Novel Food Information - AquAdvantage Salmon

Health Canada has notified AquaBounty Canada Inc. that it has no objection to the food use of AquAdvantage salmon (AAS). The Department conducted a comprehensive assessment of this fish according to the Codex Alimentarius Guideline for the Conduct of Food Safety Assessment of Foods Derived from Recombinant-DNA Animals. These guidelines are internationally accepted principles for establishing the safety of foods with novel traits.

Background

The following provides a summary of the notification from AquaBounty Canada Inc. and the evaluation by Heath Canada and contains no confidential business information.

1. Introduction

AAS are Atlantic salmon (Salmo salar) that have been genetically modified (GM) to grow more rapidly. The AAS is intended to be sold on the market as fillets. There will be no importation of live fish. AAS contains the protein coding domain of a growth hormone (GH) gene from Chinook salmon and the regulatory sequences of an antifreeze protein (AFP) gene from the ocean pout. The integrated GH transgene allows AAS to grow more rapidly during early-life and therefore reach market size sooner. As adults, AAS are not larger than their non-transgenic comparators.

The immediate result of AAS production is predominantly triploid eyed-eggs that will generate sterile female Atlantic salmon containing a single copy of the GH transgene. The eggs will be produced in AquaBounty's facility in Prince Edward Island and then shipped to AquaBounty's land based facility in Panama where they will be grown to market size, processed, and shipped to approved markets for food consumption.

The safety assessment performed by Food Directorate evaluators was conducted according to the Codex Alimentarius Guideline for the Conduct of Food Safety Assessment of Foods Derived from Recombinant-DNA Animals. The assessment considered: how AAS was developed; how the composition and nutritional quality of AAS compares to non-modified salmon; what the potential is for AAS to be toxic or cause allergic reactions; and the health status of AAS. AquaBounty Canada has provided data which demonstrates that AAS are as safe as traditional farmed salmon varieties used as food in Canada.

The Food Directorate has a legislated responsibility for pre-market assessment of novel foods and novel food ingredients as detailed in the Food and Drug Regulations (Division 28). Foods derived from AAS are considered novel foods under the following part of the definition of novel foods: "c) a food that is derived from a plant, animal or microorganism that has been genetically modified such that

  1. the plant, animal or microorganism exhibits characteristics that were not previously observed in that plant, animal or microorganism."

2. Product Development

The petitioner has provided information describing the methods used to develop AAS and data that characterize the genetic modification which results in the rapid growth phenotype.

AAS was developed by micro-injection of the opAFP-GHc2 construct into wild-type Atlantic salmon eggs. The transgene is comprised of the protein coding domain of a growth hormone gene (GH) from Chinook salmon (Oncorhynchus tshawytscha) and the regulatory sequences (opAFP) of an antifreeze protein (AFP) gene from the ocean pout (Macrozoarces americanus).

The AAS eggs are produced by fertilizing eggs from non-transgenic female Atlantic salmon with milt (sperm) from neomales that are homozygous for the EO-1α transgene (AAS broodstock). The neomale AAS broodstock have undergone sex reversal using 17α-methyltestosterone. The fertilized eggs are then treated with hydrostatic pressure shock to induce triploidy. This process is slightly less than 100% effective at inducing triploidy and could lead to a very small number of diploid eyed-eggs (≤1%). Therefore, both diploid and triploid AAS were assessed for safety.

The transgenic founder animal was designated EO-1. The commercial line was derived from the progeny of EO-1 through multigenerational crosses with domesticated Atlantic salmon broodstock common to Atlantic Canada. The current generation (F10) of AAS carries a single copy of the integrated transgene (EO-1α) that is genetically stable and predictably heritable. A β-locus integrant was present in some F2 fish during early stages of product development, but was removed by selecting for the α-locus during the selective breeding process leading to the final commercial line. AAS is hemizygous at the α-locus for the stably integrated transgene EO-1α. The opAFP-GHc2 construct was prepared using standard molecular-cloning techniques. The construct contains the 5' flanking sequence, promoter elements, 5' UTR region, and 3' flanking sequence of the ocean pout AFP gene along with the complementary DNA sequence coding region and 3'UTR of the Chinook salmon GH gene.

3. Characterization of the Modified Animal

Southern blot analysis was performed to characterize the insertion of novel DNA into the salmon genome. AAS genomic DNA digested with PstI was hybridized with a 1.2 kb probe that represented a fragment of the ocean pout AFP promoter region. The AAS showed a single band of ~5 kb which indicated random integration of a single copy of the transgene at a single locus.

