Cargando…

Interactions of β-Conglycinin (7S) with Different Phenolic Acids—Impact on Structural Characteristics and Proteolytic Degradation of Proteins

p-Coumalic acid (PCA), caffeic acid (CA), gallic acid (GA) and chlorogenic acid (CGA) are the major phenolic acids that co-exist with soy protein components in foodstuffs. Surprisingly, there are only a handful of reports that describe their interaction with β-Conglycinin (7S), a major soy protein....

Descripción completa

Detalles Bibliográficos
Autores principales: Gan, Jing, Chen, Hao, Liu, Jiyuan, Wang, Yongquan, Nirasawa, Satoru, Cheng, Yongqiang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5085704/
https://www.ncbi.nlm.nih.gov/pubmed/27706090
http://dx.doi.org/10.3390/ijms17101671
_version_ 1782463625473032192
author Gan, Jing
Chen, Hao
Liu, Jiyuan
Wang, Yongquan
Nirasawa, Satoru
Cheng, Yongqiang
author_facet Gan, Jing
Chen, Hao
Liu, Jiyuan
Wang, Yongquan
Nirasawa, Satoru
Cheng, Yongqiang
author_sort Gan, Jing
collection PubMed
description p-Coumalic acid (PCA), caffeic acid (CA), gallic acid (GA) and chlorogenic acid (CGA) are the major phenolic acids that co-exist with soy protein components in foodstuffs. Surprisingly, there are only a handful of reports that describe their interaction with β-Conglycinin (7S), a major soy protein. In this report, we investigated the interaction between phenolic acids and soy protein 7S and observed an interaction between each of these phenolic acids and soy protein 7S, which was carried out by binding. Further analysis revealed that the binding activity of the phenolic acids was structure dependent. Here, the binding affinity of CA and GA towards 7S was found to be stronger than that of PCA, because CA and GA have one more hydroxyl group. Interestingly, the binding of phenolic acids with soy protein 7S did not affect protein digestion by pepsin and trypsin. These findings aid our understanding of the relationship between different phenolic acids and proteins in complex food systems.
format Online
Article
Text
id pubmed-5085704
institution National Center for Biotechnology Information
language English
publishDate 2016
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-50857042016-11-01 Interactions of β-Conglycinin (7S) with Different Phenolic Acids—Impact on Structural Characteristics and Proteolytic Degradation of Proteins Gan, Jing Chen, Hao Liu, Jiyuan Wang, Yongquan Nirasawa, Satoru Cheng, Yongqiang Int J Mol Sci Article p-Coumalic acid (PCA), caffeic acid (CA), gallic acid (GA) and chlorogenic acid (CGA) are the major phenolic acids that co-exist with soy protein components in foodstuffs. Surprisingly, there are only a handful of reports that describe their interaction with β-Conglycinin (7S), a major soy protein. In this report, we investigated the interaction between phenolic acids and soy protein 7S and observed an interaction between each of these phenolic acids and soy protein 7S, which was carried out by binding. Further analysis revealed that the binding activity of the phenolic acids was structure dependent. Here, the binding affinity of CA and GA towards 7S was found to be stronger than that of PCA, because CA and GA have one more hydroxyl group. Interestingly, the binding of phenolic acids with soy protein 7S did not affect protein digestion by pepsin and trypsin. These findings aid our understanding of the relationship between different phenolic acids and proteins in complex food systems. MDPI 2016-10-02 /pmc/articles/PMC5085704/ /pubmed/27706090 http://dx.doi.org/10.3390/ijms17101671 Text en © 2016 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC-BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Gan, Jing
Chen, Hao
Liu, Jiyuan
Wang, Yongquan
Nirasawa, Satoru
Cheng, Yongqiang
Interactions of β-Conglycinin (7S) with Different Phenolic Acids—Impact on Structural Characteristics and Proteolytic Degradation of Proteins
title Interactions of β-Conglycinin (7S) with Different Phenolic Acids—Impact on Structural Characteristics and Proteolytic Degradation of Proteins
title_full Interactions of β-Conglycinin (7S) with Different Phenolic Acids—Impact on Structural Characteristics and Proteolytic Degradation of Proteins
title_fullStr Interactions of β-Conglycinin (7S) with Different Phenolic Acids—Impact on Structural Characteristics and Proteolytic Degradation of Proteins
title_full_unstemmed Interactions of β-Conglycinin (7S) with Different Phenolic Acids—Impact on Structural Characteristics and Proteolytic Degradation of Proteins
title_short Interactions of β-Conglycinin (7S) with Different Phenolic Acids—Impact on Structural Characteristics and Proteolytic Degradation of Proteins
title_sort interactions of β-conglycinin (7s) with different phenolic acids—impact on structural characteristics and proteolytic degradation of proteins
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5085704/
https://www.ncbi.nlm.nih.gov/pubmed/27706090
http://dx.doi.org/10.3390/ijms17101671
work_keys_str_mv AT ganjing interactionsofbconglycinin7swithdifferentphenolicacidsimpactonstructuralcharacteristicsandproteolyticdegradationofproteins
AT chenhao interactionsofbconglycinin7swithdifferentphenolicacidsimpactonstructuralcharacteristicsandproteolyticdegradationofproteins
AT liujiyuan interactionsofbconglycinin7swithdifferentphenolicacidsimpactonstructuralcharacteristicsandproteolyticdegradationofproteins
AT wangyongquan interactionsofbconglycinin7swithdifferentphenolicacidsimpactonstructuralcharacteristicsandproteolyticdegradationofproteins
AT nirasawasatoru interactionsofbconglycinin7swithdifferentphenolicacidsimpactonstructuralcharacteristicsandproteolyticdegradationofproteins
AT chengyongqiang interactionsofbconglycinin7swithdifferentphenolicacidsimpactonstructuralcharacteristicsandproteolyticdegradationofproteins