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Evaluation of the potential allergenicity of the enzyme microbial transglutaminase using the 2001 FAO/WHO Decision Tree
Author(s) -
Pedersen Mona H.,
Hansen Tine K.,
Sten Eva,
Seguro Katsuya,
Ohtsuka Tomoko,
Morita Akiko,
BindslevJensen Carsten,
Poulsen Lars K.
Publication year - 2004
Publication title -
molecular nutrition and food research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.495
H-Index - 131
eISSN - 1613-4133
pISSN - 1613-4125
DOI - 10.1002/mnfr.200400014
Subject(s) - allergen , immunoglobulin e , pepsin , biochemistry , enzyme , allergy , chemistry , food allergy , amino acid , tissue transglutaminase , biology , food science , microbiology and biotechnology , antibody , immunology
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.