Safety evaluation of the food enzyme endo‐1,4‐β‐xylanase from the non‐genetically modified Trichoderma citrinoviride strain TCLSC

TL;DR

This study evaluates the safety of a food enzyme produced by a non-genetically modified fungus and concludes it is safe for use in food manufacturing.

Contribution

The novel contribution is the safety evaluation of endo-1,4-β-xylanase from Trichoderma citrinoviride for food applications.

Findings

Genotoxicity tests showed no safety concerns for the food enzyme.

The enzyme's amino acid sequence does not match known allergens, but allergic reactions cannot be completely ruled out.

The estimated dietary exposure is well below the no observed adverse effect level, ensuring a high margin of safety.

Abstract

The food enzyme endo‐1,4‐β‐xylanase (4‐β‐D‐xylan xylanohydrolase; EC 3.2.1.8) is produced with the non‐genetically modified Trichoderma citrinoviride strain TCLSC by Advanced Enzyme Technologies Ltd. It was considered free from viable cells of the production organism. It is intended to be used in four food manufacturing processes. Since residual amounts of food enzyme–total organic solids (TOS) are removed in one process, dietary exposure was calculated for the remaining three food manufacturing processes and was estimated to be up to 0.754 mg TOS/kg body weight (bw) per day in European populations. Genotoxicity tests did not indicate a safety 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 of 856 mg TOS/kg bw per day, the highest dose tested, which when compared with the estimated dietary exposure, resulted in a margin of exposure of at least 1135. A search for the homology of the amino acid sequence of the endo‐1,4‐β‐xylanase to known allergens was made and no match was found. The Panel considered that a risk of allergic reactions upon dietary exposure to the food enzyme cannot be excluded, but that the likelihood is 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.

Tables

TABLE 1. Composition of the food enzyme.

Parameters	Unit	Batches
		1	2 a	3 b
Endo‐1,4‐β‐xylanase activity	XU/g c	205,195	205,180	205,235
Protein	%	67.6	66.7	65.2
Ash	%	6.6	7.5	8.5
Water	%	6.6	6.2	6.1
Total organic solids (TOS) d	%	86.8	86.3	85.4
Activity/TOS ratio	XU/mg TOS	236.4	237.8	240.3

TABLE 2. Intended uses and recommended use levels of the food enzyme as provided by the applicant. 29

Food manufacturing process a	Raw material (RM)	Maximum recommended use level (mg TOS/kg RM) b
Processing of cereals and other grains
Production of baked products	Flour	6.38
Production of brewed products	Cereals	85
Production of distilled alcohol	Cereals	17
Processing of fruits and vegetables
Production of juices	Fruits and vegetables 30	17

TABLE 3. Summary of the estimated dietary exposure to food enzyme–TOS in six population groups.

Population group	Estimated exposure (mg TOS/kg body weight per day)
	Infants	Toddlers	Children	Adolescents	Adults	The elderly
Age range	3–11 months	12–35 months	3–9 years	10–17 years	18–64 years	≥ 65 years
Min–max mean (number of surveys)	0.006–0.122 (12)	0.042–0.444 (15)	0.025–0.232 (19)	0.026–0.150 (21)	0.028–0.119 (22)	0.014–0.088 (23)
Min–max 95th percentile (number of surveys)	0.023–0.448 (11)	0.193–0.731 (14)	0.045–0.754 (19)	0.056–0.483 (20)	0.117–0.433 (22)	0.051–0.299 (22)

TABLE 4. Qualitative evaluation of the influence of uncertainties on the dietary exposure estimate.

Sources of uncertainties	Direction of impact
Model input data
Consumption data: different methodologies/representativeness/underreporting/misreporting/no portion size standard	+/−
Use of data from food consumption surveys of a few days to estimate long‐term (chronic) exposure for high percentiles (95th percentile)	+
Possible national differences in categorisation and classification of food	+/−
Model assumptions and factors
Exposure to food enzyme–TOS always calculated based on the recommended maximum use level	+
Selection of broad FoodEx categories for the exposure assessment	+
Use of recipe fractions to disaggregate FoodEx categories	+/−
Use of technical factors in the exposure model	+/−
Exclusion of one process from the exposure assessment: ‐ Production of distilled alcohol	−

Full text

INTRODUCTION

1

Article 3 of the Regulation (EC) No 1332/20081 provides definition for ‘food enzyme’ and ‘food enzyme preparation’.

