High Hydrostatic Pressure-Assisted Enzymatic Hydrolysis Affect Mealworm Allergenic Proteins

Abstract

Edible insects have garnered increased interest as alternative protein sources due to the world’s growing population. However, the allergenicity of specific insect proteins is a major concern for both industry and consumers. This preliminary study investigated the capacity of high hydrostatic pressure (HHP) coupled to enzymatic hydrolysis by Alcalase® or pepsin in order to improve the in vitro digestion of mealworm proteins, specifically allergenic proteins. Pressurization was applied as pretreatment before in vitro digestion or, simultaneously, during hydrolysis. The degree of hydrolysis was compared between the different treatments and a mass spectrometry-based proteomic method was used to determine the efficiency of allergenic protein hydrolysis. Only the Alcalase® hydrolysis under pressure improved the degree of hydrolysis of mealworm proteins. Moreover, the in vitro digestion of the main allergenic proteins was increased by pressurization conditions that were specifically coupled to pepsin hydrolysis. Consequently, HHP-assisted enzymatic hydrolysis represents an alternative strategy to conventional hydrolysis for generating a large amount of peptide originating from allergenic mealworm proteins, and for lowering their immunoreactivity, for food, nutraceutical, and pharmaceutical applications.

Effects of Hexane on Protein Profile, Solubility and Foaming Properties of Defatted Proteins Extracted from Tenebrio molitor Larvae

“…Proteins were probably unable to migrate in TMI fractions, since they were aggregated with other components of the cuticular matrix, such as chitin and lipids [ 45 , 46 ]. This phenomenon of protein aggregates was also observed by Boukil et al (2020) for non-processed T. molitor meal [ 32 ].…”

“…Both proteomic and 2D electrophoresis results were consistent with previously published work on the characterization of T. molitor proteins. These studies identified many pan-allergens, such as muscle proteins (actin, myosin, tropomyosin) [ 15 , 32 , 39 ], hemolymph proteins (hexamerin 1 and 2) [ 15 , 32 , 39 ], and proteins associated with various metabolic activities (arginine kinase, α-amylase) [ 39 , 40 , 41 ], to be the most abundant in T. molitor. Overall, the protein profiles were quite similar for the four fractions although specific differences in the abundance of major proteins were observed.…”

“…Proteins that contained similar peptides and could not be differentiated based on MS/MS analysis alone were grouped to satisfy the principles of parsimony. The total spectrum count value, which corresponds to the total number of spectra identified for a protein, was used to identify selected protein spots from the 2D gels, as this parameter was reported to be a semi-quantitative measure for a given protein abundance in proteomic studies [ 31 , 32 ].…”

Functionality of Cricket and Mealworm Hydrolysates Generated after Pretreatment of Meals with High Hydrostatic Pressures

“…For the high-pressure conditions, both insect dispersions were prepared as described for the control. Pressurization parameters (200 and 380 MPa for 1 min for cricket and mealworm meals, respectively) were based on results obtained by Boukil et al [ 42 ]. All hydrolysates were stored at 4 °C between experiments.…”

Recent Trends in Pretreatment of Food before Freeze-Drying

“…In this process, water is used as a pressure medium, with pressure in the range of 100-1000 MPa [105,106]. Food processing by HHP results in the inactivation of microorganisms [107] and modifies the enzyme activity [108]. Moreover, this process retains the food shape and does not require the use of chemical additives [106].…”