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

نویسندگان

  • Jing Gan
  • Hao Chen
  • Jiyuan Liu
  • Yongquan Wang
  • Satoru Nirasawa
  • Yongqiang Cheng
چکیده

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.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Assessment of seed storage protein composition of six Iranian adopted soybean cultivars [Glycine max (L.) Merrill.]

Seed protein quality is an important topic in the production of soybean. The quality of soybean proteins is limited by anti-nutrient proteins and low levels of essential sulfur amino acids. In this study, protein content and solubility of six cultivars were evaluated and seed storage proteins were analyzed using SDS-PAGE and scanning densitometry. The results showed that seed storage protein ba...

متن کامل

Improvement of the Nutritional Value of Soybean [Glycine max (L) Merr.] Seed with Alteration in Protein Subunits of Glycinin (11S Globulin) and β-conglycinin (7S Globulin)

Protein quality in soybean seeds is strongly influenced by nutritional conditions. Glycinin (11S globulin) and β-conglycinin (7S globulin) are the 2 main proteins in soybean seeds. Protein quality of glycinin (11S) is higher than that of β-conglycinin (7S), due to the presence of higher amounts of s-containing amino acids (methionine and cysteine) in glycinin than β-conglycinin. Of the amino ac...

متن کامل

On the surface interactions of proteins with lignin.

Lignins are used often in formulations involving proteins but little is known about the surface interactions between these important biomacromolecules. In this work, we investigate the interactions at the solid-liquid interface of lignin with the two main proteins in soy, glycinin (11S) and β-conglycinin (7S). The extent of adsorption of 11S and 7S onto lignin films and the degree of hydration ...

متن کامل

Identification of epitopes of the β subunit of soybean β-conglycinin that are antigenic in pigs, dogs, rabbits and fish.

BACKGROUND β-Conglycinin (conglycinin) is one of the major seed storage proteins of soybean. Conglycinin is a 7S trimer composed of different combinations of β, α and α' subunits. All subunits of conglycinin have been reported to be allergenic in humans. The goal of this research is to identify epitopes of the β subunit of conglycinin that are antigenic in multiple animal species. RESULTS Ser...

متن کامل

Effects of proteome rebalancing and sulfur nutrition on the accumulation of methionine rich δ-zein in transgenic soybeans

Expression of heterologous methionine-rich proteins to increase the overall sulfur amino acid content of soybean seeds has been only marginally successful, presumably due to low accumulation of transgenes in soybeans or due to gene silencing. Proteome rebalancing of seed proteins has been shown to promote the accumulation of foreign proteins. In this study, we have utilized RNAi technology to s...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره 17  شماره 

صفحات  -

تاریخ انتشار 2016