‘Food enzyme’ means a product obtained from plants, animals or microorganisms or products thereof including a product obtained by a fermentation process using microorganisms: (i) containing one or more enzymes capable of catalysing a specific biochemical reaction; and (ii) added to food for a technological purpose at any stage of the manufacturing, processing, preparation, treatment, packaging, transport or storage of foods.

‘Food enzyme preparation’ means a formulation consisting of one or more food enzymes in which substances such as food additives and/or other food ingredients are incorporated to facilitate their storage, sale, standardisation, dilution or dissolution.

Before January 2009, food enzymes other than those used as food additives were not regulated or were regulated as processing aids under the legislation of the Member States. On 20 January 2009, Regulation (EC) No 1332/2008 on food enzymes came into force. This Regulation applies to enzymes that are added to food to perform a technological function in the manufacture, processing, preparation, treatment, packaging, transport or storage of such food, including enzymes used as processing aids. Regulation (EC) No 1331/20082 established the European Union (EU) procedures for the safety assessment and the authorisation procedure of food additives, food enzymes and food flavourings. The use of a food enzyme shall be authorised only if it is demonstrated that:

• it does not pose a safety concern to the health of the consumer at the level of use proposed;
• there is a reasonable technological need;
• its use does not mislead the consumer.

All food enzymes currently on the EU market and intended to remain on that market, as well as all new food enzymes, shall be subjected to a safety evaluation by the European Food Safety Authority (EFSA) and approval via an EU Community list.

An application has been introduced by the company Advanced Enzyme Technologies Ltd. for the authorisation of a food enzyme Xylanase from Trichoderma citrinoviride strain TCLSC.

Following the requirements of Article 12.1 of Regulation (EC) No 234/20113 implementing Regulation (EC) No 1331/2008, the Commission has verified that the application falls within the scope of the food enzyme Regulation and contains all the elements required under Chapter II of that Regulation.

Terms of Reference

1.1

The European Commission requests the European Food Safety Authority to carry out the safety assessment on the food enzyme Xylanase from Trichoderma citrinoviride strain TCLSC in accordance with Article 17.3 of Regulation (EC) No 1332/2008 on food enzymes.

DATA AND METHODOLOGIES

2

Data

2.1

The applicant has submitted a dossier in support of the application for authorisation of the food enzyme endo‐1,4‐β‐xylanase from Trichoderma citrinoviride TCLSC (DSM 27790).

Additional information was requested from the applicant during the assessment phase on 16 January 2024 and on 12 September 2025 and was received on 1 April 2024 and on 19 November 2025, respectively (see Documentation provided to EFSA).

Methodologies

2.2

The assessment was conducted in line with the principles described in the EFSA ‘Guidance on transparency in the scientific aspects of risk assessment’ (EFSA, 2009) and following the relevant guidance documents of the EFSA Scientific Committee.

The ‘Guidance on the submission of a dossier on food enzymes for safety evaluation’ (EFSA CEF Panel, 2009) has been followed for the evaluation of the application. Additional information was requested in accordance with the updated ‘Scientific Guidance for the submission of dossiers on food enzymes’ (EFSA CEP Panel, 2021) and the guidance on the ‘Food manufacturing processes and technical data used in the exposure assessment of food enzymes’ (EFSA CEP Panel, 2023).

ASSESSMENT

3

IUBMB nomenclatureEndo‐1,4‐β‐xylanaseSystematic name4‐β‐D‐xylan xylanohydrolaseSynonymsXylanase; endo‐(1,4)‐D‐β‐xylanaseIUBMB NoEC 3.2.1.8CAS No9025‐57‐4EINECS No232‐800‐2

Endo‐1,4‐β xylanases catalyse the random hydrolysis of 1,4‐β‐D‐xylosidic linkages in xylans (including arabinoxylans), resulting in the generation of (1,4)‐β‐D‐xylan oligosaccharides of different lengths. The food enzyme under assessment is intended to be used in four food manufacturing processes as defined in the EFSA guidance (EFSA CEP Panel, 2023): processing of cereals and other grains for the production of (1) baked products, (2) brewed products and (3) distilled alcohol; (4) processing of fruits and vegetables for the production of juices.

