The barattiere, a landrace immature melon (Cucumis melo L.) native to the Apulia region in southern Italy, represents a valuable genetic and cultural resource with unique organoleptic properties and high digestibility [1-3]. To support the valorisation of barattiere fruits and deepen the understanding of their metabolic composition, an analytical method for the comprehensive profiling of amino acids (AAs) was developed. A hydrophilic interaction liquid chromatography coupled with high-resolution mass spectrometry (HILIC-ESI-HRMS) method was employed to separate and quantify proteinogenic and non-proteinogenic AAs in different anatomical parts of the fruit (viz., epicarp/mesocarp and placenta). Building upon previous work on the AA profiling, extraction was performed employing a simple and green protocol based on the use of acidified water, thus aligning with sustainable analytical practices [4]. Such an eco-friendly and straightforward extraction method was further enhanced through a systematic experimental design approach, achieving an efficiency of up to 90%. Moreover, a comparative assessment of calibration strategies was conducted, exploring matrix-matched calibration against external calibration in solvent, to refine the quantification of both proteinogenic and non-proteinogenic AAs. Findings indicate no significant differences between the quantitative approaches (p = 0.7), encouraging the adoption of external calibration because of practical advantages in the routine application of the method. The enhanced extraction and quantification protocol allow for a reliable and detailed characterization of AA profiles in barattiere fruits, contributing to the understanding of metabolic composition and nutraceutical potential. Advances to further support the valorisation of traditional Apulian cultivars and their sustainable exploitation in agro-food systems, along with the most relevant findings about the AA-ome of barattiere will be presented in this contribution.
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