PCR analysis of individual F2-generation progeny demonstrated that the promoter region of EO-1α had been subject to 5' to 3' rearrangement during integration of the transgene into the EO-1 genome. However, the possibility of a tandem copy of opAFP-GHc2 was eliminated by further Southern blot analysis of the locus using multiple restriction enzyme analyses that hybridize to the 5'OP and 3'OP domains. The data therefore was consistent with a 5' to 3' rearrangement of a single copy of the transgene that was subject to a break-point in the 5'OP domain.

The 5' to 3' rearrangement was subsequently confirmed using linker-mediated PCR to genome walk. Nucleotide sequence analysis of a ~250 bp PCR product revealed ~70 bp of 5'OP sequence downstream from the proposed break-point in opAFP-GHc2, which adjoined ~125 bp of flanking sequence from the Atlantic salmon genome. Also, analysis of a ~450 bp PCR product revealed ~145 bp of 5'OP sequence upstream of the proposed break-point which adjoined ~268 bp of genomic flanking sequence. This rearrangement did not result in any changes to the sequence of the Chinook salmon GH-1 transgene.

The analysis of the rearrangement also determined the presence of a 45 bp plasmid-vector sequence between the 3'OP domain and the displaced 5'-flank of the 5'OP domain in EO-1α. This 45 bp sequence is derived from the multiple cloning sites of pUC9 and pUC18. The multiple cloning site from pUC18 comprises 20 bp from the 5'-EcoR I to BamH I site and the multiple cloning site sequence from pUC9 comprises 25 bp from the 3' Hind III to EcoR I site.

Sequence analysis also demonstrated that the EO-1α insert is flanked by a 35 bp repeat region of genomic DNA which suggests that the α-integrant did not disrupt any endogenous genes during integration.

The EO-1α locus comprises four principal domains, and one non-functional "intragenic" sequence, from three sources as follows: a 613 bp transcription-initiation(i.e., promoter) domain from a genomic clone (λOP5) of the Type III AFP gene from ocean pout, a 705 bp protein-codingdomain from a cDNA clone (GH-4) of the GH-I gene from Chinook salmon, a 1164 bp transcription-terminationdomain from λOP5 comprising transcription termination and polyadenylation signals of the Type III AFP gene, a 45 bp, non-sense polylinkersequence from pUC9 and pUC18 that is an artifact of plasmid-transgene construction and integration.

Genomic DNA from the F1 progeny of EO-1♀ was screened for the presence of plasmid vector sequence (other than the aforementioned 45 bp of multiple cloning site sequence) that may have integrated following co-injection with the linearized rDNA constructs, using Southern blot analysis following restriction enzyme digestion. The restriction enzymes HindIII, Bgl II and PstI were used along with a full length probe derived from pUC19 which included the ampR gene. F1 progeny of EO-1♀ showed no detectable hybridization bands when digested with the above mentioned restriction enzymes, indicating that AAS does not contain any vector sequences.

An analysis of the EO-1α locus for novel open reading frames (ORF) was performed using bioinformatics. There were eight ORF's identified from this analysis which had a start and stop codon as well as a minimum length of 150 bp. None of these ORF's extended from the flanking DNA into the EO-1α locus. One ORF was found to extend from the locus into the genomic flanking region. BLAST analysis of the predicted amino acid sequences of the eight ORF's reveals no significant homology with other known biologically active proteins, and none were associated with the regulatory elements within the EO-1α locus that would be required for active transcription. Also, the construct was found to be located within a repeat region of the host organism genome. Therefore, it would be highly unlikely that the region flanking the insertion site would contain the necessary elements to generate a novel ORF. The expression of a novel polypeptide or fusion protein from a novel ORF at the EO-1α locus is highly unlikely.

The heritability and stability of the EO-1α line which contains the opAFP-GHc2 construct was determined using Southern blot analysis and multiplex PCR. This analysis also confirmed the absence of the β-locus. AAS from the F2 to F6 generations were examined. The hybridisation patterns and amplification patterns were consistent with a stably integrated and heritable copy of the α-locus and the absence of the β-locus. PCR results also confirmed the absence of the β-locus in the commercial line.

Southern blot analysis of AAS across multiple generations, including those F2 fish which also contained a β-locus integrant, produced an inheritance pattern that is consistent with Mendelian inheritance. Later generations of fish which contained only the α-integrant produced an inheritance pattern that is consistent with Mendelian inheritance principles for a single locus trait. This analysis also confirmed once more the lack of the β-integrant in the commercial line.