Source of the food enzyme

3.1

The endo‐1,4‐β xylanase is produced with the non‐genetically modified filamentous fungus Trichoderma citrinoviride strain TCLSC which is deposited at the German Collection of Microorganisms and Cell Cultures (DSMZ, Germany) with deposition number ■■■■■. The production strain was identified as T. citrinoviride by phylogenetic analysis of the RNA polymerase II subunit (RPB2) encoding gene and the ITS sequences.4

Production of the food enzyme

3.2

The food enzyme is manufactured according to the Food Hygiene Regulation (EC) No 852/2004,5 with food safety procedures based on Hazard Analysis and Critical Control Points, and in accordance with Good Manufacturing Practice.6

The production strain is grown as a pure culture using a typical industrial medium in a ■■■■■ fermentation system with conventional process controls in place. After completion of the fermentation, the solid biomass is removed by filtration. The filtrate containing the enzyme is then further purified and concentrated, including an ultrafiltration step in which enzyme protein is retained, while most of the low molecular mass material passes the filtration membrane and is discarded.7 The applicant provided information on the identity of the substances used to control the fermentation and in the subsequent downstream processing of the food enzyme.

The Panel considered that sufficient information has been provided on the manufacturing process and the quality assurance system implemented by the applicant to exclude issues of concern.

Characteristics of the food enzyme

3.3

Properties of the food enzyme

3.3.1

The endo‐1,4‐β‐xylanase is a single polypeptide chain of 204 amino acids.8 The molecular mass of the mature protein, calculated from the amino acid sequence, is 22.2 kDa.9 The food enzyme was analysed by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis.10 A consistent protein pattern was observed across all batches.11 The gels showed a major protein band corresponding to an apparent molecular mass of about 21 kDa, consistent with the expected mass of the enzyme. The food enzyme contains β‐glucanase and cellulase activities. No other enzyme activities were reported.

The applicant's in‐house determination of endo‐1,4‐β‐xylanase activity is based on the hydrolysis of birch xylan (reaction conditions: pH 5.3, 50°C, 5 min). The release of reducing carbohydrates is measured by a colorimetric reaction detected at 540 nm. The enzyme activity is expressed in Xylanase Units (XU). One XU is defined as the amount of enzyme that releases 1 μmol reducing sugar equivalents (calculated as xylose) per minute under the assay conditions.12

The food enzyme has a temperature optimum around 65°C (at pH 5.3) and a pH optimum around 5.5 (40°C). Thermostability was tested by pre‐incubation of the food enzyme for 2 h at different temperatures (pH 5.3). The enzyme activity decreased above 40°C and around 8% residual activity remained at 70°C.13

Chemical parameters

3.3.2

Data on the chemical parameters of the food enzyme were provided for three batches intended for commercialisation, among which two (batch 2 and 3) were used for the toxicological tests (Table 1).14 The mean total organic solids (TOS) was 86.2% and the mean enzyme activity/TOS ratio was 238.2 XU/mg TOS.

Purity

3.3.3

The lead content in all batches was below 1 mg/kg15 which complies with the specification for lead as laid down in the general specifications for enzymes used in food processing (FAO/WHO, 2006). In addition, arsenic, cadmium and mercury contents were below the limits of quantification (LoQ) of the employed methods.16 ^,^ 17

The food enzyme complies with the microbiological criteria for total coliforms, Escherichia coli and Salmonella, as laid down in the general specifications for enzymes used in food processing (FAO/WHO, 2006).18 No antimicrobial activity was detected in any of the tested batches.19

Strains of the Trichoderma species, in common with most filamentous fungi, have the capacity to produce a range of secondary metabolites (Frisvad et al., 2018). The presence of aflatoxins (B1, B2, G1, G2 and M1), ochratoxin A, fumonisin, zearalenone, deoxynivalenol, nivalenol, T‐2 toxin, HT‐2 toxin, ergocornine, ergocristine, ergocryptine, ergometrine, ergosine and ergotamine was examined in three food enzyme batches and was below the LoQ of the applied analytical methods.20 ^,^ 21 Adverse effects caused by the possible presence of other secondary metabolites are addressed by the toxicological examination of the food enzyme.

The Panel considered that the information provided on the purity of the food enzyme is sufficient.

Viable cells of the production strain

3.3.4

The absence of viable cells of the production strain in the food enzyme was demonstrated in three independent batches analysed in triplicate. Ten millilitres of a 1/10 suspension of product was incubated in 150 mL of non‐selective medium at 20°C for 24 h for resuscitation. From this, 10 × 1 mL were inoculated into agar medium containing chloramphenicol and the plates were incubated for 7 days at 30°C. No colonies of the production strain were produced. A positive control was included.22

Toxicological data

3.4

A battery of toxicological tests including a bacterial reverse mutation test (Ames test), an in vitro mammalian chromosomal aberration test and a repeated dose 90‐day oral toxicity study in rats has been provided.

