ArticleFoods (Basel, Switzerland)2026
Roast-Driven Coffee Proteome Changes Characterized by Bradford Assay, SDS-PAGE, and LC-MS.
Article in Foods (Basel, Switzerland), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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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 dominant 17-26, 34-43, and 55-72 kDa bands weakened after roasting, while high molecular peaks (>180 kDa) were present only in roasted samples. In-solution tryptic digestion yielded nine protein groups. PCA scores revealed partial separation of green and roasted groups, while PLS-DA delivered unambiguous classification (Q
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