Klaus‐Dieter Jany

Max Rubner Institut

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Vittorio Silano

European Food Safety Authority

Konrad Grob

Federal Office of Consumer Protection and Food Safety

Claudia Bolognesi

Federal Office of Consumer Protection and Food Safety

Holger Zorn

Federal Office of Consumer Protection and Food Safety

André Penninks

Agencia Española de Consumo, Seguridad Alimentaría y Nutrición

Andrew Chesson

Ministère de l'Économie et des Finances

Wim Mennes

National Institute for Public Health and the Environment

Boet Glandorf

National Institute for Public Health and the Environment

Trine Husøy

Norwegian Institute of Public Health

Maria Rosaria Milana

Federal Office of Consumer Protection and Food Safety

Cooperative Institutions

Federal Office of Consumer Protection and Food Safety

European Food Safety Authority

Ministry of Health Welfare and Sport

Ministère de l'Économie et des Finances

Agencia Española de Consumo, Seguridad Alimentaría y Nutrición

Food Standards Agency

Ministry of Health

Technical University of Munich

Federal Ministry of Social Affairs, Health, Care and Consumer Protection

Ministère de la Santé

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Pros and cons of genetic engineering

Hans-Jürgen Heinrich Walter P. Hammes Beatrix Tappeser Klaus‐Dieter Jany Claus Leitzmann

cons

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Citations (0)

Safety evaluation of the food enzyme aqualysin 1 from a genetically modified Bacillus subtilis (strain LMGS 25520)

EFSA Journal (2018)

Enzymes . Efsa Panel On Food Contact Materials Vittorio Silano Claudia Bolognesi Laurence Castle Kevin Chipman

The food enzyme considered in this opinion is aqualysin 1 (EC 3.4.21.111), produced from the genetically modified strain

Strain (injury)

10.2903/j.efsa.2018.5170

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Citations (2)

Safety evaluation of the food enzyme beta‐galactosidase from Bacillus sp. (strain M3‐1)

EFSA Journal (2019)

Vittorio Silano José Manuel Barat Baviera Claudia Bolognesi Pier Sandro Cocconcelli Riccardo Crebelli

The food enzyme b-D-galactosidase galactohydrolase (EC 3.2.1.23)is produced with Bacillus sp.strain M3-1 by GenoFocus Inc.The food enzyme b-galactosidase is intended to be used in the manufacture of galactooligosaccharides (GOS).Since residual amounts of total organic solids are removed by the purification steps applied during the production of GOS, toxicological studies were considered not necessary and no dietary exposure was calculated.Similarity of the amino acid sequence of the food enzyme to those of known allergens was searched and no match was found.The Panel considered that, under the intended conditions of use, the risk of allergic sensitisation and elicitation reactions by dietary exposure cannot be excluded, but the likelihood of such reactions to occur is considered to be low.Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns under the intended conditions of use.

Strain (injury)

10.2903/j.efsa.2019.5827

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Citations (2)

Safety evaluation of the food enzyme β‐amylase obtained from soybean (Glycine max)

EFSA Journal (2017)

Enzymes . Efsa Panel On Food Contact Materials Vittorio Silano Claudia Bolognesi Laurence Castle Jean Pierre J. P. Cravedi

The food enzyme considered in this opinion is a β-amylase (EC 3.2.1.2) from soybean submitted by Nagase (Europa) GmbH. This β-amylase is intended to be used in the starch processing for maltose syrup production and the manufacture of a Japanese rice cake type. Based on the maximum use levels recommended for the respective food processes, dietary exposure to the food enzyme-total organic solids (TOS) was estimated on the basis of Japanese consumption data. Conservative average infant formula consumption, as reported in the EFSA Draft Guidance on risk assessment of substances present in food intended for infants below 16 weeks of age, was used to estimate the exposure to a fraction of soybean comparable to the food enzyme-TOS, resulting from the consumption of soybean-derived foods. The exposure estimate to the food enzyme-TOS was found to be lower than the comparable fraction from the source material. Potential allergenicity of the β-amylase was evaluated by searching for similarity of the amino acid sequence to those of known allergens, and no match was found. The β-amylase is produced from soybean, which is a known allergenic food. Japanese rice cake, consequently, may contain traces of soybean allergens, which may give rise to safety concerns in soybean-allergic consumers. Based on the origin of the food enzyme from edible parts of soybean, the manufacturing process, the compositional and biochemical data provided and the dietary intake estimates, the Panel concluded that this food enzyme does not give rise to safety concerns under the intended conditions of use, except that Japanese rice cake produced with this food enzyme may contain traces of soybean allergens.

10.2903/j.efsa.2017.4757

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Purification and Characterization of a Phytase fromKlebsiella terrigena

Archives of Biochemistry and Biophysics (1997)

Ralf Greiner Edith Haller U. Konietzny Klaus‐Dieter Jany

Phytase

10.1006/abbi.1997.9942

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Citations (176)

Safety evaluation of the food enzyme alpha‐amylase from non‐genetically modified Aspergillus niger strain (strain DP‐Azb60)

EFSA Journal (2019)

Vittorio Silano José Manuel Barat Baviera Claudia Bolognesi Beat Johannes Brüschweiler Pier Sandro Cocconcelli

The food enzyme alpha-amylase (4-a-D-glucan glucanohydrolase; EC 3.2.1.1)is produced with a nongenetically modified Aspergillus niger (strain DP-Azb60) by Danisco US Inc.The food enzyme is free from viable cells of the production organism.The a-amylase is intended to be used in baking processes.Based on the maximum use levels, dietary exposure to the food enzyme-total organic solids (TOS) was estimated to be up to 0.503 mg TOS/kg body weight (bw) per day.Genotoxicity tests with the food enzyme did not indicate a genotoxic concern.The systemic toxicity was assessed by means of a repeated dose 90-day oral toxicity study in rats.The Panel identified a no-observed-adverse-effect level (NOAEL) at the highest dose of 1,000 mg TOS/kg bw per day that, compared with the estimated dietary exposure, results in a sufficiently high margin of exposure (of at least 1,988).Similarity of the amino acid sequence to those of known allergens was searched and one match was found to Asp o 21, an alpha-amylase from Aspergillus oryzae.The Panel considered that, under the intended conditions of use, the risk of allergic sensitisation and elicitation reactions upon dietary exposure to this food enzyme cannot be excluded, but the likelihood is considered low.Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns under the intended conditions of use.

