AI Article Synopsis
- The study examines how two large and two medium-sized condensed tannin (CT) fractions impact the precipitation of different proteins: bovine serum albumin (BSA), lysozyme (LYS), and alfalfa leaf protein (ALF), revealing the effects of CT size and composition.
- High-purity CT fractions from white clover and big trefoil were analyzed, with large CTs (mDP ∼18) being more effective at precipitating proteins compared to medium CTs (mDP ∼9).
- Results indicate that while all CTs preferentially precipitate ALF over BSA and LYS, the degree of polymerization of the CTs plays a significant role in their precipitation ability, highlighting
Article Abstract
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 the mDP of CTs influences protein precipitation efficacy.
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| http://dx.doi.org/10.1021/jf504715p | DOI Listing |
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