4. Product Information

The integrated transgene codes for one expression product, the growth hormone (GH) from Chinook salmon. Based on the synthesis of the construct opAFP-GHc2, no changes were made to the primary sequence of the GH coding domain. Also, the promoter element and 3' termination signal remained intact despite the rearrangement of EO-1α during integration.

The Chinook salmon GH-1 produced in AAS was shown to have a sequence difference of 5.9 % compared with the endogenous Atlantic salmon GH-1. There are 210 total residues comprising GH-1 in both species, and the Chinook and Atlantic salmon sequences differ in ten residues, seven of which show strong residue similarity. The genes encoding Chinook and Atlantic salmon GH-1 did not show differential gene expression patterns. Sequence analysis has shown that the protein coding region of the transgene is 100% homologous to the naturally occurring chinook salmon GH gene, which is approximately 95% homologous with the Atlantic salmon GH gene.

The opAFP-GHc2 construct encodes a GH protein that is homologous with that of the native GH-1 from Chinook salmon, and does so in the proper context of regulatory elements from the ocean pout to enable active transcription.

5. Dietary Exposure

AAS represent an alternative to other farmed Atlantic salmon fillets in the marketplace. Dietary exposure will be relying on existing seafood preferences. The consumption of AAS is expected to represent a small proportion of the Atlantic salmon already being consumed by the Canadian public. AAS is not expected to affect the total consumption of salmon by Canadian consumers.

6. Nutrition

The petitioner compared the nutritional composition of AAS fillets with non-GM farmed Atlantic salmon sponsor controls (SC).

The nutritional composition study was single-blinded and comparator-controlled. Edible tissue samples (muscle-skin fillets) were analyzed to determine composition in AAS and control fish (farmed and sponsor). The analytes measured in the AAS and controls (farmed and sponsor) were: proximates (moisture, protein, fat, carbohydrate, ash), amino acids, fatty acids, minerals (calcium, copper, iron, magnesium, manganese, phosphorus, potassium, sodium, zinc, and selenium), and vitamins (folic acid, niacin, pantothenic acid, vitamin A, vitamin B1, vitamin B2, vitamin B6, vitamin B12, and vitamin C).

In the complete compositional data set (triploid and diploid, male and female SC and AAS), the following analytes in the AAS were statistically different from SC (but were within the range reported in the literature for salmon): moisture (-7%), protein (-6%) and amino acids (levels were, in general, proportional with the lower protein), total fat (+71%) and fatty acids except eicosenoic acid (i.e. eicosenoic acid was not statistically different from SC, but other fatty acid levels were, in general, proportional with the higher total fat), niacin (+10%), pantothenic acid (-13%), vitamin B1 (-12%), vitamin C (-20%), potassium (-7%), selenium (-6%), and magnesium (-10%).

A data analysis of the subset of triploid female AAS and triploid female SC salmon, as well as a separate subset analysis of diploid female AAS and diploid female SC salmon were also provided by the petitioner. In the triploid groups, the following analytes in the AAS were statistically different from the triploid SC: moisture (-6%), protein (-9%) and amino acids except tryptophan (i.e. tryptophan was not statistically different from SC, but other amino acid levels were, in general, proportional with the lower protein), total fat (+75%) and fatty acids except eicosenoic acid (i.e. eicosenoic acid was not statistically different from SC, but other fatty acid levels were, in general, proportional with the higher total fat), magnesium (-12%), phosphorous (-7%), potassium (-10%), and selenium (-6%). In the diploid groups, the following analytes in the AAS were statistically different from SC: niacin (+15%), pantothenic acid (-23%), vitamin B1 (-18%), vitamin B6 (+16%), and vitamin C (-33%).

The Food and Drug Administration in the United States (FDA) completed their own analyses of the AquaBounty data. The results of the FDA analyses showed that vitamin B6 levels in the AAS was statistically different from controls (sponsor and farmed), but following an exposure assessment, the FDA concluded that there was no food consumption hazard due to vitamin B6, and that overall, the nutrient levels of AAS are similar to levels in appropriate comparator salmon (e.g., SC, FC, literature reports, or some combination of the three).

