Identification and quantification of proteins at adsorption layer of emulsion stabilized by pea protein isolates

Colloids and Surfaces. B, Biointerfaces
Ting XiongYijie Chen

Abstract

This study adopted the method of quantitative proteomics to analyze the adsorbed proteins in oil-in-water emulsions stabilized by pea protein isolate (PPI). Adsorbed proteins were precipitated by an optimized precipitation method and precipitates were labeled and subjected to a reversed-phase high performance liquid chromatography coupled to tandem mass spectrometry (RPLC-ESI-MS/MS) for protein identification and quantification. In total, 77 proteins were identified, of which 49 proteins with significant differences were observed. There were 25 upregulated proteins (fold change > 1) and 24 downregulated proteins (fold change < 1). The interfacial adsorption abilities of these proteins were compared according to the classification of protein families. The results showed that all isoforms of vicilins exhibited high adsorption abilities at the oil-water interface. Compared with vicilin, convicilin showed opposite adsorption capacity. Different legumin families showed significantly different affinities on the oil-water interface. In contrast to albumin-1, albumin-2 was preferentially adsorbed to the interface. The amino acid sequence alignment and hydropathy profile analysis of these proteins showed that the proteins well-balanced ...Continue Reading

Citations

Jan 2, 2020·Foods·Analía A Lu MartínezEristeo García Márquez
Jan 21, 2021·Annual Review of Food Science and Technology·Lutz Grossmann, Jochen Weiss
May 15, 2021·Journal of the Science of Food and Agriculture·Cong JiaJinian Huang
Nov 26, 2020·Food Research International·Tamires Sousa de OliveiraPedro Henrique Campelo

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