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Research Article | Open Access

Efficient reduction of β-lactoglobulin allergenicity in milk using Clostridium tyrobutyricum Z816

Qianru Zhaoa,b, Yuwei Wangb, Zhengming Zhub, Quanyu Zhaoc, Liying Zhud( ), Ling Jiangb( )
College of Biotechnology and Pharmaceutical Engineering, State Key Laboratory of Materials-Oriented Chemical Engineering, Nanjing Tech University, Nanjing 210009, China
College of Food Science and Light Industry, Nanjing Tech University, Nanjing 210009, China
School of Pharmaceutical Sciences, Nanjing Tech University, Nanjing 211816, China
School of Chemistry and Molecular Engineering, Nanjing Tech University, Nanjing 210009, China

Peer review under responsibility of KeAi Communications Co., Ltd.

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Abstract

Milk allergy is one of the most common food allergies, affecting 6% of young children, and β-lactoglobulin (β-LG) is the main milk allergen. Clostridium tyrobutyricum Z816 was selected for the degradation of β-LG, which was successfully reduced by about 90% using permeabilized bacteria under the optimized conditions. The hydrolyzed peptides were identified by liquid chromatography-tandem mass spectrometry (LC-MS/MS) and analyzed by molecular modeling, which indicated that C. tyrobutyricum Z816 could effectively degrade the antigenic epitopes of β-LG. Finally, the concentration and digestibility of β-LG in actual samples was quantified using enzyme-linked immunosorbent assay (ELISA) and gastrointestinal digestion simulation experiments. The results showed more than 92% of β-LG in actual samples was hydrolyzed, and the gastric and total digestibility of whey protein isolate (WPI) was improved by 85.96% and 64.51%, respectively. Therefore, C. tyrobutyricum Z816 offers an effective method to degrade β-LG and reduce the occurrence of milk allergies, which has great significance for the development of hypoallergenic dairy products.

Keywords

Milk allergyβ-LactoglobulinClostridium tyrobutyricumPermeabilized bacteria

References

[1]

A. Fiocchi, J. Brozek, H. Schünemann, et al., World Allergy Organization (WAO) diagnosis and rationale for action against cow's milk allergy (DRACMA) guidelines, Pediatr. Allergy Immunol. 3 (2010) 57-161. http://doi.org/10.1111/j.1399-3038.2010.01068.x.
Crossref Google Scholar
[2]

M. Kondo, H. Kaneko, T. Fukao, et al., The response of bovine beta-lactoglobulin-specific T-cell clones to single amino acid substitution of T-cell core epitope, Pediatr. Allergy Immunol. 19 (2008) 592-598. http://doi.org/10.1111/j.1399-3038.2007.00704.x.
Crossref Google Scholar
[3]

C. Keet, Recognition and management of food-induced anaphylaxis, Pediatr. Clin. North Am. 58 (2011) 377-388. http://doi.org/10.1016/j.pcl.2011.02.006.
Crossref Google Scholar
[4]

M. Albrecht, Y. Kuhne, B.K. Ballmer-Weber, et al., Relevance of IgE binding to short peptides for the allergenic activity of food allergens, J. Allergy Clin. Immunol. 124 (2009) 328-336. http://doi.org/10.1016/j.jaci.2009.05.031.
Crossref Google Scholar
[5]

K.C.M. Verhoeckx, Y.M. Vissers, J.L. Baumert, et al., Food processing and allergenicity, Food Chem. Toxicol. 80 (2015) 223-240. http://doi.org/10.1016/j.fct.2015.03.005.
Crossref Google Scholar
[6]

B.I. Nwaru, L. Hickstein, S.S. Panesar, et al., Prevalence of common food allergies in Europe: a systematic review and meta-analysis, Allergy 69 (2014) 992-1007. http://doi.org/10.1111/all.12423.
Crossref Google Scholar
[7]

J. Wang, Management of the patient with multiple food allergies, Curr. Allergy Asthma Rep. 10 (2010) 271-277. http://doi.org/10.1007/s11882-010-0116-0.
Crossref Google Scholar
[8]

P. Dong, J.J. Feng, D.Y. Yan, et al., Early-life gut microbiome and cow's milk allergy-a prospective case-control 6-month follow-up study, Saudi J. Biol. Sci. 25 (2018) 875-880. http://doi.org/10.1016/j.sjbs.2017.11.051.
Crossref Google Scholar
[9]

