10/03
16 July 2003
FINAL ASSESSMENT REPORT
Full Report [ pdf 243kb ]
Executive Summary and Statement of Reasons
FSANZ received an Application from Danisco A/S to amend Standard 1.3.3 of theAustralia New Zealand Food Standards Code (the Code) to approve the use of an enzyme, hexose oxidase as a processing aid. Work commenced on 13 September 2002. The hexose oxidase is produced, using recombinant DNA techniques, from the host yeast Hansenula polymorpha which, contains the donor gene coding for hexose oxidase from the algae Chondrus crispus. The abbreviation HOX is used in this report to refer to the above enzyme.
There is currently no approval for the use of hexose oxidase as a food enzyme in Australia and New Zealand. The objective of this assessment is to determine whether it is appropriate to amend the Code to permit the use of hexose oxidase produced from this source.
The only regulatory options considered were to approve or not approve this application. Approval of the use of this enzyme has advantages for food manufacturers by providing them with a new enzyme, which can perform a range of functions for their food manufacturing. There are no significant disadvantages to food manufacturers, consumers or government agencies.
Hexose oxidase catalyses the oxidation of various mono- and oligosaccharides to lactones and hydrogen peroxide. The enzyme's main application is in bread making to increase dough strength and bread volume. The enzyme acts in a similar way to glucose oxidase for this purpose, however it has added advantages, since it acts on a wider range of substrates. Other applications in the food industries are in cheese and tofu manufacture where it aids curd formation, limiting undesirable browning by limiting Maillard reactions in food and as an oxygen scavenger during production of dressings and sauces. Use of HOX is technologically justified.
The enzyme can be isolated from the red algae Chondrus crispus. However this source is not a suitable production organism since recoveries are low. The gene for the enzyme was therefore inserted into the host yeast Hansenula polymorpha from which the enzyme can be recovered in economic quantities using a submerged fermentation process.
The gene, the vector and the host organism are all well characterised. The donor organism,Chondrus crispus (a seaweed commonly called Irish moss), has a long history of safe use in food. The host organism, Hansenula polymorpha is non-toxigenic and non-pathogenic. Hansenula polymorpha is used for the production of pharmaceutical products with two hepatitis B vaccines produced by recombinant techniques commercially available.
The safety assessment of HOX concluded that:
- the host organism and donor organisms are safe and demonstrate no evidence of toxicity and/or pathogenicity;
- the hexose oxidase gene is stably integrated into the host genome;
- the enzyme preparation complies with international specifications; and
- the enzyme preparation causes no mutagenic effects inin vitrostudies and there were no acute or subchronic toxicity effects in animals studies.
The safety assessment concludes that HOX, used as a processing aid poses no significant public health and safety risk.
In the USA a GRAS (Generally Recognized As Safe) expert panel has concluded that the enzyme is safe for food use as a processing aid. The enzyme is approved for use in baked goods (at a level up to 150 enzyme units/kg) in Denmark.
Public comment on the Initial Assessment Report for this application was sought from 9 October till 20 November 2002. Four submissions were received . Three (Goodman Fielder, Australian Food and Grocery Council (AFGC) and Food Technology Association of Victoria) supported approval of the use of the enzyme - subject to an appropriate safety assessment as part of the Draft Assessment. The fourth submission, from the Western Australian Department of Health raised a number of issues, which have been addressed.
Public comment on the Draft Assessment Report was sought from 19 March till 30 April 2003. Two submissions were received that both supported the application to approve the use of the enzyme as a processing aid.
The Final Assessment Report concludes that approval of the use of HOX as a food processing aid is technologically justified and does not pose a risk to public health and safety.
Statement of Reasons
The draft variation to Standard 1.3.3 - Processing Aids of the Food Standards Code, thereby giving approval for the use of HOX as a processing aid is recommended for the following reasons.
There are no significant public health and safety concerns associated with the use of the enzyme.
The use of the hexose oxidase enzyme is technologically justified since it has a role in food manufacturing, primarily with bread making to improve dough strength. It acts in a similar way to glucose oxidase but has wider substrate specificity. The enzyme may have potential applications in pasta and noodle manufacture where it acts in a similar way to bread making. Other potential food applications are in producing sauce and dressings, cottage cheese and tofu and limiting unwanted browning reactions.
The safety assessment of HOX found that the donor and the source organisms are safe and demonstrate no evidence of toxicity and/or pathogenicity and the hexose oxidase gene is stably integrated into the host organism.
The enzyme complies with the Joint Expert Committee on Food Additives (JECFA) specifications.
The proposed draft variation to the Food Standards Code is consistent with the section 10 objectives of the FSANZ Act. FSANZ has addressed the protection of public health and safety by undertaking a safety assessment on the enzyme. The assessment is based on the best available scientific data. An approval will give food manufacturers access to a broader range of enzymes, so encouraging an efficient and internationally competitive industry. Approval also promotes consistency with international food standards.
The benefits permitting use of the enzyme outweigh any costs associated with its use, giving manufacturers the benefits of an alternative to glucose oxidase, and an enzyme that has wider substrate specificity.
Full Report [ pdf 243kb ]