Safety evaluation of the food enzyme cellulase from the non‐genetically modified Aspergillus niger strain HBI‐AC01

TL;DR

This study evaluates the safety of a food enzyme derived from a non-GMO fungus and concludes it is safe for use in food manufacturing.

Contribution

The novel contribution is the safety assessment of a specific cellulase enzyme from a non-genetically modified Aspergillus niger strain.

Findings

Genotoxicity tests showed no safety concerns for the food enzyme.

The no observed adverse effect level was 349 mg TOS/kg body weight per day.

Allergen homology search found no matches, but a low likelihood of allergic reactions was noted.

Abstract

The food enzyme cellulase (4‐(1,3;1,4)‐β‐d‐glucan 4‐glucanohydrolase; EC 3.2.1.4) is produced with the non‐genetically modified microorganism Aspergillus niger strain HBI‐AC01 by HBI Enzymes Inc. The food enzyme was considered free from viable cells of the production strain. It is intended to be used in three 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 two food manufacturing processes. It was estimated to be up to 0.475 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 349 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 735. A search for the homology of the amino acid sequence of the cellulase to known allergens was made and no match was found. The Panel considered that a risk of allergic reactions upon dietary exposure 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 preparation.

Parameters	Unit	Batches
		1	2	3s	4 a
Cellulase activity	U/g b	4000	4370	4080	5180
Protein	%	22.1	24.2	22.6	26.7
Ash	%	0.1	0.8	0.6	0.3
Water	%	4.0	3.0	3.6	6.0
Diluent (■■■■■)	%	66.3	63.2	65.6	58.8
Total organic solids (TOS) c	%	29.6	33.0	30.2	34.9
Activity/TOS ratio	U/mg TOS	13.5	13.2	13.5	14.8

TABLE 2. Intended uses and recommended use levels of the food enzyme as provided by the applicant. 30

Food manufacturing process a	Raw material (RM)	Recommended use level (mg TOS/kg RM) b
Processing of cereals and other grains
Production of baked products	Flour	7.42–45
Production of brewed products	Cereals	7.42–74.2
Production of distilled alcohol	Cereals	102–392

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)	0–0.104 (12)	0.005–0.250 (15)	0.003–0.229 (19)	0.001–0.134 (21)	0.050–0.160 (22)	0.050–0.103 (23)
Min–max 95th percentile (number of surveys)	0–0.300 (11)	0.025–0.427 (14)	0.013–0.462 (19)	0.005–0.264 (20)	0.135–0.475 (22)	0.111–0.234 (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
Selection of broad FoodEx categories for the exposure assessment	+
Exposure to food enzyme–TOS always calculated based on the recommended maximum use level	+
Use of recipe fractions to disaggregate FoodEx categories	+/−
Use of technical factors in the exposure model	+/−
Exclusion of one process from the exposure estimation: – 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 micro‐organisms or products thereof including a product obtained by a fermentation process using micro‐organisms: (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 1331/20082established 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.

Background and Terms of Reference as provided by the requestor

1.1

Background as provided by the European Commission

1.1.1

Only food enzymes included in the Union list may be placed on the market as such and used in foods, in accordance with the specifications and conditions of use provided for in Article 7(2) of Regulation (EC) No 1332/2008^1^ on food enzymes

Four applications have been introduced by the companies “Puratos NV sa.”, “Novozymes A/S.”, “Meito Sangyo Co., Ltd” and the Association of Manufacturers and Formulators of Enzyme Products (AMFEP) for the authorisation of the food enzymes Inulinase from a genetically modified strain of Aspergillus Oryzae (strain MUCL 44346), Trypsin from porcine pancreatic glands, Triacylglycerol lipase from Candida cylindracea, and Cellulase, Glucanase and Hemicellulase covering Xylanase and Mannanase from Aspergillus niger respectively.

Following the requirements of Article 12.1 of Regulation (EC) No 234/2011 implementing Regulation (EC) No 1331/20082, the Commission has verified that the four applications fall within the scope of the food enzyme Regulation and contains all the elements required under Chapter II of that Regulation.

