Advanced

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

Lorenz, Martin M.; Alkhafadji, Loy; Stringano, Elisabetta; Nilsson, Staffan LU ; Mueller-Harvey, Irene and Uden, Peter (2014) In Journal of the Science of Food and Agriculture 94(5). p.963-968
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 x PT interaction (P = 0.001). Mean degree of polymerisation, proportions of... (More)
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 x 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 x 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. (c) 2013 Society of Chemical Industry (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Lab on Chip, Rubisco, flavanol composition, bovine serum albumin, condensed tannins, rape seed
in
Journal of the Science of Food and Agriculture
volume
94
issue
5
pages
963 - 968
publisher
Wiley-Blackwell
external identifiers
  • wos:000332520600020
  • scopus:84900630509
ISSN
1097-0010
DOI
10.1002/jsfa.6344
language
English
LU publication?
yes
id
906d64ff-5352-4813-8ef5-3523bcefe95c (old id 4414246)
date added to LUP
2014-04-29 15:44:42
date last changed
2017-10-29 03:53:09
@article{906d64ff-5352-4813-8ef5-3523bcefe95c,
  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 &lt; 0.001) in the order: Rubisco &lt; rapeseed &lt; BSA (P &lt; 0.05). The type of condensed tannin (CT) affected protein solubility (P = 0.001) with a CT x 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 &lt; 0.001) with a PT x 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. (c) 2013 Society of Chemical Industry},
  author       = {Lorenz, Martin M. and Alkhafadji, Loy and Stringano, Elisabetta and Nilsson, Staffan and Mueller-Harvey, Irene and Uden, Peter},
  issn         = {1097-0010},
  keyword      = {Lab on Chip,Rubisco,flavanol composition,bovine serum albumin,condensed tannins,rape seed},
  language     = {eng},
  number       = {5},
  pages        = {963--968},
  publisher    = {Wiley-Blackwell},
  series       = {Journal of the Science of Food and Agriculture},
  title        = {Relationship between condensed tannin structures and their ability to precipitate feed proteins in the rumen},
  url          = {http://dx.doi.org/10.1002/jsfa.6344},
  volume       = {94},
  year         = {2014},
}