Determining the effect of malondialdehyde on the IgE-binding capacity of shrimp tropomyosin upon in vitro digestion.

BACKGROUND Stability in simulated gastric fluids is considered an important parameter for the estimation of food allergenicity. Moreover, proteins in food are highly susceptible to lipid oxidation during processing and preservation. In this study, the change in the IgE-binding capacity of malondialdehyde (MDA)-treated shrimp tropomyosin (TM) following in vitro digestion was investigated by SDS-PAGE and western blot. RESULTS Shrimp TM treated with different concentrations of MDA was slightly degraded and became increasingly resistant to pepsin digestion over time. While untreated TM was rapidly degraded, MDA-treated TM showed some resistance and was degraded by trypsin only after increasing the digestion time. Results of immunoblotting studies on IgE using sera from patients allergic to shrimp indicated that the IgE-binding capacity of TM and MDA (50 mmol L-1 )-treated TM decreased slightly after pepsin digestion and significantly decreased after trypsin digestion. CONCLUSION The study indicated that the resistance of TM to degradation increased after oxidation. The treatment with proteases, especially trypsin, is quite effective in decreasing the IgG/IgE-binding capacity of shrimp TM. © 2017 Society of Chemical Industry.

[1]  S. De Smet,et al.  Protein oxidation and proteolysis during storage and in vitro digestion of pork and beef patties. , 2016, Food chemistry.

[2]  T. Børresen Originality in Research – Is Your Manuscript Original? , 2016 .

[3]  Zhenxing Li,et al.  Effect of malondialdehyde treatment on the IgE binding capacity and conformational structure of shrimp tropomyosin. , 2015, Food chemistry.

[4]  K. Raes,et al.  Effect of carnosic acid, quercetin and α-tocopherol on lipid and protein oxidation in an in vitro simulated gastric digestion model , 2015, International journal of food sciences and nutrition.

[5]  R. Mason,et al.  Absence of an effect of vitamin E on protein and lipid radical formation during lipoperoxidation of LDL by lipoxygenase. , 2014, Free radical biology & medicine.

[6]  V. Muchenje,et al.  Natural antioxidants against lipid-protein oxidative deterioration in meat and meat products: A review. , 2014, Food research international.

[7]  Tian Tong-ton Effect of Protein Oxidation on Functional Properties of Whey Protein Isolates , 2014 .

[8]  M. Cao,et al.  Purification, physicochemical and immunological characterization of arginine kinase, an allergen of crayfish (Procambarus clarkii). , 2013, Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association.

[9]  Tilman Grune,et al.  Protein oxidation in aging and the removal of oxidized proteins. , 2013, Journal of proteomics.

[10]  J. Keller,et al.  Oxidative stress, neurodegeneration, and the balance of protein degradation and protein synthesis. , 2013, Free radical biology & medicine.

[11]  I. Pavlov,et al.  Penaeus monodon tropomyosin induces CD4 T-cell proliferation in shrimp-allergic patients. , 2012, Human immunology.

[12]  M. Lagarde,et al.  Structural and functional changes in human insulin induced by the lipid peroxidation byproducts 4-hydroxy-2-nonenal and 4-hydroxy-2-hexenal. , 2011, Chemical research in toxicology.

[13]  G. Martínez‐Rodríguez,et al.  In vitro digestion of protein sources by crude enzyme extracts of the spiny lobster Panulirus argus (Latreille, 1804) hepatopancreas with different trypsin isoenzyme patterns , 2010 .

[14]  S. Maleki,et al.  Stability of major allergen tropomyosin and other food proteins of mud crab (Scylla serrata) by in vitro gastrointestinal digestion. , 2010, Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association.

[15]  Y. Hua,et al.  Structural modification of soy protein by the lipid peroxidation product acrolein , 2010 .

[16]  Y. Hua,et al.  Structural modification of soy protein by the lipid peroxidation product malondialdehyde , 2009 .

[17]  M. Cao,et al.  Identification and characterisation of the major allergen of Chinese mitten crab (Eriocheir sinensis) , 2008 .

[18]  Guo Yongchao,et al.  Mouse model in food allergy: dynamic determination of shrimp allergenicity , 2008 .

[19]  S. Udompunturak,et al.  Specific allergy to Penaeus monodon (seawater shrimp) or Macrobrachium rosenbergii (freshwater shrimp) in shrimp‐allergic children , 2008, Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology.

[20]  V. Santé-Lhoutellier,et al.  Effect of oxidation on in vitro digestibility of skeletal muscle myofibrillar proteins. , 2007, Journal of agricultural and food chemistry.

[21]  Y. Nagashima,et al.  Molecular cloning of tropomyosins identified as allergens in six species of crustaceans. , 2007, Journal of agricultural and food chemistry.

[22]  E. Padlan,et al.  Why is there a greater incidence of allergy to the tropomyosin of certain animals than to that of others? , 2007, Medical hypotheses.

[23]  N. Porter,et al.  Mechanisms of free radical oxidation of unsaturated lipids , 1995, Lipids.

[24]  E. Palacios,et al.  Influence of highly unsaturated fatty acids on the responses of white shrimp (Litopenaeus vannamei) postlarvae to low salinity , 2004 .

[25]  Neil D. Rawlings,et al.  Handbook of proteolytic enzymes , 1998 .

[26]  M. Gershwin,et al.  IgE reactivity against a cross-reactive allergen in crustacea and mollusca: evidence for tropomyosin as the common allergen. , 1996, The Journal of allergy and clinical immunology.

[27]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.