Roast-Driven Coffee Proteome Changes Characterized by Bradford Assay, SDS-PAGE, and LC-MS.

ABSTRACT: Coffee proteins are key precursors of roasting flavor. However, heat-driven changes in the bean proteome remain underexplored. This work aimed to investigate these changes and study proteomic markers of the coffee bean. The green and roasted coffee beans were quantified for their total soluble protein and compared by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and liquid chromatography-mass spectrometry (LC-MS) proteomics. The protein profiles identified by LC-MS were processed using principal component analysis (PCA) and partial least-squares discriminant analysis (PLS-DA) modeling to identify possible roast-sensitive protein markers. The alkaline-aided aqueous extract protein concentration was reduced from 14-23 g to 3-10 g/100 g dry weight (DW). SDS-PAGE showed

SUBMITTER: Lu W 

PROVIDER: S-EPMC12896866 | biostudies-literature | 2026 Feb

REPOSITORIES: biostudies-literature