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

TY - JOUR

T1 - Evaluation of the potential allergenicity of the enzyme microbial transglutaminase using the 2001 FAO/WHO Decision Tree

AU - Pedersen, Mona H

AU - Hansen, Tine K

AU - Sten, Eva

AU - Seguro, Katsuya

AU - Ohtsuka, Tomoko

AU - Morita, Akiko

AU - Bindslev-Jensen, Carsten

AU - Poulsen, Lars K.

PY - 2004/11

Y1 - 2004/11

N2 - 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.

AB - 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.

KW - Animals

KW - Consumer Product Safety

KW - Cross Reactions

KW - Decision Trees

KW - Food Hypersensitivity

KW - Gadus morhua

KW - Humans

KW - Immune Sera

KW - Immunoglobulin E

KW - Organisms, Genetically Modified

KW - Pepsin A

KW - Risk Assessment

KW - Sequence Homology, Amino Acid

KW - Streptomyces

KW - Transglutaminases

KW - Trypsin

U2 - 10.1002/mnfr.200400014

DO - 10.1002/mnfr.200400014

M3 - Journal article

C2 - 15508178

SN - 1613-4125

VL - 48

SP - 434

EP - 440

JO - Molecular Nutrition & Food Research

JF - Molecular Nutrition & Food Research

IS - 6

ER -