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Protein precipitation behaviour of condensed tannins from Lotus pedunculatus and Trifolium repens with different mean degrees of polymerization

Zeller, W. E., Sullivan, M. L., Mueller-Harvey, I., Grabber, J. H., Ramsay, A., Drake, C. and Brown, R. H. (2015) Protein precipitation behaviour of condensed tannins from Lotus pedunculatus and Trifolium repens with different mean degrees of polymerization. Journal of Agricultural and Food Chemistry, 63 (4). pp. 1160-1168. ISSN 0021-8561

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To link to this item DOI: 10.1021/jf504715p

Abstract/Summary

The precipitation of bovine serum albumin (BSA), lysozyme (LYS) and alfalfa leaf protein (ALF) by two large- and two medium-sized condensed tannin (CT) fractions of similar flavan-3-ol subunit composition is described. CT fractions isolated from white clover flowers and big trefoil leaves exhibited high purity profiles by 1D/2D NMR and purities >90% (determined by thiolysis). At pH 6.5, large CTs with a mean degree of polymerization (mDP) of ~18 exhibited similar protein precipitation behaviors and were significantly more effective than medium CTs (mDP ~9). Medium CTs exhibited similar capacities to precipitate ALF or BSA, but showed small but significant differences in their capacity to precipitate LYS. All CTs precipitated ALF more effectively than BSA or LYS. Aggregation of CT-protein complexes likely aided precipitation of ALF and BSA, but not LYS. This study, one of the first to use CTs of confirmed high purity, demonstrates that mDP of CTs influences protein precipitation efficacy.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Agriculture, Policy and Development > Food Production and Quality Division > Animal, Dairy and Food Chain Sciences (ADFCS)
ID Code:38988
Uncontrolled Keywords:condensed tannin; proanthocyanidin; protein precipitation; tannin−protein complexes; nuclear magnetic resonance spectroscopy; NMR; thiolysis
Publisher:American Chemical Society

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