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The changes induced by hydrodynamic cavitation treatment in wheat gliadin and celiac-toxic peptides

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Abstract

Hydrodynamic cavitation (HC) is thought weaken the allergenicity of beer gluten proteins. However, the mechanism of action has not been thoroughly studied. In this study, an HC device was used to treat wheat gliadin and two specific celiac-toxic peptides, P1 and P2. FT-IR, MFS, HPLC, and CD were used to monitor the structural characteristics of gliadin and the two peptides. HC reduced the abundance of the coeliac toxic peptides P1 and P2 in solution and the contents of secondary structure β-turns and PPII, which are related to reduced allergen immunoreactivity. This meant that both the primary and secondary structures of P1 and P2 were affected by HC, leading to fewer allergic reactions. This study was focused on the impact of HC on the secondary structures of allergens produced from gluten raw materials, and it has positive implications for reducing product allergenicity.

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Data availability

The data underlying this article are available and its online supplementary materials.

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Not applicable.

Abbreviations

ANOVA:

Analysis of variance

ANS:

8-Aniline-1-Naphthalenesulfonic Acid

CD:

Circular dichroism

FT-IR:

Fourier transform infrared spectroscopy

HC:

Hydrodynamic cavitation

HPLC:

High-performance liquid chromatography

MFS:

Molecular fluorescence spectroscopy

MRM:

Multiple reaction monitoring

P1:

PFPQPQLPY

P2:

PQPQLPYPQ

PBS:

Phosphate-buffered solution

ROS:

Reactive oxygen species

References

  • Albanese L, Ciriminna R, Meneguzzo F, Pagliaro M (2017) Gluten reduction in beer by hydrodynamic cavitation assisted brewing of barley malts. LWT - Food Sci Technol 82:342–353

    Article  CAS  Google Scholar 

  • Arya SS, More PR, Ladole MR, Pegu K, Pandit AB (2023) Non-thermal, energy efficient hydrodynamic cavitation for food processing, process intensification and extraction of natural bioactives: a review. Ultrason Sonochem 98:106504

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Bagal MV, Gogate PR (2014) Wastewater treatment using hybrid treatment schemes based on cavitation and Fenton chemistry: a review. Ultrason Sonochem 21(1):1–14

    Article  CAS  PubMed  Google Scholar 

  • Castro-Muñoz R, Boczkaj G, Jafari SM (2023) The role of hydrodynamic cavitation in tuning physicochemical properties of food items: a comprehensive review. Trends Food Sci Technol 134:192–206

    Article  Google Scholar 

  • Ciriminna R, Albanese L, Di Stefano V, Delisi R, Avellone G, Meneguzzo F, Pagliaro M (2018) Beer produced via hydrodynamic cavitation retains higher amounts of xanthohumol and other hops prenylflavonoids. LWT - Food Sci Technol 91:160–167

    Article  CAS  Google Scholar 

  • Gore MM, Saharan VK, Pinjari DV, Chavan PV, Pandit AB (2014) Degradation of reactive orange 4 dye using hydrodynamic cavitation based hybrid techniques. Ultrason Sonochem 21(3):1075–1082

    Article  CAS  PubMed  Google Scholar 

  • Guan X, Zhao X, Yin T (2016) Preparation and physicochemical propeities of hordein. J Chin Cereals Oils Assoc 31(4):47–50

    CAS  Google Scholar 

  • Guo P (2016) Influence of proline endo/exo conformers on PPII-helices. Unpublished Master of Science, The University of Chinese Academy of Sciences, Shanghai

    Google Scholar 

  • Han Y, Wang J, Li Y, Hang Y, Yin X, Li Q (2015) Circular dichroism and infrared spectroscopic characterization of secondary structure components of protein Z during mashing and boiling processes. Food Chem 188:201–209

    Article  CAS  PubMed  Google Scholar 

  • Herrera MG, Zamarreño F, Costabel M, Ritacco H, Hütten A, Sewald N, Dodero VI (2014) Circular dichroism and electron microscopy studies in vitro of 33-mer gliadin peptide revealed secondary structure transition and supramolecular organization. Biopolymers 101(1):96–106

    Article  CAS  PubMed  Google Scholar 

  • Huang X, Sontag-Strohm T, Stoddard FL, Kato Y (2017) Oxidation of proline decreases immunoreactivity and alters structure of barley prolamin. Food Chem 214:597–605

    Article  CAS  PubMed  Google Scholar 

  • Lamacchia C, Landriscina L, D’Agnello P (2016) Changes in wheat kernel proteins induced by microwave treatment. Food Chem. 197:634–640

    Article  CAS  PubMed  Google Scholar 

  • Landriscina L, D’Agnello P, Bevilacqua A, Corbo MR, Sinigaglia M, Lamacchia C (2017) Impact of gluten-friendly™ technology on wheat kernel endosperm and gluten protein structure in seeds by light and electron microscopy. Food Chem 221:1258–1268

    Article  CAS  PubMed  Google Scholar 

  • Liu F, Lai S, Tong H, Lakey PS, Shiraiwa M, Weller MG, Pöschl U, Kampf CJ (2017) Release of free amino acids upon oxidation of peptides and proteins by hydroxyl radicals. Anal Bioanal Chem 409(9):2411–2420