Batches 2 and 3 (Table 1) used in these studies are batches intended for commercialisation and considered suitable as test items.

Genotoxicity

3.4.1

Bacterial reverse mutation test

3.4.1.1

A bacterial reverse mutation test (Ames test) was performed according to the Organisation for Economic Co‐operation and Development (OECD) Test Guideline 471 (OECD, 1997a) and following good laboratory practice (GLP).23

Five strains of Salmonella Typhimurium (TA98, TA100, TA102, TA1535 and TA1537) were used with or without metabolic activation (S9‐mix), applying the standard plate incorporation method. A preliminary and a main experiment were carried out in triplicate.

The preliminary experiment was carried out using three concentrations of the food enzyme ranging from 1071 to 4282 μg TOS/plate.

The main experiment was carried out using five concentrations of the food enzyme of 43, 135, 428, 1353 and 4282 μg TOS/plate.

No cytotoxicity was observed at any concentration of the test substance. Upon treatment with the food enzyme, there was no biologically relevant increase in the number of revertant colonies above the control values in any strain tested, with or without S9‐mix.

The study was considered reliable without restrictions and the results of high relevance.

The Panel concluded that the food enzyme endo‐1,4‐β‐xylanase did not induce gene mutations under the test conditions applied in this study.

In vitro mammalian chromosomal aberration test

3.4.1.2

The in vitro mammalian chromosomal aberration test was carried out according to OECD Test Guideline 473 (OECD, 1997b) and following GLP.24

Two separate experiments were performed with duplicate cultures of human peripheral whole blood lymphocytes. The cell cultures were treated with the food enzyme either with or without metabolic activation (S9‐mix).

Based on the results of a range‐finding test, in the first main experiment, cells were exposed to the food enzyme and scored for chromosomal aberrations at concentrations of 1078, 2157 and 4314 μg TOS/mL in a short‐term treatment (4‐h exposure and 24‐h recovery period) either with or without S9‐mix.

In the second main experiment, cells were exposed to the food enzyme and scored for chromosomal aberrations at concentrations of 1078, 2157 and 4314 μg TOS/mL in a short‐term treatment (4‐h exposure and 24‐h recovery period) with S9‐mix and in a long‐term treatment (24‐h exposure and 24‐h recovery period) without S9‐mix.

No cytotoxicity was seen either in the short‐term treatment (with or without S9‐mix) or in the long‐term treatment. The frequency of structural and numerical aberrations was not statistically significantly different from the negative controls at all concentrations tested.

The study was considered reliable without restrictions and the results of high relevance.

The Panel concluded that the food enzyme endo‐1,4‐β‐xylanase did not induce an increase in the frequency of structural and numerical aberrations under the test conditions applied in this study.

Repeated dose 90‐day oral toxicity study in rodents

3.4.2

The repeated dose 90‐day oral toxicity study was performed under GLP and according to OECD Test Guideline 408 (OECD, 1998)25 with the following deviations: weekly detailed clinical observations and functional observation battery tests were not performed. The Panel considered that these deviations are minor and do not impact the evaluation of the study.

Groups of 10 male and 10 female Wistar rats received the food enzyme by gavage in doses of 214, 428 and 856 mg TOS/kg bw per day. Controls received the vehicle (water).

Furthermore, a recovery control and a high‐dose group were included in the study, each comprising 10 males and 10 females and terminated 4 weeks after the end of treatment.

No mortality was observed.

The feed consumption was statistically significantly decreased in week 2 of administration in low‐dose males (−4%) and in week 13 in mid‐dose males (−2%), increased in week 11 in mid‐dose females (+2%), decreased in week 2 in high‐dose recovery females (−1%) and increased in week 4 in high‐dose recovery females (+2%). The Panel considered the change as not toxicologically relevant, as it was recorded at single time intervals, there was no consistency between the changes in males and females, there was no dose–response relationship (except in week 2 and 4 of recovery period), the changes were small and there were no statistically significant changes in the final body weight, the final body weight gain and the changes were within the historical control values.

Haematological investigations revealed a statistically significant decrease in granulocytes in high‐dose females (−13%). The Panel considered the change as not toxicologically relevant, as it was only observed in one sex, there were no changes in other relevant parameters (other white blood cell parameters), there were no histopathological changes and the change was within the historical control values.

