Evaluation of the potential allergenicity of the enzyme microbial transglutaminase using the 2001 FAO/WHO Decision Tree

• Published in: Molecular Nutrition & Food Research
• Main Authors: Pedersen, Mona H, Hansen, Tine K, Sten, Eva, Seguro, Katsuya, Ohtsuka, Tomoko, Morita, Akiko, Bindslev-Jensen, Carsten, Poulsen, Lars K.
• Format: Article in Journal/Newspaper
• Language: English
• Published: 2004
• Subjects: Animals; Consumer Product Safety; Cross Reactions; Decision Trees; Food Hypersensitivity; Gadus morhua; Humans; Immune Sera; Immunoglobulin E; Organisms; Genetically Modified; Pepsin A; Risk Assessment; Sequence Homology; Amino Acid; Streptomyces; Transglutaminases; Trypsin
• Online Access: https://curis.ku.dk/portal/da/publications/evaluation-of-the-potential-allergenicity-of-the-enzyme-microbial-transglutaminase-using-the-2001-faowho-decision-tree(aab26814-c036-4a91-ac70-fb743cbbdf98).html; https://doi.org/10.1002/mnfr.200400014

All novel proteins must be assessed for their potential allergenicity before they are introduced into the food market. One method to achieve this is the 2001 FAO/WHO Decision Tree recommended for evaluation of proteins from genetically modified organisms (GMOs). It was the aim of this study to investigate the allergenicity of microbial transglutaminase (m-TG) from Streptoverticillium mobaraense. Amino acid sequence similarity to known allergens, pepsin resistance, and detection of protein binding to specific serum immunoglobulin E (IgE) (RAST) have been evaluated as recommended by the decision tree. Allergenicity in the source material was thought unlikely, since no IgE-mediated allergy to any bacteria has been reported. m-TG is fully degraded after 5 min of pepsin treatment. A database search showed that the enzyme has no homology with known allergens, down to a match of six contiguous amino acids, which meets the requirements of the decision tree. However, there is a match at the five contiguous amino acid level to the major codfish allergen Gad c1. The potential cross reactivity between m-TG and Gad c1 was investigated in RAST using sera from 25 documented cod-allergic patients and an extract of raw codfish. No binding between patient IgE and m-TG was observed. It can be concluded that no safety concerns with regard to the allergenic potential of m-TG were identified.