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Long G, Ji Y, Pan H, Sun Z, Li Y, Qin G (2015) Characterization of Thermal Denaturation Structure and Morphology of Soy Glycinin by FTIR and SEM. Int J Food Prop 18(4):763–774

    Article  CAS  Google Scholar 

  • Lu P, Yu T, Wang S, Wang J, Yang L (2006) Evaluation of protein determination methods. J Beijing Agric Univ 21(2):65–69

    Google Scholar 

  • Malalgoda M, Simsek S (2017) Celiac disease and cereal proteins. Food Hydrocoll 68:108–113

    Article  CAS  Google Scholar 

  • Meng-Xia X, Yuan L (2002) Studies on the hydrogen bonding of aniline’s derivatives by FT-IR. Spectrochim Acta A Mol Biomol Spectrosc 58(13):2817–2826

    Article  PubMed  Google Scholar 

  • Parrot I, Huang PC, Khosla C (2002) Circular dichroism and nuclear magnetic resonance spectroscopic analysis of immunogenic gluten peptides and their analogs. J Biol Chem 277(47):45572–45578

    Article  CAS  PubMed  Google Scholar 

  • Petersen J, Montserrat V, Mujico JR, Loh KL, Beringer DX, Van Lummel M, Thompson A, Mearin ML, Schweizer J, Kooy-Winkelaar Y (2014) T-cell receptor recognition of HLA-DQ2–gliadin complexes associated with celiac disease. Nat Struct Mol Biol 21(5):480

    Article  CAS  PubMed  Google Scholar 

  • Rahaman T, Vasiljevic T, Ramchandran L (2016) Shear, heat and pH induced conformational changes of wheat gluten – Impact on antigenicity. Food Chem 196:180–188

    Article  CAS  PubMed  Google Scholar 

  • Stănciuc N, Banu I, Bolea C, Patraşcu L, Aprodu I (2018) Structural and antigenic properties of thermally treated gluten proteins. Food Chem 267:43–51

    Article  PubMed  Google Scholar 

  • Sun F, Xie X, Zhang Y, Duan J, Ma M, Wang Y, Qiu D, Lu X, Yang G, He G (2020) Effects of cold jet atmospheric pressure plasma on the structural characteristics and immunoreactivity of celiac-toxic peptides and wheat storage proteins. Int J Mol Sci 21(3):1012

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Taddei P, Zanna N, Tozzi S (2013) Raman characterization of the interactions between gliadins and anthocyanins. J Raman Spectrosc 44(10):1435–1439

    Article  CAS  Google Scholar 

  • Tatham AS, Marsh MN, Wieser H, Shewry PR (1990) Conformational studies of peptides corresponding to the coeliac-activating regions of wheat α-gliadin. Biochem J 270(2):313–318

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Wang Q, Tang Y, Yang Y, Zhao J, Zhang Y, Li L, Wang Q, Ming J (2020) Interaction between wheat gliadin and quercetin under different pH conditions analyzed by multi-spectroscopy methods. Spectrochim Acta A Mol Biomol Spectrosc 229:117937

    Article  CAS  PubMed  Google Scholar 

  • Watson HG, Vanderputten D, Van Landschoot A, Decloedt AI (2019) Applicability of different brewhouse technologies and gluten-minimization treatments for the production of gluten-free (barley) malt beers: Pilot- to industrial-scale. J Food Eng 245:33–42

    Article  CAS  Google Scholar 

  • Widyarani SYW, Ratnaningsih E, Sanders JPMBruins ME, (2016) Production of hydrophobic amino acids from biobased resources: wheat gluten and rubber seed proteins. Appl Microbiol Biotechnol 100(18):7909–7920

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Wieser H (2007) Chemistry of gluten proteins. Food Microbiol 24(2):115–119

    Article  CAS  PubMed  Google Scholar 

  • Zhang R, Zhu M, Deng C, Shi X, Deng Y, Ma J, Liu H, Chen P (2018) Kinetic Analysis of Methylene Blue Degradation by Hydrocavitation. Ind Water Treat 38(6):31–34

    Google Scholar 

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Acknowledgements

The study described in this report was carried out by the Bioengineering Laboratory, Hainan University.

Funding

This study was financially supported by the Natural Science Foundation of Hainan Province of China (No. 321MS0766).

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Authors and Affiliations

  1. Department of Bioengineering, College of Life Sciences, Hainan University, Renmin Avenue NO: 160, Haikou, 570228, China

    Junyu Yu, Shida Xie & Dongsheng Yang

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  1. Junyu Yu
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  2. Shida Xie
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  3. Dongsheng Yang
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Contributions

Dongsheng Yang designed the study. Junyu Yu and Shida Xie collected data and interpreted the results. Junyu Yu drafted the manuscript.

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Correspondence to Dongsheng Yang.

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The Changes induced by hydrodynamic cavitation treatment in wheat gliadin and celiac-toxic peptides.

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Yu, J., Xie, S. & Yang, D. The changes induced by hydrodynamic cavitation treatment in wheat gliadin and celiac-toxic peptides. J Food Sci Technol (2024). https://doi.org/10.1007/s13197-024-05973-7

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  • DOI: https://doi.org/10.1007/s13197-024-05973-7

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