当前位置： SCI文献检索 > INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES期刊下所有文献 > Molecular crowding prevents the aggregation of protein-dextran conjugate by inducing structural changes, improves its functional properties, and stabilizes it in nanoemulsions.

Molecular crowding prevents the aggregation of protein-dextran conjugate by inducing structural changes, improves its functional properties, and stabilizes it in nanoemulsions.

Abstract：

:In most of the recent research on emulsions related to food products containing protein-polysaccharide interactions established via the Maillard reaction have been used as emulsifiers. Key challenges in such studies include long reaction times, uncontrollable extent of reaction, and protein denaturation and aggregation. The living cell is inherently crowded molecularly with biomacromolecules, occupying 20-40% of the total volume. In this study, to mimic cellular crowding conditions, we have used polyethylene glycol as a chemical crowding agent. The degree of glycation and the results of sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) indicated that a crowding environment triggers glycosylation and that the glycosylation degree gradually increases (p < 0.05) with increasing PEG concentration, which shortens the reaction time. The surface hydrophobicity of soybean protein isolate (SPI) significant decreased (p < 0.05), and the protein structure gradually unfolded from a helix to a random coil to prevent aggregation of SPI in the crowded environment. The solubility and the emulsifying and antioxidant properties improved upon adding the crowding reagent PEG. The chemical, freeze-thaw, and thermal stabilities of the nanoemulsion-stabilized SPI-dextran conjugate improved with increasing PEG concentration. However, the crowding environment had no effect on the salt stability of nanoemulsions.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Hu M,Liu G,Du X,Zhang X,Qi B,Li Y

doi

10.1016/j.ijbiomac.2020.09.007

subject

Has Abstract

pub_date

2020-12-01 00:00:00

pages

4183-4192

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(20)34359-2

journal_volume

164

pub_type

杂志文章

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