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Protein profile of commercial soybean milks analyzed by label-free quantitative proteomics

ABSTRACT: This study compared the protein profile of 15 different commercial soy milks using a label-free quantitative proteomics approach. Proteins related to nutrient reservoir activity, endopeptidase inhibitor activity, lipid binding, and seed maturation contribute the most in terms of percentage mass. Their associated Gene Oontology terms are also enriched. Samples could be clustered into three groups based on their protein composition, with glycinins and beta-conglycinins being the most influential for determining the clustering. Amino acid composition estimated from the proteomics data also reflects the clustering of samples. Twenty allergenic proteins varying in abundance were identified, with Gly m 5 and Gly m 6 being the predominantly abundant allergens.

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ORGANISM(S): Glycine Max

SUBMITTER: Giorgio Arrigoni

LAB HEAD: Giorgio Arrigoni

PROVIDER: PXD023052 | Pride | 2021-03-11

REPOSITORIES: Pride

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Protein profile of commercial soybean milks analyzed by label-free quantitative proteomics.

Battisti Ilaria I Ebinezer Leonard Barnabas LB Lomolino Giovanna G Masi Antonio A Arrigoni Giorgio G

Food chemistry 20210220

The consumption of soy milk is increasing worldwide for its nutritional value and health benefits, however, its protein composition after commercialization is not well known. Technological and thermal treatments to which soy milk is subjected could affect the protein composition of the commercial products. This study compared the protein profile of 15 different commercial soy milks using a label-free quantitative proteomics approach. Proteins related to nutrient reservoir activity, endopeptidase ...[more]

PMID: 33690076

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			Action	DRS
	OxidationMSites.txt	Txt
	Soy_1.raw	Raw
	Soy_10.raw	Raw
	Soy_11.raw	Raw
	Soy_12.raw	Raw