Structural changes in emulsion-bound bovine beta-lactoglobulin affect its proteolysis and immunoreactivity
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- 作者：Mauro Marengoa ; Matteo Miriania ; Pasquale Ferrantib ; Francesco Bonomia ; Stefania Iamettia ; stefania.iametti@unimi.it" class="auth_mail" title="E-mail the corresponding author ; Alberto Barbirolia
- 关键词：BLG ; beta-lactoglobulin ; NP ; nanoparticles ; DTNB ; 5 ; 5&prime ; -dithiobis-2-nitrobenzoic acid ; ELISA ; enzyme-linked immunoassay ; MALDI-TOF ; matrix-assisted laser desorption ionization time-of-flight mass spectrometry
- 刊名：Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- 出版年：2016
- 出版时间：July 2016
- 年：2016
- 卷：1864
- 期：7
- 页码：805-813
- 全文大小：635 K
文摘
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Beta-lactoglobulin (BLG) is an allergenic, rigid, proteolysis-resistant, food protein.
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Adsorption on oil droplets modifies BLG structure increasing its immunoreactivity.
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Proteolysis of emulsion-bound BLG did not decrease the immunoreactivity.
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A structural analysis of emulsion-bound proteins was provided.