Clinical chemistry investigations revealed a statistically significant decrease in alanine transaminase activity (ALT) in high‐dose males (−14%) and in high‐dose recovery males on day 91 of administration (−13%) and a decrease in urea in high‐dose females (−11%). The Panel considered the changes as not toxicologically relevant, as they were only observed in one sex (both parameters), the changes were small, there were no changes in other relevant parameters (other liver enzymes, creatinine), there were no histopathological changes in liver and kidneys and the changes were within the historical control values.

No other statistically significant or toxicologically relevant differences from controls were reported.

The Panel identified a no observed adverse effect level (NOAEL) of 856 mg TOS/kg bw per day, the highest dose tested.

Allergenicity

3.4.3

The allergenicity assessment considered only the food enzyme and not additives, carriers or other excipients that may be used in the final formulation.

The potential allergenicity of the endo‐1,4‐β‐xylanase produced with the Trichoderma citrinoviride strain TCLSC was assessed by comparing its amino acid sequence with those of known allergens as described in the EFSA GMO Scientific Opinion (EFSA GMO Panel, 2010). Using higher than 35% identity in a sliding window of 80 amino acids as the criterion, no match was found in the AllergenOnline database.26

No reports on oral and respiratory sensitisation or elicitation reactions of the endo‐1,4‐β‐xylanase under assessment have been published.27

Respiratory allergy, e.g. baker's asthma, following occupational exposure to xylanase has been described (Elms et al., 2003; Martel et al., 2010; Baur et al., 1998; Merget et al., 2001, Lipińska‐Ojrzanowska et al., 2016). Several studies have shown that individuals respiratorily sensitised to a food enzyme are usually able to ingest the corresponding enzyme without acquiring clinical symptoms of food allergy (Armentia et al., 2009; Cullinan et al., 1997; Poulsen, 2004). Adverse reactions upon dietary exposure to xylanases in individuals sensitised through the respiratory route have not been reported.

The Panel considered that the results of the sequence homology search and the available literature do not indicate a risk of allergic reactions upon dietary exposure to the endo‐1,4‐β‐xylanase under assessment.

■■■■■, products from ■■■■■ that may cause allergies or intolerances (listed in the Regulation (EU) No 1169/201128), are used as raw materials. In addition, ■■■■■, known sources of allergens, are present in the culture medium. During the fermentation process, these products will mostly be degraded and utilised by the production strain.

The Panel considered that residual amounts of allergenic proteins could be present in the food enzyme. Taking into account the level of dietary exposure (see Section 3.5), this would result in minute amounts in the final foods from which allergic reactions are usually not expected.

In conclusion, when used for the production of distilled alcohols, the Panel considered that a risk of allergic reactions upon dietary exposure can be excluded. For the remaining intended uses, the risk of allergic reactions upon dietary exposure to this food enzyme cannot be excluded, but the likelihood is low.

Dietary exposure

3.5

Intended use of the food enzyme

3.5.1

The food enzyme is intended to be used in four food manufacturing processes at the recommended use levels summarised in Table 2.

TABLE 2: Intended uses and recommended use levels of the food enzyme as provided by the applicant. 29

In the production of baked products, the food enzyme is added to flour during the preparation of the dough or batter31 to hydrolyse (arabino)xylans to reduce the stiffness of the dough. The food enzyme–TOS remain in the baked products.

In the production of brewed products, the food enzyme is added to cereals during the mashing32 to promote the release of starch and protein, increasing the brewing yield. It also reduces viscosity and turbidity, which aids beer filtration. The food enzyme–TOS remains in the brewed products.

In the production of distilled alcohol, the food enzyme is added to cereals during slurry mixing, liquefaction or fermentation33 to reduce viscosity and to increase yield.34 The food enzyme–TOS are not carried over into the distilled alcohols (EFSA CEP Panel, 2023).

In the production of fruit and vegetable35 juices, the food enzyme is added to fruit and vegetables during the maceration36 to degrade cell wall polymers and reduce juice cloudiness and turbidity. The food enzyme–TOS remains in the juices.

Based on data provided on the temperature profile and thermostability (see Section 3.3.1) and the downstream processing within the respective food manufacturing processes, the Panel considered that the food enzyme is inactivated during the production of brewed products. However, it may remain in its active form in the other food manufacturing processes listed in Table 2 in which the food enzyme–TOS remain, depending on the heat treatment conditions.

Dietary exposure estimation

3.5.2

In accordance with the guidance document (EFSA CEP Panel, 2021), dietary exposure was calculated for the three food manufacturing processes where the food enzyme–TOS remains in the final foods.