Terms of Reference

1.1.2

The European Commission requests the European Food Safety Authority to carry out the safety assessments on the food enzymes Inulinase from a genetically modified strain of Aspergillus Oryzae (strain MUCL 44346), Trypsin from porcine pancreatic glands, Triacylglycerol lipase from Candida cylindracea, and Cellulase, Glucanase and Hemicellulase covering Xylanase and Mannanase from Aspergillus niger in accordance with Article 17.3 of Regulation (EC) No 1332/2008 on food enzymes.

Interpretation of the Terms of Reference

1.2

The present scientific opinion addresses the European Commission's request to carry out the safety assessment of food enzyme cellulase, glucanase and hemicellulase covering xylanase and mannanase from Aspergillus niger submitted by Association of Manufacturers and Formulators of Enzyme Products (AMFEP).

The application was submitted initially as a joint dossier2 and identified as EFSA‐Q‐2015‐00340/EFSA‐Q‐2018‐01034/EFSA‐Q‐2018‐01035. Agreement to split the joint dossiers into individual data packages was made between EFSA, the European Commission and AMFEP.3

The current opinion addresses one data package originating from the joint dossier. This data package, identified as EFSA‐Q‐2022‐00518, concerns the food enzyme cellulase produced with the Aspergillus niger strain HBI‐AC01 and submitted by HBI Enzymes Inc.

DATA AND METHODOLOGIES

2

Data

2.1

The applicant submitted a dossier in support of the application for authorisation of the food enzyme cellulase from a non‐genetically modified Aspergilus niger (strain HBI‐AC01).

Additional information, requested from the applicant during the assessment phase on 18 September 2023 and 23 September 2025, and were received on 24 January 2024 and 26 September 2025 (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, 2009a) 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, 2009b) as well as the ‘Statement on characterisation of microorganisms used for the production of food enzymes’ (EFSA CEP Panel, 2019) have 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 nomenclatureCellulaseSystematic name4‐(1,3;1,4)‐β‐d‐glucan 4‐glucanohydrolaseSynonymsβ‐1,4‐glucanaseIUBMB No3.2.1.4CAS No9012‐54‐8EINECS No232‐734‐4

Cellulases catalyse the hydrolysis of 1,4‐β‐glycosidic linkages in cellulose and other β‐glucans, resulting in the generation of shorter β‐d‐glucan chains. The food enzyme under assessment is intended to be used in three 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.

Source of the food enzyme

3.1

The cellulase is produced with the non‐genetically modified filamentous fungus Aspergillus niger strain HBI‐AC01, which is deposited at the National Institute of Technology and Evaluation (NITE) Biological Resource Center (Japan), with the deposition number ■■■■■.4 The production strain was identified as A. niger by ■■■■■.5 A. niger HBI‐AC01 was obtained by ■■■■■.6

Production of the food enzyme

3.2

The food enzyme is manufactured according to the Food Hygiene Regulation (EC) No 852/2004,7 with food safety procedures based on Hazard Analysis and Critical Control Points, and in accordance with Good Manufacturing Practice.8

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 from the fermentation broth 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.9 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.10

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 cellulase is a single polypeptide chain of ■■■■■ amino acids.11 The molecular mass of the mature protein, calculated from the amino acid sequence, is ■■■■■ kDa.12 The food enzyme was analysed by sodium dodecyl sulfate–polyacrylamide gel electrophoresis.13 A consistent protein pattern was observed across all batches. The gel showed a major protein band of about ■■■■■ kDa, consistent with the expected molecular mass of the enzyme.

No other enzyme activities were reported.14

The applicant's in‐house determination of cellulase activity is based on the hydrolysis of carboxymethyl cellulose (reaction conditions: ■■■■■) and determined measuring the release of reducing sugars colorimetrically. The enzyme activity is quantified relative to an internal standard and expressed in units (U)/g. One U is defined as the quantity of enzyme required to release reducing sugars equivalent to 1 μmol of glucose per minute under the conditions of the assay.15

The food enzyme has a temperature optimum around 50°C (■■■■■) and a pH optimum around pH 4.5 (■■■■■). Thermostability was tested by pre‐incubation of the food enzyme for 10 min at different temperatures (■■■■■). Enzyme activity decreased above 45°C showing no residual activity at 75°C.16

Chemical parameters

3.3.2

Data on the chemical parameters of the food enzyme were provided for three batches used for commercialisation and one batch produced for the toxicological tests (Table 1).17 The mean total organic solids (TOS) of the three food enzyme batches for commercialisation was 30.9% and the mean enzyme activity/TOS ratio was 13.4 U/mg TOS.

