Evaluation of the potential allergenicity of the enzyme microbial transglutaminase using the 2001 FAO/WHO Decision Tree
| Autor: | Tine K Hansen, Katsuya Seguro, Tomoko Ohtsuka, Akiko Morita, Mona H. Pedersen, Lars K. Poulsen, Eva Sten, Carsten Bindslev-Jensen |
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| Jazyk: | angličtina |
| Rok vydání: | 2004 |
| Předmět: |
Tissue transglutaminase
Cross Reactions Immunoglobulin E medicine.disease_cause Cross-reactivity Risk Assessment Allergen Pepsin otorhinolaryngologic diseases medicine Animals Humans Trypsin Peptide sequence chemistry.chemical_classification Transglutaminases biology Organisms Genetically Modified Sequence Homology Amino Acid Immune Sera Decision Trees Pepsin A Streptomyces respiratory tract diseases Amino acid Genetically modified organism Biochemistry chemistry Gadus morhua Consumer Product Safety biology.protein Food Hypersensitivity Food Science Biotechnology |
| Zdroj: | Pedersen, M H, Hansen, T K, Sten, E, Seguro, K, Ohtsuka, T, Morita, A, Bindslev-Jensen, C & Poulsen, L K 2004, ' Evaluation of the potential allergenicity of the enzyme microbial transglutaminase using the 2001 FAO/WHO Decision Tree ', Molecular Nutrition & Food Research, vol. 48, pp. 434-440 . University of Southern Denmark |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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