Skip to main content
ARS Home » Midwest Area » Madison, Wisconsin » U.S. Dairy Forage Research Center » Cell Wall Biology and Utilization Research » Research » Publications at this Location » Publication #312344

Research Project: Removing Limitations to the Efficient Utilization of Alfalfa and Other Forages in Dairy Production, New Bio-Products, and Bioenergy to...

Location: Cell Wall Biology and Utilization Research

Title: Impact by condensed tannins with different mean degrees of polymerization on protein precipitation

Author
item Zeller, Wayne
item Sullivan, Michael
item MUELLER-HARVEY, IRENE - University Of Reading
item Grabber, John
item RAMSAY, AINA - University Of Reading
item DRAKE, CHRIS - University Of Reading
item BROWN, RONALD - University Of Reading

Submitted to: American Chemical Society Abstracts
Publication Type: Abstract Only
Publication Acceptance Date: 12/19/2014
Publication Date: 3/23/2015
Citation: Zeller, W.E., Sullivan, M.L., Mueller-Harvey, I., Grabber, J.H., Ramsay, A., Drake, C., Brown, R.H. 2015. Impact by condensed tannins with different mean degrees of polymerization on protein precipitation [abstract]. 249th American Chemical Society Meeting, March 22-26, 2015, Denver, Colorado. Abstract No. AGFD 51.

Interpretive Summary:

Technical Abstract: Condensed tannins (CTs) isolated from white clover (Trifolium repens) flowers and big trefoil (Lotus pedunculatus) leaves were evaluated in precipitation studies with bovine serum albumin (BSA), lysozyme (LYS), and alfalfa leaf protein (ALF). The CTs were of similar compositions, but differed in their mean degree of polymerization (mDP); medium CTs with mDP ~9 and large CTs with mDP ~18. At pH 6.5, large CTs exhibited similar protein precipitation behaviors and were significantly more effective precipitants than medium CTs. All CTs precipitated ALF more effectively than BSA or LYS. Medium CTs exhibited similar capacities to precipitate ALF, but showed small but significant differences in their capacity to precipitate BSA and LYS. Aggregation of CT-protein complexes may have contributed to ALF and BSA, but not LYS precipitation. This study, one of the first to use CTs of confirmed high purity, demonstrated that the mDP of CTs influences protein precipitation efficacy.