Purity

3.3.3

The lead content in the three commercial batches and in the batch used for toxicological studies was below 5 mg/kg,18 ^,^ 19 which complies with the specification for lead as laid down in the general specifications for enzymes used in food processing (FAO/WHO, 2006).

The food enzyme preparation 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).20 No antimicrobial activity was detected in any of the tested batches.21

Strains of Aspergillus species, in common with most filamentous fungi, have the capacity to produce a range of secondary metabolites (Frisvad et al., 2018). The presence of fumonisins and ochratoxin A was examined in three food enzyme batches and was below the limit of quantification (LoQ) of the applied methods.22 ^,^ 23 Adverse effects caused by the potential presence of other secondary metabolites is 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. ■■■■■. No colonies were produced. A positive control was included.24

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.

The batch 4 (Table 1) used in these studies has a similar activity/TOS ratio as the batches used for commercialisation, and is considered suitable as a test item.

Genotoxicity

3.4.1

Bacterial reverse mutation test

3.4.1.1

A bacterial reverse mutation test (Ames test) was performed according to Japanese guideline (No. 1604, JMHV, 1999a) and following Japanese Good Laboratory Practice (GLP).25 The study is in accordance with OECD Test Guideline 471 (OECD, 1997). Four strains of Salmonella Typhimurium (TA98, TA100, TA1535 and TA1537) and Escherichia coli WP2uvrA were used with or without metabolic activation (S9‐mix), applying the pre‐incubation method.

The experiment was carried out in duplicate, using five concentrations of the food enzyme of 109, 218, 436, 873, 1745 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 with restrictions because the experiment was carried out in duplicate. The results were considered of limited relevance, but acceptable.

The Panel concluded that the food enzyme cellulase 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 Japanese guideline (No. 1604, JMHV, 1999a) and following Japanese GLP.26 An experiment was performed with duplicate cultures of a Chinese hamster lung fibroblast (CHL/IU) cell line. The cell cultures were treated with the food enzyme either with or without metabolic activation (S9‐mix).

Based on the results of the growth inhibition test, cells were exposed to the food enzyme and scored for chromosomal aberrations at concentrations of 436, 873, 1745 μg TOS/mL in a short‐term treatment (6‐h exposure and 18‐h recovery period) either with or without S9‐mix and in a long‐term treatment (24‐h exposure without recovery period) without S9‐mix.

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

The study was considered reliable without restrictions and the results were considered of high relevance. The Panel concluded that the food enzyme cellulase 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 in accordance with Japanese guideline (No. 655, JMHV, 1999b) and following Japanese GLP.27 The study is in accordance with OECD Test Guideline 408 (OECD, 1998) with the following deviations: weight of epididymides was not recorded, the level of spinal cord for histopathological examination was not indicated, the determination of urea and functional observational battery tests were not performed. The Panel considered that these deviations are minor and do not impact on the evaluation of the study.

Groups of 10 male and 10 female Sprague–Dawley (Crl:CD(SD)) rats received the food enzyme by gavage in doses of 87, 175 or 349 mg TOS/kg bw per day. Controls received the vehicle (water for injection).

No mortality was observed.

The feed consumption was statistically significantly increased on day 79 of administration in high‐dose males (+15%). The Panel considered the change as not toxicologically relevant, as it was only recorded at single time interval, it was only observed in one sex, there was no statistically significant change in the final feed consumption, the body weight or the body weight gain.

Haematological investigation revealed a statistically significant increase in haemoglobin concentration (+4%) and in haematocrit (+4%) in high‐dose females. The Panel considered the changes as not toxicologically relevant, as they were only observed in one sex, the changes were small, there were no changes in other red blood cell parameters and there were no histopathological changes in bone marrow.

