Correlation Engine 2.0
Clear Search sequence regions

Sizes of these terms reflect their relevance to your search.

The solution turbidity and intrinsic fluorescence quenching increased after procyanidin was mixed with lactoferrin. The addition of procyanidin also caused a reduction in the surface hydrophobicity of the lactoferrin, suggesting procyanidin bound to non-polar patches on lactoferrin's surfaces. Moreover, the binding interaction caused an appreciable alteration in the structure of both the polyphenol and protein. Thermodynamic analysis indicated the interaction was spontaneous and mainly driven by entropy changes, suggesting that hydrophobic interactions dominated. A computational docking simulation provided insights into the location of the most-likely binding sites on the protein, as well as the nature of the interaction forces involved. In particular, both hydrophobic and hydrogen bonding were found to be important. The binding of the procyanidin to the lactoferrin enhanced its foaming properties. These results may lead to the development of a new class of natural functional ingredients that can be used in food products to improve their quality attributes. Copyright © 2020. Published by Elsevier Ltd.


Changhong Li, Taotao Dai, Jun Chen, Xin Li, Ti Li, Chengmei Liu, David Julian McClements. Protein-polyphenol functional ingredients: The foaming properties of lactoferrin are enhanced by forming complexes with procyanidin. Food chemistry. 2021 Mar 01;339:128145

Expand section icon Mesh Tags

Expand section icon Substances

PMID: 33152895

View Full Text