab) [5,7,8]. Consequently, particularly for consumers with a food allergy to crustaceans, it is necessary to consider the risk of an allergic reaction after consuming edible insects.

Different food processing methods, such as boiling [9,10], autoclaving [11], extrusion [12], microwave [13], pulsed-electric field [14], ultrasound [15], and HHP [16,17], may alter the intrinsic structure of food proteins and, consequently, decrease their allergenic properties. These processes may be coupled to enzymatic hydrolysis to further decrease the allergenicity of a wide range of conventional food proteins and generate protein hydrolysates that could potentially be integrated into specific formulations for food-allergic patients [18]. Similar strategies for reducing protein allergenicity were applied to edible insect products. Specifically, Alcalase® and pepsin were used to decrease the protein allergenicity of a wide range of food matrices, including edible insects. Indeed, Hall et al. [19] demonstrated that increasing the degree of hydrolysis (DH) of cricket proteins after proteolysis by Alcalase® positively impacted their bioactive potential while lowering the reactivity to tropomyosin. Van Broekhoven, Bastiaan-Net, de Jong, and Wichers [5] showed that mealworm protein allergenicity decreased significantly after heat processing and in vitro digestion by pepsin. Additionally, the application of microwave-assisted enzymatic hydrolysis by Alcalase® to cricket protein was an efficient method for generating hypoallergenic peptide fractions [20].

High hydrostatic pressure (HHP), a non-thermal technology that applies isostatic pressure from 100 to 1,000 MPa, induces the modification of secondary, tertiary, and quaternary structures of proteins, causing protein unfolding due to the rupture of noncovalent bonds (hydrogen, hydrophobic, and ionic bonds) [21]. The use of HHP combined with diverse enzymes to reduce protein allergenicity has been previously reviewed [18]. However, HHP-assisted enzymatic hydrolysis to modify allergenic protein digestion from edible insects has not yet been reported. Consequently, the aims of this preliminary work were 1) to apply HHP in combination with enzymatic hydrolysis by Alcalase® or pepsin to generate protein hydrolysates from mealworm meal and 2) to evaluate different pressurization strategies (applied as a pretreatment before enzymatic hydrolysis or simultaneously with enzymatic hydrolysis) to potentially improve the in vitro digestion of mealworm allergenic proteins.