Clinical chemistry investigation revealed a statistically significant increase in alpha‐2 globulin (+6%) and a decrease in total bilirubin (−9%) in mid‐dose males. The Panel considered the changes as not toxicologically relevant, as they were only observed in one sex, there was no dose–response relationship and there were no histopathological changes in liver.

Statistically significant changes detected in organ weights were an increase in relative liver weight in low‐dose males (+6%) and an increase in absolute (+5%) and relative (+8%) brain weight in mid‐dose males. The Panel considered the changes as not toxicologically relevant, as they were only observed in one sex, there was no dose–response relationship, the changes were small and there were no histopathological changes in liver and brain.

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

The Panel identified a no observed adverse effect level (NOAEL) of 349 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 cellulase produced with the Aspergillus niger strain HBI‐AC01 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.28

No reports on oral or respiratory sensitisation or elicitation reactions of the cellulase under assessment have been published.

Respiratory allergy, e.g. baker's asthma, following occupational exposure to cellulase has been described (Elms et al., 2003; Martel et al., 2010). Several studies have shown that individuals respiratorily sensitised to a food enzyme are usually able to ingest the corresponding allergen without acquiring clinical symptoms of food allergy (Armentia et al., 2009; Cullinan et al., 1997; Poulsen, 2004). Adverse reactions upon dietary exposure to cellulases 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 cellulase under assessment.

The production strain belongs to the Aspergillus genus, which is known to cause respiratory allergy (Kurup et al., 2000; Shen & Han, 1998; Vermani et al., 2015). Allergic reactions upon dietary exposure have been observed, but are rare (Xing et al., 2022). The biomass is removed during the production process; however, allergenic proteins of the production strain can be released into the culture medium from which the food enzyme is obtained.

■■■■■, products from soy and wheat, that may cause allergies or intolerances (listed in the Regulation (EU) No 1169/201129) are used as raw materials. In addition, corn steep liquor, a known source of allergens, is present in the culture medium. During the fermentation process, these products will mostly be degraded and utilised by the production strain.

Taken together, concerning the potential allergic reactions due to the production strain and the raw materials in the culture medium, 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 3.5.2), 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 three food 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. 30

In production of baked products, the food enzyme is added to flour during dough making.31 The enzymatic treatment improves dough handling and reduces batter stiffness.32 The food enzyme–TOS remain in the final baked products.

In the production of brewed products, the cellulase is added to the cereals during the mashing step or to the wort during fermentation.33 The enzymatic treatment hydrolyses cellulose, reducing viscosity and expanding the variety of suitable raw materials.34 The food enzyme–TOS remain in the brewed products.

In the production of distilled alcohol, cellulase may be added to the cereals during slurry mixing, liquefaction, pre‐saccharification or during the fermentation step.35 The enzymatic treatment decreases viscosity, improves processing and increases yield.36 The food enzyme–TOS are not carried over with the distilled alcohols (EFSA CEP Panel, 2023).

Based on data provided on thermostability (see Section 3.3.1) and the downstream processing steps applied in the respective food manufacturing processes, the Panel considered that the food enzyme may remain in its active form in baked and brewed products, 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 two food manufacturing processes where the food enzyme–TOS remain 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 0.475 mg TOS/kg bw per day in adults 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 (349 mg TOS/kg bw per day) identified from the 90‐day rat study with the derived exposure estimates of 0–0.250 mg TOS/kg bw per day at the mean and from 0 to 0.475 mg TOS/kg bw per day at the 95th percentile resulted in a margin of exposure (MOE) of at least 735.

CONCLUSION

4

Based on the data provided and the derived margin of exposure, the Panel concluded that the food enzyme cellulase produced with the non‐genetically modified Aspergillus niger strain HBI‐AC01 does not give rise to safety concerns under the intended conditions of use.

DOCUMENTATION AS PROVIDED TO EFSA

5

Dossier “Cellulase from Aspergillus niger”. August 2022. Submitted by HBI Enzymes Inc.

Additional information. January 2024. Submitted by HBI Enzymes Inc.

Additional information. September 2025. Submitted by HBI Enzymes Inc.

REQUESTOR

European Commission

QUESTION NUMBER

EFSA‐Q‐2022‐00518

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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