Nutrient composition differences have also been reported between wild and non-GM farmed salmon, and Friesen EN et al. 2015Footnote 1 indicated that these differences were larger than those seen for GM versus non-GM Coho salmon. In addition, the authors indicated that diet and rearing location could have a larger effect on nutrient composition than transgenic differences.

As part of the nutritional assessment, Health Canada reviewed both the AquaBounty study and the FDA analysis. In addition, Health Canada compared the AAS nutrient values to those reported for Atlantic salmon in the Canadian Nutrient File (CNF) (e.g., wild and/or farmed) and other databases (e.g., Norway National Institute of Nutrition and Seafood Research (NIFES) Farmed Atlantic salmon), and to the nutrient values reported for another salmon species, Chinook salmon, which was the source of the growth hormone gene for this event.

There were some components reported as statistically different in the original AquaBounty study, the triploid and diploid female salmon data analysis, and in the FDA analysis. For the complete compositional data set the AAS nutrient levels of moisture, protein, amino acids, vitamin C, pantothenic acid, vitamin B1, vitamin B6, potassium, magnesium and selenium were within the ranges reported for controls (farmed and sponsor), Atlantic salmon in the CNF (wild and/or farmed), other databases, and/or those reported for Chinook salmon. The AAS niacin levels did not fall within the ranges reported for the above comparators. The potential increases in niacin consumption resulting from AAS intake, however, would not pose a nutritional concern. According to the IOM (2004), there is no evidence of adverse effects associated with the excessive consumption of naturally occurring niacin in foods.

The total fat reported for AAS is within the ranges reported in other databases including the CNF farmed Atlantic salmon, Norway NIFES farmed Atlantic salmon and those reported in the literature (e.g., Friesen EN et al. 2015). For fatty acids, including the nutritionally important omega-3 fatty acids present in salmon, (docosahexanoic and eicosopenanoic acids), the levels reported in the AAS were within the ranges reported in the above databases, and proportional with the level of total fat. This is also consistent with the findings for protein as the lower levels of amino acids were proportional with the lower level of protein. These observations suggest that there were no substantial changes to the fat and protein profiles to pose any nutritional concerns.

Health Canada's comments for the triploid and diploid female salmon compositional data subsets are consistent with the comments for the complete compositional data set. For the majority of nutrients, the nutrient levels of the triploid or diploid AAS fall within the ranges reported for controls (farmed and sponsor), Atlantic salmon in the CNF (wild and/or farmed salmon), other databases, and/or those reported for Chinook salmon. In the diploid AAS, the niacin level remained higher than the compared ranges, but this level is not of nutritional concern. Consistent with the original analysis, there were also no substantial changes in the fat and protein profiles to pose a nutritional concern.

Based on the review of the above information, there were no nutritional safety concerns identified with the use of AAS as food in Canada.

7. Toxicology

Health Canada assessed information provided by the petitioner on the potential toxicity of AAS and the novel Chinook salmon growth hormone 1 (GH-1) protein that is produced by AAS. The production process generates triploid and diploid AAS. The triploid fish constitutes ≥ 99 % of all the GM fish produced by this method, as determined by fluorescence-activated cell sorting. Both triploid and diploid fish were assessed for safety since both could be consumed by the public.

AAS produces transgenic GH-1 derived from Chinook salmon. Chinook salmon is a commercially farmed or harvested finfish that can be readily purchased in supermarkets. The consumption of Chinook salmon (which includes Chinook salmon GH-1) is not associated with any toxicity and it can be considered to have a safe history of food use.

The expression levels of total GH protein in the muscle and skin tissue of market-sized triploid AAS, diploid AAS, non-transgenic sibling control salmon and farmed control salmon were below the limits of quantitation (LOQ = 10.40 ng GH-1/g muscle-skin), as determined by radioimmunoassay. As the total GH levels in transgenic salmon were indistinguishable from those of non-transgenic salmon, it can be concluded that consumers of transgenic triploid AAS, diploid AAS or non-transgenic salmon would be exposed to similar levels of total fish GH.

The scientific literature has consistently shown that dietary growth hormones from various animal species have very poor bioavailability in mammals and humans (i.e., ingested GH would likely be digested and not be absorbed as an intact peptide in the gastrointestinal tract). Additionally, it is expected that any minute amount of Chinook salmon GH-1that is absorbed would not be able to elicit a somatotropic response in consumers due to the species specificity exhibited by the human GH receptor.

Taken together, the exposure to total GH-1 from triploid and diploid AAS is indistinguishable from non-transgenic salmon. Like non-transgenic Chinook salmon GH-1, transgenic Chinook salmon GH-1 would not be expected to survive digestion or activate human GH receptors when consumed with AAS.

