SCOPE: The growing world population requires the exploration of new sustainable protein sources to ensure food security. Insects such as mealworm are promising candidates. For safety reasons, a risk assessment, including allergy risks, is needed. Since allergenicity can be influenced by thermal processing, it is highly important to take this into account. METHODS AND RESULTS: Fresh mealworm was heat processed and extracted by a sequential extraction method using in succession Tris, urea, and a combined SDS/DTT buffer. Extracts were tested using immunoblot, basophil activation test and skin prick test in 15 shrimp allergic patients, previously indicated as population at risk for mealworm allergy. Immunoblots showed a difference in IgE binding between processed and unprocessed mealworm extracts. However, this was due to change in solubility. Some allergens were soluble in urea buffer, but became more soluble in Tris buffer and vice versa. IgE binding was seen for all extracts in blot and basophil activation test. The results from 13 skin prick tests showed a skin reaction similar between processed and unprocessed mealworm. CONCLUSION: Thermal processing did not lower allergenicity but clearly changed solubility of mealworm allergens. A sequential extraction method allowed for assessment of a broader protein panel.
SCOPE: The growing world population requires the exploration of new sustainable protein sources to ensure food security. Insects such as mealworm are promising candidates. For safety reasons, a risk assessment, including allergy risks, is needed. Since allergenicity can be influenced by thermal processing, it is highly important to take this into account. METHODS AND RESULTS: Fresh mealworm was heat processed and extracted by a sequential extraction method using in succession Tris, urea, and a combined SDS/DTT buffer. Extracts were tested using immunoblot, basophil activation test and skin prick test in 15 shrimp allergicpatients, previously indicated as population at risk for mealworm allergy. Immunoblots showed a difference in IgE binding between processed and unprocessed mealworm extracts. However, this was due to change in solubility. Some allergens were soluble in urea buffer, but became more soluble in Tris buffer and vice versa. IgE binding was seen for all extracts in blot and basophil activation test. The results from 13 skin prick tests showed a skin reaction similar between processed and unprocessed mealworm. CONCLUSION: Thermal processing did not lower allergenicity but clearly changed solubility of mealworm allergens. A sequential extraction method allowed for assessment of a broader protein panel.
Authors: Dominique Turck; Jacqueline Castenmiller; Stefaan De Henauw; Karen Ildico Hirsch-Ernst; John Kearney; Alexandre Maciuk; Inge Mangelsdorf; Harry J McArdle; Androniki Naska; Carmen Pelaez; Kristina Pentieva; Alfonso Siani; Frank Thies; Sophia Tsabouri; Marco Vinceti; Francesco Cubadda; Thomas Frenzel; Marina Heinonen; Rosangela Marchelli; Monika Neuhäuser-Berthold; Morten Poulsen; Miguel Prieto Maradona; Josef Rudolf Schlatter; Henk van Loveren; Ermolaos Ververis; Helle Katrine Knutsen Journal: EFSA J Date: 2021-01-13