Effects of high hydrostatic pressure on the structure and potential allergenicity of the major allergen bovine β-lactoglobulin

Meng, Xuanyi; Bai, Yuxin; Gao, Jinyan; Li, Xin

doi:10.1016/j.foodchem.2016.09.153

Cited by 88 publications

(40 citation statements)

References 36 publications

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“…, no noticeable differences in SDS‐PAGE were observed among lane A, lane B and lane C and their molecular weights were about 18.4 kDa, suggesting that the primary structure of β‐LG remained stable after DHPM treatment from 0.1 to 160 MPa. Some published studies suggested that the primary structure of some proteins kept stable and was not affected by physical processing such as HHP and DHPM (Liu et al ., ; Meng et al ., ). The molecular weight of 0.1 DM‐β‐LG‐VD had scarcely significant change compared to DM‐β‐LG because β‐LG can resist gastrointestinal digestion (Kleber et al ., ).…”

Section: Resultsmentioning

confidence: 97%

The enhancement of gastrointestinal digestibility of β‐LG by dynamic high‐pressure microfluidization to reduce its antigenicity

Chen

Hong

Zhong

et al. 2018

Int J of Food Sci Tech

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Dynamic high-pressure microfluidization (DHPM) can increase the antigenicity of b-lactoglobulin (b-LG) in previous researches. We observed in this study that the antigenicity of DHPM-modified b-LG at pressures of 0.1, 80 and 160 MPa after in vitro digestion declined from 13.41 to 12.27 and 7.19 lg mL À1 , gradually. The enhancement of gastrointestinal digestibility of b-LG was related to the aggregation state and conformational changes induced by DHPM and was reflected by the electrophoretic bands of low molecular weight (5 and 10 kDa) shown in electrophoresis, the reduction of particle size, the generation of smaller peptide fragments (m/z 837.444, 955.492 and 1215.616) detected by mass spectrum and the increase in surface hydrophobicity. These changes contributed to the decrease in antigenicity. Simultaneously, a schematic diagram was proposed to demonstrate the conceivable mechanism of antigenicity changes of modified b-LG after in vitro digestion.Digests reduce antigenicity of modified b-LG H. Chen et al.

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Section: Resultsmentioning

confidence: 97%

The enhancement of gastrointestinal digestibility of β‐LG by dynamic high‐pressure microfluidization to reduce its antigenicity

Chen

Hong

Zhong

et al. 2018

Int J of Food Sci Tech

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“…Antigenicity of all β-LG samples were determined by indirect competitive ELISA with polyclonal IgG antibodies of rabbit, which are monospecific against β-LG (Zhong et al, 2014;Meng et al, 2017). Then 2.5 µg/mL antigen in 0.05 M carbonate-bicarbonate coating buffer was used to coat individual wells (100 µL/ well) of a 96-well microplate (flat-bottomed; Costar, Corning, Corning, NY) at 4°C overnight.…”

Section: Antigenicity Analysismentioning

confidence: 99%

Antigenicity of β-lactoglobulin reduced by combining with oleic acid during dynamic high-pressure microfluidization: Multi-spectroscopy and molecule dynamics simulation analysis

Zhong

et al. 2019

Journal of Dairy Science

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Some food components can modulate the antigenicity of β-lactoglobulin (β-LG). This study investigated the role of oleic acid (OA) in reducing the antigenicity of β-LG. The results indicate the antigenicity of β-LG gradually decreased from 15 (sample with no OA) to 9.86, 7.51, and 6.01 µg/mL when interacting with OA during dynamic high-pressure microfluidization treatment at 0.1, 80, and 160 MPa. Although binding sites (n) of β-LG combined with OA at 0.1, 80, and 160 MPa decreased from 0.79 to 0.5 and 0.66, β-LG had a higher binding affinity (K a) to OA than that of untreated β-LG. The values of K a for β-LG/OA at 0.1, 80, and 160 MPa were 5.51 × 10 6 , 17.43 × 10 6 , and 49.75 × 10 6 M −1 , respectively. The molecule dynamic simulation showed that the OA molecules located at both β-barrel (site 1) interacted with Lys60, Glu62, and Lys69 and outer surface site 2 consisting of Tyr20, Tyr42, Ser21, Glu157, and His161. Additionally, when binding with OA during the dynamic high-pressure microfluidization treatment, the conformation of β-LG changed, reflected by the decrease of fluorescence intensity and total sulfhydryl group content, the increase of surface sulfhydryl group content, and secondary structure changes of β-LG. These results deduce that some epitopes may be masked by OA or modified by the conformational changes, resulting in the decline of antigenicity of β-LG molecules.

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“…In addition to the US treatment, HHP treatment increased the G′ and G″ in both cooling and heating periods of fish gelatin. Increase in both G′ and G″ values of the fish gelatin might be due to the higher degree of unfolding after pressurisation which enabled the gelation process (Meng et al , ). This increasing trend among treated samples indicated gel setting and also resulted in increase in the strength of the gels.…”

Section: Resultsmentioning

confidence: 99%

Improving the physical properties of fish gelatin by high hydrostatic pressure (HHP) and ultrasonication (US)

Sezer

Okur

Alpas

2020

Int J of Food Sci Tech

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Summary In this study, it was aimed to improve the physical properties of fish gelatin by using high hydrostatic pressure (HHP) and ultrasonication (US). Gelatin solutions were exposed to different pressures and ultrasonication separately and gelled afterwards. The physicochemical measurements based on gel strength, turbidity and rheology experiments showed that HHP treatment on fish and bovine gelatin stabilized the gelatin network by organising the structure and reducing the free volume. Both processing methods (HHP and US) increased the gel strength significantly (P < 0.05) compared with non‐treated samples. Fourier‐transform infrared spectroscopy (FTIR) results indicated that conformations of amino acids changed after the treatments. Furthermore, US treatment was shown to destroy the gelatin network, change the gelation mechanism and decreased the degree of aggregation. Both treatments improved the gel characteristics as gel strength, gelling and melting temperatures of the fish gelatin. At the end, the best combination for fish gelatin among HHP and US treatments was found as 400 MPa–10 °C–15 min pressurisation.

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Effects of high hydrostatic pressure on the structure and potential allergenicity of the major allergen bovine β-lactoglobulin

Cited by 88 publications

References 36 publications

The enhancement of gastrointestinal digestibility of β‐LG by dynamic high‐pressure microfluidization to reduce its antigenicity

The enhancement of gastrointestinal digestibility of β‐LG by dynamic high‐pressure microfluidization to reduce its antigenicity

Antigenicity of β-lactoglobulin reduced by combining with oleic acid during dynamic high-pressure microfluidization: Multi-spectroscopy and molecule dynamics simulation analysis

Improving the physical properties of fish gelatin by high hydrostatic pressure (HHP) and ultrasonication (US)

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