Chronic exposure to the food enzyme–TOS was calculated by combining the maximum recommended use level with individual consumption data (EFSA CEP Panel, 2021). The estimation involved selection of relevant food categories and application of technical conversion factors (EFSA CEP Panel, 2023).

Table 3 provides an overview of the derived exposure estimates across all surveys. Detailed mean and 95th percentile exposure to the food enzyme–TOS per age class, country and survey, as well as contribution from each FoodEx category to the total dietary exposure are reported in Appendix A – Tables 1 and 2. For the present assessment, food consumption data were available from 48 dietary surveys (covering infants, toddlers, children, adolescents, adults and the elderly), carried out in 26 European countries (Appendix B). The highest dietary exposure was estimated to be 0.754 mg TOS/kg bw per day in children at the 95th percentile.

Uncertainty analysis

3.5.3

In accordance with the guidance provided in the EFSA opinion related to uncertainties in dietary exposure assessment (EFSA, 2006), the following sources of uncertainties have been considered and are summarised in Table 4.

The conservative approach applied to estimate the dietary exposure to the food enzyme–TOS, in particular assumptions made on the occurrence and use levels of this specific food enzyme, is likely to have led to an overestimation of the exposure.

The exclusion of one food manufacturing process from the exposure estimation was based on > 99% of TOS removal. This is not expected to impact the overall estimate derived.

Margin of exposure

3.6

A comparison of the NOAEL (856 mg TOS/kg bw per day) identified from the 90‐day rat study with the derived exposure estimates of 0.006–0.444 mg TOS/kg bw per day at the mean and from 0.023 to 0.754 mg TOS/kg bw per day at the 95th percentile resulted in a margin of exposure of at least 1135.

CONCLUSION

4

Based on the data provided and the derived margin of exposure, the Panel concluded that the food enzyme endo‐1,4‐β‐xylanase produced with the non‐genetically modified Trichoderma citrinoviride strain TCLSC does not give rise to safety concerns under the intended conditions of use.

REMARK

5

The use of this endo‐1,4‐β‐xylanase from the non‐genetically modified Trichoderma citrinoviride strain TCLSC is not considered to raise safety concerns when used in the production of fruit and vegetable juices. However, the Panel noted that, according to Directive 2012/12/EU, the use of endo‐1,4‐β‐xylanase is not permitted in the treatment of fruits for juice production.

DOCUMENTATION AS PROVIDED TO EFSA

6

Food enzyme name: endo‐1,4‐β‐xylanase. February 2014. Submitted by Advanced Enzyme Technologies Ltd. The dossier was updated on 7 July 2014.

Additional information. April 2024. Submitted by Advanced Enzyme Technologies Ltd.

Additional information November 2025. Submitted by Advanced Enzyme Technologies Ltd.

ABBREVIATIONSbwbody weightCASChemical Abstracts ServiceCEFEFSA Panel on Food Contact Materials, Enzymes, Flavourings and Processing AidsCEPEFSA Panel on Food Contact Materials, Enzymes and Processing AidsEINECSEuropean Inventory of Existing Commercial Chemical SubstancesFAOFood and Agricultural Organization of the United NationsGLPGood Laboratory PracticeGMOgenetically modified organismIUBMBInternational Union of Biochemistry and Molecular BiologyJECFAJoint FAO/WHO Expert Committee on Food AdditiveskDakilodaltonLOQlimit of quantificationMNBNbi‐nucleated cells with micronucleiMOEmargin of exposureOECDOrganisation for Economic Cooperation and DevelopmentSDS‐PAGEsodium dodecyl sulfate‐polyacrylamide gel electrophoresisTOStotal organic solidsWHOWorld Health Organization

REQUESTOR

European Commission

QUESTION NUMBER

EFSA‐Q‐2014‐00543

COPYRIGHT FOR NON‐EFSA CONTENT

EFSA may include images or other content for which it does not hold copyright. In such cases, EFSA indicates the copyright holder and users should seek permission to reproduce the content from the original source.

PANEL MEMBERS

José Manuel Barat Baviera, Claudia Bolognesi, Francesco Catania, Gabriele Gadermaier, Ralf Greiner, Baltasar Mayo, Alicja Mortensen, Yrjö Henrik Roos, Marize de Lourdes Marzo Solano, Henk Van Loveren, Laurence Vernis and Holger Zorn.

NOTE

The full opinion will be published in accordance with Article 12 of Regulation (EC) No 1331/2008 once the decision on confidentiality will be received from the European Commission.

Supporting information

APPENDIX A: Dietary exposure estimates to the food enzyme–TOS in details