V. Schichter-Konfino, M. Almog, E. Bamberger, et al., The significance of allergic contact urticaria to milk in children with cow's milk allergy, Pediatr. Allergy Immunol. 26 (2015) 218-222. http://doi.org/10.1111/pai.12375.
Crossref Google Scholar
[10]

J.M. Skripak, E.C. Matsui, K. Mudd, et al., The natural history of IgE-mediated cow's milk allergy, J. Allergy Clin. Immunol. 120 (2007) 1172-1177. http://doi.org/10.1016/j.jaci.2007.08.023.
Crossref Google Scholar
[11]

A. Høst, Frequency of cow's milk allergy in childhood, Ann. Allergy Asthma Immunol. 89 (2002) 33-37. http://doi.org/10.1016/s1081-1206(10)62120-5.
Crossref Google Scholar
[12]

S.L. Bavaro, E. De Angelis, S. Barni, et al., Modulation of milk allergenicity by baking milk in foods: a proteomic investigation, Nutrients 11 (2019) 1536. http://doi.org/10.3390/nu11071536.
Crossref Google Scholar
[13]

G. Docena, R. Fernandez, F. Chirdo, et al., Identification of casein as the major allergenic and antigenic protein of cow's milk, Allergy 51 (1996) 412-416. https://doi.org/10.1111/j.1398-9995.1996.tb04639.x.
Crossref Google Scholar
[14]

A. Maurmayr, A. Cecchinato, L. Grigoletto, et al., Detection and quantification of αS1-, αS2-, β-, κ-casein, α-lactalbumin, β-lactoglobulin and lactoferrin in bovine milk by reverse-phase high-performance liquid chromatography, Agriculturae Conspectus Scientificus 78 (2013) 201-205. https://hrcak.srce.hr/106905.
Google Scholar
[15]

F. Roth-Walter, L.F. Pacios, C. Gomez-Casado, et al., The major cow milk allergen Bos d 5 manipulates T-helper cells depending on its load with siderophore-bound iron, PLoS ONE 9 (2014) e104803. http://doi.org/10.1371/journal.pone.0104803.
Crossref Google Scholar
[16]

R.N. Pereira, R.M. Rodrigues, O.L. Ramos, et al., Electric field processing: novel perspectives on allergenicity of milk proteins, J. Agric. Food Chem. 66 (2018) 11227-11233. http://doi.org/10.1021/acs.jafc.8b03689.
Crossref Google Scholar
[17]

J.M. Lee, J.S. Yoon, S.A. Jeon, et al., Sensitization patterns of cow's milk and major components in young children with atopic dermatitis, Asia Pac. Allergy 3 (2013) 179-185. http://doi.org/10.5415/apallergy.2013.3.3.179.
Crossref Google Scholar
[18]

M. Pescuma, E.M. Hebert, T. Haertle, et al., Lactobacillus delbrueckii subsp. bulgaricus CRL 454 cleaves allergenic peptides of beta-lactoglobulin, Food Chem. 170 (2015) 407-414. http://doi.org/10.1016/j.foodchem.2014.08.086.
Crossref Google Scholar
[19]

I. Cerecedo, J. Zamora, W.G. Shreffler, et al., Mapping of the IgE and IgG4 sequential epitopes of milk allergens with a peptide microarray-based immunoassay, J. Allergy Clin. Immunol. 122 (2008) 589-594. http://doi.org/10.1016/j.jaci.2008.06.040.
Crossref Google Scholar
[20]

Z. Sun, M. Wang, S. Han, et al., Production of hypoallergenic milk from DNA-free beta-lactoglobulin (BLG) gene knockout cow using zinc-finger nucleases mRNA, Sci. Rep. 8 (2018) 1-11. http://doi.org/10.1038/s41598-018-32024-x.
Crossref Google Scholar
[21]

M. Pescuma, E.M. Hebert, H. Rabesona, et al., Proteolytic action of Lactobacillus delbrueckii subsp. bulgaricus CRL 656 reduces antigenic response to bovine beta-lactoglobulin, Food Chem. 127 (2011) 487-492. http://doi.org/10.1016/j.foodchem.2011.01.029.
Crossref Google Scholar
[22]

Q. Xu, J. Shi, M. Yao, et al., Effects of heat treatment on the antigenicity of four milk proteins in milk protein concentrates, Food Agr. Immunol. 27 (2015) 401-413. http://doi.org/10.1080/09540105.2015.1117059.
Crossref Google Scholar
[23]

F. Yuan, I. Ahmed, L. LÜ, et al., Impacts of glycation and transglutaminase-catalyzed glycosylation with glucosamine on the conformational structure and allergenicity of bovine beta-lactoglobulin, Food Funct. 9 (2018) 3944-3955. http://doi.org/10.1039/c8fo00909k.
Crossref Google Scholar
[24]

M. Zeece, T. Huppertzand, A. Kelly, Effect of high-pressure treatment on in-vitro digestibility of β-lactoglobulin, Innov. Food Sci. Emerg. Technol. 9 (2008) 62-69. http://doi.org/10.1016/j.ifset.2007.05.004.
Crossref Google Scholar
[25]

A.B. Martı́n-Diana, C. Janer, C. Peláez, et al., Development of a fermented goat's milk containing probiotic bacteria, Int. Dairy J. 13 (2003) 827-833. https://doi.org/10.1016/S0958-6946(03)00117-1.
Crossref Google Scholar
[26]

G. Bu, Y. Luo, Y. Zhang, et al., Effects of fermentation by lactic acid bacteria on the antigenicity of bovine whey proteins, J. Sci. Food Agric. 90 (2010) 2015-2020. http://doi.org/10.1002/jsfa.4046.
Crossref Google Scholar
[27]

A.M. De Leblanc, C. Matar, N. Leblanc, et al., Effects of milk fermented by Lactobacillus helveticus R389 on a murine breast cancer model, Breast Cancer Res. 7 (2005) 477-486. http://doi.org/10.1186/bcr1032.
Crossref Google Scholar
[28]

N. Kleber, U. Weyrichand, J. Hinrichs, Screening for lactic acid bacteria with potential to reduce antigenic response of β-lactoglobulin in bovine skim milk and sweet whey, Innov. Food Sci. Emerg. Technol. 7 (2006) 233-238. http://doi.org/10.1016/j.ifset.2005.12.005.
Crossref Google Scholar
[29]

C.E. Vargas Garcia, M. Petrova, I.J. Claes, et al., Piliation of Lactobacillus rhamnosus GG promotes adhesion, phagocytosis, and cytokine modulation in macrophages, Appl. Environ. Microbiol. 81 (2015) 2050-2062. http://doi.org/10.1128/AEM.03949-14.
Crossref Google Scholar
[30]

R. Berni Canani, N. Sangwan, A.T. Stefka, et al., Lactobacillus rhamnosus GG-supplemented formula expands butyrate-producing bacterial strains in food allergic infants, ISME J. 10 (2016) 742-750. http://doi.org/10.1038/ismej.2015.151.
Crossref Google Scholar
[31]

R. Berni Canani, F. de Filippis, R. Nocerino, et al., Gut microbiota composition and butyrate production in children affected by non-IgE-mediated cow's milk allergy, Sci. Rep. 8 (2018) 12500. http://doi.org/10.1038/s41598-018-30428-3.
Crossref Google Scholar
[32]

P.M. Smith, M.R. Howitt, N. Panikov, et al., The microbial metabolites, short-chain fatty acids, regulate colonic Treg cell homeostasis, Science 341 (2013) 569-573. http://doi.org/10.1126/science.1241165.
Crossref Google Scholar
[33]

S.M. Vindigni, E.K. Broussard, C.M. Surawicz, Alteration of the intestinal microbiome: fecal microbiota transplant and probiotics for Clostridium difficile and beyond, Expert Rev. Gastroenterol. Hepatol. 7 (2013) 615-628. http://doi.org/10.1586/17474124.2013.832501.
Crossref Google Scholar
[34]

X. Yan, L. Zhu, Y. Yu, et al., In-situ biocatalytic production of trehalose with autoinduction expression of trehalose synthase, J. Agric. Food Chem. 66 (2018) 1444-1451. http://doi.org/10.1021/acs.jafc.7b06031.
Crossref Google Scholar
[35]

