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PubMed · 10995272

Functional changes in beta-lactoglobulin upon conjugation with carboxymethyl cyclodextrin.

M Hattori·Y Okada·K Takahashi
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Abstract

Bovine beta-lactoglobulin-carboxymethyl cyclodextrin (beta-LG-CMCyD) conjugate was prepared using water-soluble carbodiimide, in an effort to improve the functional properties of the protein. The molar ratio of beta-LG to CMCyD in the conjugate was 1:2. The isoelectric point of the conjugate was 4.1-5.8. Spectroscopic studies indicated that the global conformation of the conjugate was similar to that of native beta-LG. Structural analyses with monoclonal antibodies indicated that there was a conformational change around (15)Val-(29)Ile (beta-sheet). The denaturation temperature of the conjugate was about 77 degrees C, which is about 4 degrees C higher than that of native beta-LG. The beta-LG-CMCyD conjugate maintained retinol-binding activity as strong as that of beta-LG. The emulsifying activity of beta-LG was much improved and the antioxidative activity of beta-LG was maintained after conjugation with CMCyD.

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AntioxidantsChromatography, GelCyclodextrinsLactoglobulinsProtein ConformationJournal ArticleResearch Support, Non-U.S. Gov't

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M Hattori, Y Okada, K Takahashi. 2000. Functional changes in beta-lactoglobulin upon conjugation with carboxymethyl cyclodextrin.. https://doi.org/10.1021/jf000204z

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