Aspergillus niger

Aspergillus oryzae

Alpha-amylase

Strain (injury)

Animal Feed

No-observed-adverse-effect level

Food additive

10.2903/j.efsa.2019.5680

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Citations (2)

PURIFICATION AND CHARACTERIZATION OF HOMOGENEOUS ACID PHOSPHATASE FROM NONGERMINATED BUCKWHEAT (FAGOPYRUM ESCULENTUM) SEEDS

Journal of Food Biochemistry (2003)

Ralf Greiner Klaus‐Dieter Jany

A buckwheat acid phosphatase (orthophosphoric-monoester phosphohydrolase, EC 3.1.3.2) was purified about 250-fold from nongerminated buckwheat seeds to apparent homogeneity with a recovery of 4% from the acid phosphatase activity in the crude extract. It is the major acid phosphatase among eight different acid phosphatases identified in the crude extract. The purified enzyme behaved as a monomeric protein of molecular mass about 45 kDa. The purified enzyme exhibited a single pH optimum at 5.25. Optimum temperature for the degradation of p-nitrophenyl phosphate was 50C. The kinetic parameters for the hydrolysis of p-nitrophenyl phosphate were determined to be KM= 76 μmol L−1 and kcat= 924 s−1 at pH 5.25 and 37C. While the enzyme failed to act on phytate as a substrate, the enzyme exhibited a broad substrate selectivity. The purified enzyme showed no measureable carboxylesterase activity and no divalent metal ion requirement.

Fagopyrum

Enzyme Kinetics

10.1111/j.1745-4514.2003.tb00277.x

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Citations (9)

Application of Two-Dimensional Gel Electrophoresis To Interrogate Alterations in the Proteome of Genetically Modified Crops. 2. Assessing Natural Variability

Journal of Agricultural and Food Chemistry (2006)

Martin C. Ruebelt Markus Lipp Tracey L. Reynolds James D. Astwood Karl‐Heinz Engel

Proteomics is currently tested as a complementary tool for the safety assessment of genetically modified (GM) crops. Understanding the natural variability of the proteome is crucial for the interpretation of biological differences between transgenic and nontransgenic parental lines. The natural variation of seed protein profiles among a set of 12 Arabidopsis thaliana ecotypes was determined by utilizing two-dimensional electrophoresis (2DE). The total number of different resolved protein spots found among the 12 ecotypes was 931 with a range of 573 (Mt-0) to 653 (Condara) in any one ecotype. Although the ecotypes were grown side-by-side in an environmentally controlled growth chamber, almost half of the resolved spots varied with respect to their presence/absence, and 95% of the spots present in all ecotypes varied in spot quantity (2−53-fold). In the evaluation of unintended effects of genetic modification, it is concluded that the experimental design must account for existing natural variability, which, in the case of the expressed proteome, can be substantial. Keywords: Two-dimensional gel electrophoresis; Arabidopsis thaliana; seed proteome; natural variability

Proteome

10.1021/jf052357y

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Citations (63)

Identification and Properties of myo -Inositol Hexakisphosphate Phosphohydrolases (Phytases) from Barley (Hordeum vulgare)

Journal of Cereal Science (2000)

Ralf Greiner Klaus‐Dieter Jany Marie Alminger

Phytase

10.1006/jcrs.1999.0254

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Citations (91)

Evidence for an essential histidine residue in glucose dehydrogenase from Bacillus megaterium and sequence analysis of the peptides labeled with bromoacetyl pyridine

European Journal of Biochemistry (1983)

W. T. Ulmer Marion Fröschle Klaus‐Dieter Jany

Bromoacetylpyridine acts as an active‐site‐directed inhibitor on glucose dehydrogenase from Bacillus megaterium . The inactivation is irreversible with a K i of 7.7 mM. The coenzyme NAD but not the substrate glucose protects the enzyme from the inactivation. It is proposed that bromoacetylpyridine modifies a residue at or nearby the active site. The inactivation is correlated with the modification of a single histidine residue. Modification of the enzyme with 3‐(2‐bromo[ carbonyl ‐ 14 C]acetyl)‐pyridine and partial acid hydrolysis of the protein yielded one labeled fragment. From the arginine restricted tryptic cleavage of this fragment four radioactively labeled peptides were purified. Comparison of the specific radioactivity leads to the conclusion that the active site histidine residue must be located in the 58‐residue fragment AH2‐TA3. Sequence analysis showed that only one residue is modified in this fragment and the sequence around the labeled histidine residue is ‐Met‐Ser‐Ser‐Val‐His‐Glu‐Trp‐Lys‐Ile‐Pro‐Trp‐Pro‐. The minor labeled arginine fragments, comprising 86, 20 and 13 residues, were also sequenced. Only lysine residues are modified in these peptides. The modification of the individual residues does not exceed 10%.

Bacillus megaterium

Residue (chemistry)

Alanine

10.1111/j.1432-1033.1983.tb07724.x

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Citations (6)