Modifications of the Structural, Nutritional, and Allergenic Properties of Atlantic Cod Induced by Novel Thermal Glycation Treatments

Overview

Journal Foods

Specialty Biotechnology

Date 2024 Jul 27

PMID 39063259

Authors

Xin Dong

Vijaya Raghavan

Affiliations

Soon will be listed here.

Abstract

This study aimed to assess the effect of novel thermal glycation, utilizing microwave processing (100-150 °C) combined with sugars (glucose and lactose), on the in vitro protein digestibility, peptides, secondary structures, microstructures, and allergenic properties of Atlantic cod. The research demonstrated that microwave heating at 150 °C with glucose significantly reduced cod allergenicity by up to 16.16%, while also enhancing in vitro protein digestibility to 69.05%. Glucose was found to be more effective than lactose in conjunction with microwave heating in reducing the allergenicity of Atlantic cod. Moreover, treatments conducted at 150 °C were more effective in increasing in vitro protein digestibility and peptide content compared to those at 100 °C. This study revealed that the novel processing technique of thermal glycation effectively reduced the allergenicity of Atlantic cod. It also offered fresh insights into the potential benefits of combining microwave heating with sugars.

References

Khalid W, Maggiolino A, Kour J, Arshad M, Aslam N, Afzal M . Dynamic alterations in protein, sensory, chemical, and oxidative properties occurring in meat during thermal and non-thermal processing techniques: A comprehensive review. Front Nutr. 2023; 9:1057457. PMC: 9876618. DOI: 10.3389/fnut.2022.1057457. View

Luo C, Hu C, Gao J, Li X, Wu Z, Yang A . A potential practical approach to reduce Ara h 6 allergenicity by gamma irradiation. Food Chem. 2012; 136(3-4):1141-7. DOI: 10.1016/j.foodchem.2012.09.091. View

Mukherjee S, Horka P, Zdenkova K, cermakova E . Parvalbumin: A Major Fish Allergen and a Forensically Relevant Marker. Genes (Basel). 2023; 14(1). PMC: 9858982. DOI: 10.3390/genes14010223. View

Dong X, Wang J, Raghavan V . Impact of microwave processing on the secondary structure, in-vitro protein digestibility and allergenicity of shrimp (Litopenaeus vannamei) proteins. Food Chem. 2020; 337:127811. DOI: 10.1016/j.foodchem.2020.127811. View

Baird G, Farrell C, Cheung J, Semple A, Blue J, Ahl P . FTIR Spectroscopy Detects Intermolecular β-Sheet Formation Above the High Temperature T for Two Monoclonal Antibodies. Protein J. 2020; 39(4):318-327. PMC: 7387379. DOI: 10.1007/s10930-020-09907-y. View

Kalic T, Radauer C, Lopata A, Breiteneder H, Hafner C . Fish Allergy Around the World-Precise Diagnosis to Facilitate Patient Management. Front Allergy. 2022; 2:732178. PMC: 8974716. DOI: 10.3389/falgy.2021.732178. View

Dwek R . Glycobiology: Toward Understanding the Function of Sugars. Chem Rev. 1996; 96(2):683-720. DOI: 10.1021/cr940283b. View

Zhang Q, Huang Z, Li H, Cen C, Zheng R, Lili C . Deciphering Changes in the Structure and IgE-Binding Ability of Ovalbumin Glycated by α-Dicarbonyl Compounds under Simulated Heating. J Agric Food Chem. 2022; 70(6):1984-1995. DOI: 10.1021/acs.jafc.1c06939. View

Ma X, Chen H, Gao J, Hu C, Li X . Conformation affects the potential allergenicity of ovalbumin after heating and glycation. Food Addit Contam Part A Chem Anal Control Expo Risk Assess. 2013; 30(10):1684-92. DOI: 10.1080/19440049.2013.822105. View

10.

Dong X, Raghavan V . High-intensity ultrasound treatment of Atlantic cod: Impact on nutrients, structure, sensory quality, bioactivity, and in-vitro digestibility. Food Res Int. 2024; 186:114363. DOI: 10.1016/j.foodres.2024.114363. View

11.

Li R, Wu Z, Wangb Y, Ding L, Wang Y . Role of pH-induced structural change in protein aggregation in foam fractionation of bovine serum albumin. Biotechnol Rep (Amst). 2017; 9:46-52. PMC: 5360987. DOI: 10.1016/j.btre.2016.01.002. View

12.

Mirmoghtadaie L, Shojaee Aliabadi S, Hosseini S . Recent approaches in physical modification of protein functionality. Food Chem. 2016; 199:619-27. DOI: 10.1016/j.foodchem.2015.12.067. View

13.

Gruber P, Becker W, Hofmann T . Influence of the maillard reaction on the allergenicity of rAra h 2, a recombinant major allergen from peanut (Arachis hypogaea), its major epitopes, and peanut agglutinin. J Agric Food Chem. 2005; 53(6):2289-96. DOI: 10.1021/jf048398w. View

14.

Cardoso H, Wierenga P, Gruppen H, Schols H . Maillard induced aggregation of individual milk proteins and interactions involved. Food Chem. 2018; 276:652-661. DOI: 10.1016/j.foodchem.2018.10.061. View

15.

Pi X, Liu J, Sun Y, Ban Q, Cheng J, Guo M . Heat-induced changes in epitopes and IgE binding capacity of soybean protein isolate. Food Chem. 2022; 405(Pt A):134830. DOI: 10.1016/j.foodchem.2022.134830. View

16.

Huang Z, Jiang Y, Li H, Li Q, Gao Z, Zhang Y . Effect of glycation derived from α-dicarbonyl compounds on the in vitro digestibility of ovalbumin: Tracing of advanced glycation end-products and immuno-active peptides. Food Res Int. 2023; 169:112842. DOI: 10.1016/j.foodres.2023.112842. View

17.

Tsai C, Perng K, Hou Y, Shen C, Chen I, Chen Y . Effect of species, muscle location, food processing and refrigerated storage on the fish allergens, tropomyosin and parvalbumin. Food Chem. 2022; 402:134479. DOI: 10.1016/j.foodchem.2022.134479. View

18.

Wang Y, Liu C, Lang H, Hu Z, Wang X, Yang Z . Effects of microwave on the structural and emulsifying properties and interfacial properties of oxidized soybean protein aggregates. Food Chem X. 2023; 19:100861. PMC: 10534243. DOI: 10.1016/j.fochx.2023.100861. View

19.

Wu Y, Dong L, Wu Y, Wu D, Zhang Y, Wang S . Effect of methylglyoxal on the alteration in structure and digestibility of α-lactalbumin, and the formation of advanced glycation end products under simulated thermal processing. Food Sci Nutr. 2021; 9(4):2299-2307. PMC: 8020911. DOI: 10.1002/fsn3.2211. View

20.

Joye I . Protein Digestibility of Cereal Products. Foods. 2019; 8(6). PMC: 6617089. DOI: 10.3390/foods8060199. View