The expression levels of endogenous regulatory hormones related to metabolism (triiodothyronine (T3), thyroxin (T4)) and sexual maturation (estradiol, testosterone, 11-ketotestosterone) in the muscle and skin tissues were demonstrated by radioimmunoassay, not to be significantly different between market-sized triploid AAS, diploid AAS and non-transgenic salmon.

The expression levels of the endogenous growth hormone insulin-like growth factor 1 (IGF-1) were not detectable (LOD: 2.18 ng/g) or quantifiable (LOQ: 3.27 ng/g) in the muscle-skin tissue of triploid female AAS and non-transgenic sponsor and farmed control salmon. It can be concluded that consumers of transgenic triploid AAS or non-transgenic salmon would be exposed to similar levels of IGF-1.

There was a 4% difference in mean muscle-skin IGF-1 values between mature female diploid AAS and mature female diploid sponsor control salmon; this slight difference was not considered to be biologically or statistically significant.

One diploid female AAS showed an increase in muscle-skin IGF-1 compared to sponsor control salmon (i.e., the maximum IGF-1 level reported in this diploid female AAS was ~ 50% greater than that of maximum IGF-1 level reported in diploid female sponsor control fish). However, this increase was not considered toxicologically relevant since a daily serving of AAS containing the highest potential level of IGF-1 (reported in diploid female AAS) would not exceed the levels of IGF-1 present in a daily serving of milk and will have negligible health effects on the most sensitive subpopulation (teenage boys). Additionally, IGF-1 is poorly absorbed in the human gastrointestinal system and is not expected to produce a physiological effect as it will be sequestered by IGF binding proteins if it enters the circulation. Finally, exposure to IGF-1 from diploid AAS will be low as the probability of consuming diploid AAS is approximately 2 in every 1000 servings of AAS. The probability of chronic exposure to elevated levels of IGF-1 by consuming diploid AAS was considered negligible.

8. Allergenicity

Health Canada assessed information provided by the petitioner on the potential allergenicity of AAS and the Chinook salmon growth hormone 1 (GH-1) protein that is produced by this GM fish.

AAS produces transgenic GH-1 derived from Chinook salmon. Chinook salmon is a commercially farmed or harvested finfish that can be readily purchased in supermarkets. Routine consumption of GH-I from Chinook salmon muscle-skin is not associated with any allergenicity.

The expression levels of total GH protein in the muscle and skin tissue of market-sized triploid AAS, diploid AAS, non-transgenic sibling control salmon and farmed control salmon were below the limits of quantitation (LOQ = 10.40 ng GH-1/g muscle-skin), as determined by radioimmunoassay. As the total GH levels in transgenic salmon were indistinguishable from those of non-transgenic salmon, it can be concluded that consumers of transgenic triploid AAS, diploid AAS or non-transgenic salmon would be exposed to similar levels of total fish GH.

The source organism for the GH-1 sequence, Chinook salmon, is a potential source of proteins that can cause an allergic response in individuals allergic to finfish. An in silico search compared the amino acid sequences of Chinook salmon GH-1 to amino acid sequences of putative or known allergens. The results of the search determined that Chinook salmon GH-1 protein did not share significant sequence homology with putative or known allergens.

The scientific literature has consistently shown that dietary growth hormones from various animal species have very poor bioavailability in mammals and humans (i.e., ingested GH would likely be digested and not be absorbed as an intact peptide in the gastrointestinal tract). Therefore, Chinook salmon GH-1 is not expected to enter the blood circulation and elicit an immune response.

The exposure to total GH-1 from triploid and diploid AAS is indistinguishable from non-transgenic salmon. Chinook salmon GH-1 does not share significant sequence homology with putative or known allergens and is not expected to survive digestion. Taken together, it is not expected that transgenic Chinook salmon GH-1 would exert an allergenic effect when consumed with triploid or diploid AAS.

Health Canada lists seafood, which includes finfish such as salmon, as a priority food allergen. A radioallergosorbent inhibition assay (RI assay) was performed to compare the allergenic potencies of the protein extracts from the muscle and skin tissues of market-sized triploid AAS, diploid AAS and non-transgenic control salmon. Results of this experiment show that the levels of endogenous allergens in triploid AAS are within the range normally observed in non-transgenic salmon. As such, triploid AAS are not considered to be any more allergenic than non-transgenic salmon that are currently available to consumers.

