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Effect of acid and in vitro digestion on conformation and IgE-binding capacity of major oyster allergen Cra g 1 (tropomyosin).
Zhang, Jiangtao; Liu, Wenying; Fang, Lei; Gu, Ruizeng; Lu, Jun; Li, Guoming.
Afiliação
  • Zhang J; Beijing Engineering Research Center of Protein & Functional Peptides, China National Research Institute of Food and Fermentation Industries, Beijing 100015, PR China.
  • Liu W; Beijing Engineering Research Center of Protein & Functional Peptides, China National Research Institute of Food and Fermentation Industries, Beijing 100015, PR China.
  • Fang L; Beijing Engineering Research Center of Protein & Functional Peptides, China National Research Institute of Food and Fermentation Industries, Beijing 100015, PR China.
  • Gu R; Beijing Engineering Research Center of Protein & Functional Peptides, China National Research Institute of Food and Fermentation Industries, Beijing 100015, PR China.
  • Lu J; Beijing Engineering Research Center of Protein & Functional Peptides, China National Research Institute of Food and Fermentation Industries, Beijing 100015, PR China. Electronic address: Johnljsmith@163.com.
  • Li G; Beijing Engineering Research Center of Protein & Functional Peptides, China National Research Institute of Food and Fermentation Industries, Beijing 100015, PR China. Electronic address: 297756628@qq.com.
Allergol Immunopathol (Madr) ; 48(1): 26-33, 2020.
Article em En | MEDLINE | ID: mdl-31623945
ABSTRACT
INTRODUCTION AND

OBJECTIVES:

The production and consumption of oysters is increasing annually because it can provide essential nutrients and benefit for human health, leading to frequent occurrence of severe allergic reactions observed in sensitized individuals. The aim of the present study was to investigate the effects of acid and protease treatment on the conformation and IgE-binding capacity of recombinant Crassostrea gigas tropomyosin (Cra g 1).

RESULTS:

Under acidic conditions, Cra g 1 did not undergo degradation, however, the changes obvious in the intensity of CD signal and ANS-binding fluorescence were observed, which was associated with a decrease in antibody reactivity. In simulated gastrointestinal fluid (SGF) and simulated intestinal fluid (SIF) digestion system, acid-treated Cra g 1 was relatively resistant to digestion, but the degradative patterns were very different. Moreover, owing to alterations of secondary structure and hydrophobic surface of the protein during digestive processing, antigenicity of acid-induced Cra g 1 reduced in SGF while it increased significantly in SIF.

CONCLUSION:

To our knowledge, this is the first study reporting that antigenicity of acid-treated oyster tropomyosin increased after SIF digestion. These results revealed that treatment with acid and pepsin, rather than trypsin, was an effective way of reducing IgE-binding capacity of tropomyosin from oyster.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Tropomiosina / Ácidos / Imunoglobulina E / Alérgenos Limite: Humans Idioma: En Revista: Allergol Immunopathol (Madr) Ano de publicação: 2020 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Tropomiosina / Ácidos / Imunoglobulina E / Alérgenos Limite: Humans Idioma: En Revista: Allergol Immunopathol (Madr) Ano de publicação: 2020 Tipo de documento: Article