L. Zhu, B. Shen, Z. Song, et al., Permeabilized TreS-expressing Bacillus subtilis cells decorated with glucose isomerase and a shell of ZIF-8 as a reusable biocatalyst for the coproduction of trehalose and fructose, J. Agric. Food Chem. 68 (2020) 4464-4472. http://doi.org/10.1021/acs.jafc.0c00971.
Crossref Google Scholar
[36]

P. Sáez-Plaza, T. Michałowski, M.J. Navas, et al., An overview of the Kjeldahl method of nitrogen determination. part I. early history, chemistry of the procedure, and titrimetric finish, Crit. Rev. Anal. Chem. 43 (2013) 178-223. http://doi.org/10.1080/10408347.2012.751786.
Crossref Google Scholar
[37]

T. Liu, L. Zhu, Z. Zhu, et al., Genome sequence analysis of Clostridium tyrobutyricum, a promising microbial host for human health and industrial applications, Curr. Microbiol. 77 (2020) 3685-3694. http://doi.org/10.1007/s00284-020-02175-0.
Crossref Google Scholar
[38]

R. Kazemi, A. Taheri-Kafrani, A. Motahari, et al., Allergenicity reduction of bovine milk β-lactoglobulin by proteolytic activity of Lactococcus lactis BMC12C and BMC19H isolated from Iranian dairy products, Int. J. Biol. Macromol. 112 (2018) 876-881. http://doi.org/10.1016/j.ijbiomac.2018.02.044.
Crossref Google Scholar
[39]

B. Wróblewska, L.H. Markiewicz, A.M. Szyc, et al., Lactobacillus casei LcY decreases milk protein immunoreactivity of fermented buttermilk but also contains IgE-reactive proteins, Food Res. Int. 83 (2016) 95-101. http://doi.org/10.1016/j.foodres.2016.02.016.
Crossref Google Scholar
[40]

V. Biscola, Y. Choiset, H. Rabesona, et al., Brazilian artisanal ripened cheeses as sources of proteolytic lactic acid bacteria capable of reducing cow milk allergy, J. Appl. Microbiol. 125 (2018) 564-574. http://doi.org/10.1111/jam.13779.
Crossref Google Scholar
[41]

S. Peyron, J. Mouécoucou, S. Frémont, et al., Effects of heat treatment and pectin addition on β-lactoglobulin allergenicity, J. Agric. Food Chem. 54 (2006) 5643-5650. http://doi.org/10.1021/jf053178j.
Crossref Google Scholar
[42]

I. Maier, V.M. Okun, F. Pittner, et al., Changes in peptic digestibility of bovine beta-lactoglobulin as a result of food processing studied by capillary electrophoresis and immunochemical methods, J. Chromatogr. B 841 (2006) 160-167. http://doi.org/10.1016/j.jchromb.2006.06.040.
Crossref Google Scholar
[43]

A. Koh, F. de Vadder, P. Kovatcheva-Datchary, et al., From dietary fiber to host physiology: short-chain fatty acids as key bacterial metabolites, Cell 165 (2016) 1332-1345. http://doi.org/10.1016/j.cell.2016.05.041.
Crossref Google Scholar
[44]

T. Hudcovic, J. Kolinska, J. Klepetar, et al., Protective effect of Clostridium tyrobutyricum in acute dextran sodium sulphate-induced colitis: differential regulation of tumour necrosis factor-alpha and interleukin-18 in BALB/c and severe combined immunodeficiency mice, Clin. Exp. Immunol. 167 (2012) 356-365. http://doi.org/10.1111/j.1365-2249.2011.04498.x.
Crossref Google Scholar
Food Science and Human Wellness
Volume 12 Issue 3,
May 2023
Pages 809-816
DOI: 10.1016/j.fshw.2022.09.017
Cite this article:
Zhao Q, Wang Y, Zhu Z, et al. Efficient reduction of β-lactoglobulin allergenicity in milk using Clostridium tyrobutyricum Z816. Food Science and Human Wellness, 2023, 12(3): 809-816. https://doi.org/10.1016/j.fshw.2022.09.017

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Received: 01 May 2021
Revised: 03 August 2021
Accepted: 11 October 2021
Published: 15 October 2022
© 2023 Beijing Academy of Food Sciences. Publishing services by Elsevier B.V. on behalf of KeAi Communications Co., Ltd.

This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
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