Co-fermented cow milk protein by Lactobacillus helveticus KLDS 1.8701 and Lactobacillus plantarum KLDS 1.0386 attenuates its allergic immune response in Balb/c mice

Abstract

Milk protein is one of the major food allergens. As an effective processing method, fermentation may reduce the potential allergenicity of allergens. This study aimed to evaluate the therapeutic potential of co-fermented milk protein using Lactobacillus helveticus KLDS 1.8701 and Lactobacillus plantarum KLDS 1.0386 in cow milk protein allergy (CMPA) management. This study determined the secondary and tertiary structures of the fermented versus unfermented proteins by Fourier-transform infrared spectroscopy and surface hydrophobicity to evaluate its conformational changes. Our results showed that different fermentation methods have significantly altered the conformational structures of the cow milk protein, especially the tertiary structure. Further, the potential allergenicity of the fermented cow milk protein was assessed in Balb/c mice, and mice treated with the unfermented milk and phosphate-buffered saline were used as a control. We observed a significant reduction in allergenicity via the results of the spleen index, serum total IgE, specific IgE, histamine, and mouse mast cell protease 1 in the mice treated with the co-fermented milk protein. In addition, we analyzed the cytokines and transcription factors expression levels of spleen and jejunum and confirmed that co-fermentation could effectively reduce the sensitization of cow milk protein by regulating the imbalance of T helper (Th1/Th2 and Treg/Th17). This study suggested that changes of conformational structure could reduce the potential sensitization of cow milk protein; thus, fermentation may be a promising strategy for developing a method of hypoallergenic dairy products.

Raw milk kefir: microbiota, bioactive peptides, and immune modulation

“…Then IgE specifically binds to a high-affinity Fc receptor on the surface of mast cells or basophils that binds to allergen epitopes and triggers the release of inflammatory mediators and as a result the induction of food allergic symptoms. Although the effects of milk fermentation have been studied (60)(61)(62), only one study describes kefir related effects on food sensitisation. Hong et al showed suppression of IgE production and modulation of the T-cell compartment in LAB, Lactobacillus kefiranofaciens M1 treated mice (63).…”

Raw milk kefir: microbiota, bioactive peptides, and immune modulation

“…Then IgE specifically binds to a high-affinity Fc receptor on the surface of mast cells or basophils that binds to allergen epitopes and triggers the release of inflammatory mediators and as a result the induction of food allergic symptoms. Although the effects of milk fermentation have been studied, [65][66][67] only one study describes kefir related effects on food sensitisation. Hong et al showed suppression of IgE production and modulation of the T-cell compartment in LAB, Lactobacillus kefiranofaciens M1 treated mice.…”

Effect of lactic acid bacteria fermentation on cow milk allergenicity and antigenicity: A review

“…salivarius strain 1351 in a ratio of 1:1 (Kleber et al, 2006) was found to have a synergistic effect of β-Lg antigenicity reduction. Zhao et al (2022) evaluated the potential allergenicity of cow milk protein co-fermented by L. helveticus KLDS 1.8701 and L. plantarum KLDS 1.0386 and found that the conformational structure of milk proteins changed after fermentation, especially the tertiary structure. Therefore, the conformational structure of cow milk proteins may be closely related to their potential allergenicity.…”

“…In BALB/c mice fed a mixture of four probiotics ( B. lactis , L. casei , L. rhamnosus , and L. plantarum ), the differentiation of Th1 and Treg cells in MLN and spleen tissues was elevated, and whey protein‐induced allergic reactions were reduced (Kim et al., 2018). Co‐fermentation of L. helveticus KLDS 1.8701 and L. plantarum KLDS 1.0386 was effective in reducing milk protein allergic reactions by regulating imbalances of Th1/Th2 and of Treg/Th17 (Zhao et al., 2022). In mice models, the hydrolysis of β‐Lg by L. delbrueckii subsp.…”