Accessibility navigation


Relationship between condensed tannin structures and their ability to precipitate feed proteins in the rumen

Lorenz, M. M., Alkhafadji, L., Stringano, E., Nilsson, S., Mueller-Harvey, I. and Uden, P. (2014) Relationship between condensed tannin structures and their ability to precipitate feed proteins in the rumen. Journal of the Science of Food and Agriculture, 94 (5). pp. 963-968. ISSN 0022-5142

Full text not archived in this repository.

It is advisable to refer to the publisher's version if you intend to cite from this work. See Guidance on citing.

To link to this item DOI: 10.1002/jsfa.6344

Abstract/Summary

Abstract BACKGROUND Tannins can bind to and precipitate protein by forming insoluble complexes resistant to fermentation and with a positive effect on protein utilisation by ruminants. Three protein types, Rubisco, rapeseed protein and bovine serum albumin (a single high-molecular weight protein), were used to test the effects of increasing concentrations of structurally different condensed tannins on protein solubility/precipitation. RESULTS Protein type (PT) influenced solubility after addition of condensed tannins (P < 0.001) in the order: Rubisco < rapeseed < BSA (P < 0.05). The type of condensed tannin (CT) affected protein solubility (P = 0.001) with a CT × PT interaction (P = 0.001). Mean degree of polymerisation, proportions of cis- versus trans-flavanol subunits or prodelphinidins versus procyanidins among CTs could not explain precipitation capacities. Increasing tannin concentration decreased protein solubility (P < 0.001) with a PT × CT concentration interaction. The proportion of low-molecular weight rapeseed proteins remaining in solution increased with CT concentration but not with Rubisco. CONCLUSIONS Results of this study suggest that PT and CT type are both of importance for protein precipitation but that the CT structures investigated did not allow identification of parameters that contribute most to precipitation. It is possible that the three-dimensional structures of tannins and proteins may be more important factors in tannin–protein interactions. © 2013 Society of Chemical Industry

Item Type:Article
Refereed:Yes
Divisions:Interdisciplinary Research Centres (IDRCs) > Walker Institute
Life Sciences > School of Agriculture, Policy and Development > Department of Animal Sciences > Animal, Dairy and Food Chain Sciences (ADFCS)- DO NOT USE
ID Code:35413
Uncontrolled Keywords:condensed tannins;flavanol composition;Rubisco;bovine serum albumin;rape seed;Lab on Chip
Publisher:Wiley

University Staff: Request a correction | Centaur Editors: Update this record

Page navigation