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Reduction of peanut allergens by high pressure combined with polyphenol oxidase


Key words Allergens, high pressure, polyphenol oxidase, peanut
Latest version 2013/12/12
Completed by FRIP

How does it work?

Primary objective Reduction of peanut allergens can be achieved through high pressure combined with polyphenol oxidase
Working principle Peanut allergy is one of the most serious food allergies, and Ara h 2 is one of the most important peanut allergens as it is recognised by serum immunoglobulin E from more than 90% of peanut-allergic individuals [1]. High pressure processing (HPP) is normally applied to food allergens (e.g. Effect of oxidation and high pressure treatment on fruit and vegetable juices deallergization) for reduction of their immunoreactivity. For instance, allergens from such foods as soybean,[2], apple,[3] carrot,[4] and beef [5] are reported to have to a lower immunoreactivity after HP treatment. However, HPP (300 or 500MPa) alone had no direct effect on the major peanut allergens (Ara h 1 and Ara h 2). On the other hand, HPP can exert an indirect effect by enhancing polyphenol oxidase (PPO) activity. combination may perform much better than PPO alone in terms of reducing the allergenic capacity of peanut extracts [6]. PPO(tyrosinase) is a copper-containing enzyme widely distributed in fruits and vegetables. It catalyzes the oxidation of phenols such as caffeic acid (CA) to o-quinones, which react with the amino groups of proteins to form cross-links or protein polymers (Figure 1) [7].

PPO together with CA reduces the allergenic capacity of peanut allergens by cross-linking and masking the immunoglobulin E (IgE)-binding sites of peanut allergens.

When PPO was combined with HPP at 300MPa and applied to peanut extracts, the results were the same as those of PPO itself. However, pressure treatment at 500MPa combined with PPO induced a higher (approximately two-fold) reduction of the major peanut allergens, in comparison with PPO alone or with PPO combined with HPP at 300 MPa [6].

Figure 1. Formation of protein–protein cross-links in a PPO-catalyzed reaction. Proteins (P1 and P2) are cross-linked as shown in the presence of PPO and CA..
Additional effects microbial stabilization in dependence of HPP conditions, rancidity
Important process parameters Pressure, time, temperature, content of PPO
Important product parameters pH, amount of product

What can it be used for?

Products peanuts
Operations Deallergization
Solutions for short comings This technology allows to produce peanuts with lower content of allergens

What can it NOT be used for?

Other limitations See important parameters.
Risks or hazards No clinical tests have been performed yet. Each batch of deallergized peanut should be checked by some quick allergenicity test


Maturity This technology is not yet used at industrial scale, clinical tests have to be done first. HP equipment is available at industrial scale though.
Modularity /Implementation The technology could be implemented in a general production line.
Consumer aspects According to several investigations, HPP has been judged to be relatively similar to conventional process technologies in terms of overall consumer acceptability [8].
Legal aspects Allergens presence labelling is under the EU legislation regulation.

The EFSA Journal (2004) 32, 1 – 197; Opinion of the Scientific Panel on Dietetic Products, Nutrition and Allergies on a request from the Commission relating to the evaluation of allergenic foods for labelling purposes Directive 2003/89/EC of the European Parliament and of the Council of 10 November 2003 Directive 2000/13/EC of the European Parliament and of the Council of 20 March 2000 Directive 2006/142/EC of the European Parliament and of the Council of 22 December 2006 Directive 2005/26/EC of the European Parliament and of the Council of 21 March 2005

Environmental aspects No substantial impact of this technology on energy consumption or environment is known.

Further Information

Institutes FRIP, Southern Regional Research Center
References [1] Hu Chun-qiu, Chen Hong-bing, Gao Jin-yan et al.: High-pressure microfluidisation-induced changes in the antigenicity and conformation of allergen Ara h 2 purified from Chinese peanut. Journal of the Science of Food and Agriculture. 2011; 91(7): 1304-1309

[2] Penas E, Gomez R, Friasa J, Baeza ML, Vidal-Valverdea C.: High hydrostatic pressure effects on immunoreactivity and nutritional quality of soybean products. Food Chem. 2011; 125:423–429.

[3] Husband FA, Aldick T, Van der Plancken I, Grauwet T, Skypala I, Mackie A.: High pressure treatment reduces the allergenicity of the major allergens in apple and celeriac. Mol Nutr Food Res. 2011; 55:1087–1095.

[4] Heroldova M, Houska M, Vavrova H, Kucera P, Setinova I, Honzova S.: Influence of high-pressure treatment on allergenicity of rDau c1 and carrot juice demonstrated by in vitro and in vivo tests. High Press Res. 2009; 29:695–704.

[5] Yamamoto S, Matsuno N, Mikami M, Hara T, Odani T, Suzuki A, Nishiumi T.: Effects of a high pressure treatment on bovine gamma globulin and its reduction in allergenicity. Biosci Biotechnol Biochem. 2010; 74(3):525–530.

[6] Chunga Si-Yin, Houska M and Reed S.: Reducing peanut allergens by high pressure combined with polyphenol oxidase. High Pressure Research. 2013;

[7] Chung SY, KatoY, Champagne ET.: Polyphenol oxidase/caffeic acid may reduce the allergenic properties of peanut allergens. J Sci Food Agric. 2005; 85:2631–2637.

[8] Sorenson D. and Henchion M.: Understanding consumers’ cognitive structures with regard to high pressure processing: A means-end chain application to the chilled ready meals category. Food Quality. 2011; 22 (3): 271–280.

Pressure, time, temperature, content of PPO pH, amount of product High Pressure equipment 2.1.2 physical, chemical conversion not applicable Web of science: peanut allergens high pressure - 10 articles were found, no all are relevant, also sources from internet (Google) were used. WikiSysop :Template:Review document :Template:Review status

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Created by LandfeldA on 11 December 2013, at 12:12