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Food and Agricultural Immunology Volume 24, 2013 - Issue 3
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ARTICLES

Reduced allergenicity of β-lactoglobulin in vitro by tea catechins binding

Xuli WuCollege of Light Industry and Food Science, South China University of Technology, Guangzhou510642, Guangdong Province, PR China;School of Medicine, Shenzhen University, Shenzhen518060, Guangdong Province, PR China
,
Xiaojun ZhongSchool of Medicine, Shenzhen University, Shenzhen518060, Guangdong Province, PR China
,
Meixia LiuCollege of Chemistry and Chemistry Engineering, Shenzhen University, Shenzhen518060, Guangdong Province, PR China
,
Lixin XiaSchool of Medicine, Shenzhen University, Shenzhen518060, Guangdong Province, PR China
,
Kaiqian FengSchool of Medicine, Shenzhen University, Shenzhen518060, Guangdong Province, PR China
,
Hui WuCollege of Light Industry and Food Science, South China University of Technology, Guangzhou510642, Guangdong Province, PR ChinaCorrespondence[email protected]
&
Zhigang LiuSchool of Medicine, Shenzhen University, Shenzhen518060, Guangdong Province, PR China
 show all
Pages 305-313 | Received 06 Sep 2011, Accepted 10 Apr 2012, Published online: 14 May 2012

Figures & data

Figure 1. Spectroscopic analysis of the βLG–catechin complex. (A): intrinsic; (B) CD spectra.
Figure 1. Spectroscopic analysis of the βLG–catechin complex. (A): intrinsic; (B) CD spectra.
Figure 2. Retinol-binding activity of the βLG–catechin complex: (•): βLG; (Δ): βLG-catechin.
Figure 2. Retinol-binding activity of the βLG–catechin complex: (•): βLG; (Δ): βLG-catechin.
Figure 3. Indirect ELISA. Inhibition of the bind of polyclonal anti-βLG IgG (A) and polyclonal anti-βLG IgE (B) to immobilised βLG–catechin complex. (•): βLG; (○): βLG-catechin.
Figure 3. Indirect ELISA. Inhibition of the bind of polyclonal anti-βLG IgG (A) and polyclonal anti-βLG IgE (B) to immobilised βLG–catechin complex. (•): βLG; (○): βLG-catechin.

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