Results of the RI assay showed that diploid AAS exhibited a statistically significant increase (1.5 fold) in allergen content compared to non-transgenic control salmon. The petitioner provided the opinion of of three allergen experts (associated with the University of Nebraska-Lincoln and Johns Hopkins Medicine). The experts concluded that the elevation in allergen content in diploid AAS is unlikely to be relevant in terms of a biological/clinical response and that this elevation would not exceed the variation that might occur when a consumer eats a small or large portion of food. Health Canada reviewed the opinion and concurred with the conclusions.

Diploid AAS are not considered to pose an additional allergenic concern to Canadian consumers as exposure to diploid AAS is very low (0.23% of all AAS can be diploid) and the elevation in allergen content is not expected to be biologically or clinically relevant to finfish allergic individuals. Additionally, those individuals who are allergic to finfish will likely also be allergic to Atlantic salmon and would avoid the consumption of all salmon, including products made from AAS.

9. Animal Health

The data provided demonstrated AAS were as healthy as non-transgenic salmon. Data submitted was of considerable volume and collected over 11 years and provide no indication of diminished capacity of AAS to survive at any life-stage or be more susceptible to microbial infections.

Diagnostic pathology of morbid or dead fish most often identified a non-infectious disease process or opportunistic infection (e.g. fungus, bacterial gill disease) not uncommon to aquaculture facilities. Nephrocalcinosis (non-infectious) was a finding common to both AquAdvantage and non-transgenic fish.

The submitted data showed that both GM and non-GM fish had slight to moderate morphological irregularities. These types of irregularities observed do occur in farm-raised Atlantic salmon. Even though there was a higher incidence of these irregularities in the GE fish, Health Canada's assessment concluded that these fish are as likely to survive to market weight and be no more susceptible to disease.

AAS do not appear to be less resistant to infectious diseases compared to non-transgenic salmon. Therefore, AAS would not be expected to require more veterinary drugs compared to conventional aquaculture salmon, and fillets derived from these fish would be comparable in terms of food safety and drug residue profiles.

Conclusion

Health Canada's review of the information presented in support of the food use of AAS does not raise concerns related to food safety. Health Canada is of the opinion that fillets derived from AAS are as safe and nutritious as fillets from current available farmed Atlantic salmon.

Health Canada's opinion deals only with the food use of AAS. Issues related to its use as animal feed have been addressed separately through existing regulatory processes in the Canadian Food Inspection Agency (CFIA). From their assessment, the CFIA concluded that there are no feed safety concerns.

The Canadian Environmental Protection Act, 1999 (CEPA 1999), administered by Environment Canada (EC) and Health Canada (HC), is the key authority for the Government of Canada to ensure that all new substances, including organisms, are assessed for their potential harm to the environment and human health. The New Substances Notification Regulations (Organisms) [NSNR (Organisms)] under CEPA 1999 prescribe the information that must be provided to EC prior to the import or manufacture in Canada of new organisms that are animate products of biotechnology, including fish products of biotechnology.

Fisheries and Oceans Canada (DFO), EC and HC have a Memorandum of Understanding respecting the implementation of the NSNR (Organisms) for fish. DFO assists in implementing the NSNR (Organisms) by conducting an environmental and indirect human health risk assessment for fish products of biotechnology and recommending any necessary measures to manage risks. The risk assessment conducted by DFO was peer-reviewed by an independent panel of experts under the auspices of the Canadian Science Advisory Secretariat.

The DFO completed their environmental risk assessment and determined that AAS was not "CEPA toxic"; in other words that there was no concern for the environment or indirect human health from the contained production of these fish. This decision allows AquaBounty Canada to produce sterile eyed-eggs in Canada in contained facilities. Any other growth of the fish outside of the approved contained production conditions would require another notification and is not currently allowed under the NSNR (Organisms).

This Novel Food Information document has been prepared to summarize the opinion regarding the subject product provided by the Food Directorate, Health Products and Food Branch, Health Canada.  This opinion is based upon the comprehensive review of information submitted by the petitioner according to the Guidelines for the Safety Assessment of Novel Foods.

(Également disponible en français)

For further information, please contact:

Novel Foods Section
Food Directorate
Health Products and Food Branch
Health Canada, PL2204A1
251 Frederick Banting Driveway
Ottawa, Ontario K1A 0K9
novelfoods-alimentsnouveaux@hc-sc.gc.ca

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