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Preliminary Results on the Peptidomic Characterization of Traditional Greek PDO Cheeses from the Thessaly Region

Year: 2026

Type: article

Abstract: This study presents the first preliminary biopeptide profiling of three Thessalian PDO cheeses (Kaseri, Manouri, and Batzos) using HPLC-ESI-MS coupled with in silico bioactivity prediction. The three cheeses were chosen as representative Thessalian PDO cheeses made from sheep and/or goat milk, reflecting the traditional dairy practices and regional identity of this area. A total of 212 peptide masses were putatively identified (86 in Kaseri, 85 in Batzos, 41 in Manouri), mainly originating from β-casein (45%) and αs1-casein (30%), indicating region-specific proteolysis driven by processing technologies and microbial ecology. Kaseri exhibited the greatest peptidomic diversity (31 bioactive peptides), whereas Manouri exhibited the greatest frequency of bioactive peptides (34/41; 83%), dominated by DPP-IV-inhibitory peptides (44%). Batzos displayed a balanced ACE and DPP-IV-inhibitory profile typical of brine-ripened cheeses. Screening with MBPDB, BIOPEP-UWM, and PeptideRanker identified 80 known bioactive peptides and 98 uncharacterized sequences, nine common across all cheeses. Peptide length distribution showed consistent proportions of tri- and tetrapeptides (16–19% and 5–7%), with Kaseri enriched in longer sequences (≥6 aa; 60.5%). Batzos peptides, not found in databases, with high PeptideRanker scores (>0.75) suggest potential authentication markers. These preliminary findings provide a basis for further investigation of the peptide profiles and potential bioactivities of Thessalian PDO cheeses.

Source: Sci

DOI: 10.3390/sci8090226