biostudies-literatureAlbuquerque WState of HesseDeutsche Forschungsgemeinschaft (DFG)LOEWE Center Insect Biotechnology and BioresourcesGerman Ministry of Economic Affairs and Climate Action (BMWK)451https://www.ebi.ac.uk/biostudies/studies/S-EPMC10046487biostudies-literatureUnknown13(3)Thermolabile grape berry proteins such as thaumatin-like proteins (TLPs) and chitinases (CHIs) promote haze formation in bottled wines if not properly fined. As a natural grapevine pest, the spotted-wing fly <i>Drosophila suzukii</i> is a promising source of peptidases that break down grape berry proteins because the larvae develop and feed inside mature berries. Therefore, we produced recombinant TLP and CHI as model thermolabile wine haze proteins and applied a peptidomics strategy to investigate whether <i>D. suzukii</i> larval peptidases were able to digest them under acidic conditions (pH 3.5), which are typically found in winemaking practices. The activity of the novel peptidases was confirmed by mass spectrometry, and cleavage sites within the wine haze proteins were visualized in 3BiomoleculesPeptidomics as a Tool to Assess the Cleavage of Wine Haze Proteins by Peptidases from <i>Drosophila suzukii</i> Larvae.PMC10046487AiF 20911 NINST 162/500-1 FUGGOmokungbe BGross PSpengler BSchneider QAlbuquerque WKessel TGhezellou PZorn HLee KZVilcinskas AGand MfalsePeptidomics as a Tool to Assess the Cleavage of Wine Haze Proteins by Peptidases from <i>Drosophila suzukii</i> Larvae.Thermolabile grape berry proteins such as thaumatin-like proteins (TLPs) and chitinases (CHIs) promote haze formation in bottled wines if not properly fined. As a natural grapevine pest, the spotted-wing fly <i>Drosophila suzukii</i> is a promising source of peptidases that break down grape berry proteins because the larvae develop and feed inside mature berries. Therefore, we produced recombinant TLP and CHI as model thermolabile wine haze proteins and applied a peptidomics strategy to investigate whether <i>D. suzukii</i> larval peptidases were able to digest them under acidic conditions (pH 3.5), which are typically found in winemaking practices. The activity of the novel peptidases was confirmed by mass spectrometry, and cleavage sites within the wine haze proteins were visualized in 32023-01-01T00:00:00Z2023 Feb2026-04-08T14:15:08.153Z2025-02-19T02:38:12.433ZS-EPMC100464873697938610.3390/biom13030451