WU Xu Li; WANG Wen Pu; XIA Li Xin; XU Hong; WU Hui; LIU Zhi Gang

doi:10.3967/0895-3988.2012.03.012

In Vitro Refolding Process of Bovine Allergen β-lactoglobulin by Multispectroscopic Method

WU Xu Li, WANG Wen Pu, XIA Li Xin, XU Hong, WU Hui, LIU Zhi Gang

文章导航 > Biomedical and Environmental Sciences > 2012 > 25(3): 334-339

WU Xu Li, WANG Wen Pu, XIA Li Xin, XU Hong, WU Hui, LIU Zhi Gang. In Vitro Refolding Process of Bovine Allergen β-lactoglobulin by Multispectroscopic Method[J]. Biomedical and Environmental Sciences, 2012, 25(3): 334-339. doi: 10.3967/0895-3988.2012.03.012

Citation:

WU Xu Li, WANG Wen Pu, XIA Li Xin, XU Hong, WU Hui, LIU Zhi Gang. In Vitro Refolding Process of Bovine Allergen β-lactoglobulin by Multispectroscopic Method[J]. Biomedical and Environmental Sciences, 2012, 25(3): 334-339. doi: 10.3967/0895-3988.2012.03.012

doi: 10.3967/0895-3988.2012.03.012

基金项目: This research was supported by the Natural Science Foundation of China(30871752)%the High-tech Industrialization Funding of Guangdong Province(2009B011300010)

In Vitro Refolding Process of Bovine Allergen β-lactoglobulin by Multispectroscopic Method

College of Light Industry and Food Science, South China University of Technology, Guangzhou 510642,Guangdong, China; School of Medicine, Shenzhen University, Shenzhen 518060, Guangdong, China
School of Medicine, Shenzhen University, Shenzhen 518060, Guangdong, China
College of Chemistry and Chemical Engineering, Shenzhen University, Shenzhen 518060, Guangdong, China
College of Light Industry and Food Science, South China University of Technology, Guangzhou 510642,Guangdong, China

Funds: This research was supported by the Natural Science Foundation of China(30871752)%the High-tech Industrialization Funding of Guangdong Province(2009B011300010)

摘要: Objective To characterize the relationship between the refolding process of recombinant bovine β-lactoglobulin and its immunoreactivity for clinical purposes.To establish a spectral method which examine the extent of recombinant allergen renaturation.Methods The refolding process of recombinant bovine β-lactoglobulin was investigated by using circular dichroism,fluorescence and synchronous fluorescence spectra.IgE-binding capacity of recombinant protein was analyzed by ELISA.In addition,bioinformatic methods were used to explain the spectral characteristics and analyze the relationship between the conformational changes and the immunoreactivity of the protein during renaturation in vitro.Results Renaturation of recombinant bovine β-lactoglobulin resulted in a more compact structure resembling the natural counterpart with stronger IgE-binding capacity.Conclusion The degree of protein renaturation correlated with the IgE-binding capacity of the protein.Results from this study may be of help for food allergy therapy and development of vaccination in the future.
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Abstract: Objective To characterize the relationship between the refolding process of recombinant bovine β-lactoglobulin and its immunoreactivity for clinical purposes.To establish a spectral method which examine the extent of recombinant allergen renaturation.Methods The refolding process of recombinant bovine β-lactoglobulin was investigated by using circular dichroism,fluorescence and synchronous fluorescence spectra.IgE-binding capacity of recombinant protein was analyzed by ELISA.In addition,bioinformatic methods were used to explain the spectral characteristics and analyze the relationship between the conformational changes and the immunoreactivity of the protein during renaturation in vitro.Results Renaturation of recombinant bovine β-lactoglobulin resulted in a more compact structure resembling the natural counterpart with stronger IgE-binding capacity.Conclusion The degree of protein renaturation correlated with the IgE-binding capacity of the protein.Results from this study may be of help for food allergy therapy and development of vaccination in the future.
- Food allergen /
- β-Lactoglobulin /
- Protein folding /
- Spectroscopy /
- Immunoreactivity

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In Vitro Refolding Process of Bovine Allergen β-lactoglobulin by Multispectroscopic Method

doi: 10.3967/0895-3988.2012.03.012

基金项目: This research was supported by the Natural Science Foundation of China(30871752)%the High-tech Industrialization Funding of Guangdong Province(2009B011300010)

刊出日期: 2012-06-20

关键词:

摘要: Objective To characterize the relationship between the refolding process of recombinant bovine β-lactoglobulin and its immunoreactivity for clinical purposes.To establish a spectral method which examine the extent of recombinant allergen renaturation.Methods The refolding process of recombinant bovine β-lactoglobulin was investigated by using circular dichroism,fluorescence and synchronous fluorescence spectra.IgE-binding capacity of recombinant protein was analyzed by ELISA.In addition,bioinformatic methods were used to explain the spectral characteristics and analyze the relationship between the conformational changes and the immunoreactivity of the protein during renaturation in vitro.Results Renaturation of recombinant bovine β-lactoglobulin resulted in a more compact structure resembling the natural counterpart with stronger IgE-binding capacity.Conclusion The degree of protein renaturation correlated with the IgE-binding capacity of the protein.Results from this study may be of help for food allergy therapy and development of vaccination in the future.

English Abstract

In Vitro Refolding Process of Bovine Allergen β-lactoglobulin by Multispectroscopic Method

College of Light Industry and Food Science, South China University of Technology, Guangzhou 510642,Guangdong, China; School of Medicine, Shenzhen University, Shenzhen 518060, Guangdong, China

School of Medicine, Shenzhen University, Shenzhen 518060, Guangdong, China

College of Chemistry and Chemical Engineering, Shenzhen University, Shenzhen 518060, Guangdong, China

College of Light Industry and Food Science, South China University of Technology, Guangzhou 510642,Guangdong, China

Funds: This research was supported by the Natural Science Foundation of China(30871752)%the High-tech Industrialization Funding of Guangdong Province(2009B011300010)

Publish Date: 2012-06-20

Keywords:

Abstract: Objective To characterize the relationship between the refolding process of recombinant bovine β-lactoglobulin and its immunoreactivity for clinical purposes.To establish a spectral method which examine the extent of recombinant allergen renaturation.Methods The refolding process of recombinant bovine β-lactoglobulin was investigated by using circular dichroism,fluorescence and synchronous fluorescence spectra.IgE-binding capacity of recombinant protein was analyzed by ELISA.In addition,bioinformatic methods were used to explain the spectral characteristics and analyze the relationship between the conformational changes and the immunoreactivity of the protein during renaturation in vitro.Results Renaturation of recombinant bovine β-lactoglobulin resulted in a more compact structure resembling the natural counterpart with stronger IgE-binding capacity.Conclusion The degree of protein renaturation correlated with the IgE-binding capacity of the protein.Results from this study may be of help for food allergy therapy and development of vaccination in the future.

Citation: