biostudies-literatureTakeyama MMCoordenação de Aperfeicoamento de Pessoal de Nível SuperiorFederal University of the State of Rio de JaneiroNational Council for Scientific and Technological Development4981https://www.ebi.ac.uk/biostudies/studies/S-EPMC9370124biostudies-literatureUnknown27(15)A sequential design strategy was applied to optimize the secretion of pectinases by a <i>Saccharomyces cerevisiae</i> strain, from Brazilian sugarcane liquor vat, on passion fruit residue flour (PFRF), through solid-state fermentation (SSF). A factorial design was performed to determine the influence variables and two rotational central composite designs were executed. The validated experimental result was of 7.1 U mL^-1 using 50% PFRF (<i>w</i>/<i>w</i>), pH 5, 30 °C for 24 h, under static SSF. Polygalacturonase, pectin methyl esterase, pectin-lyase and pectate-lyase activities were 3.5; 0.08; 3.1 and 0.8 U mL^-1, respectively. Shotgun proteomics analysis of the crude extract enabled the identification of two pectin-lyases, one pectate-lyase and a glucosidase. The crudMolecules (Basel, Switzerland)Pectinases Secretion by <i>Saccharomyces cerevisiae</i>: Optimization in Solid-State Fermentation and Identification by a Shotgun Proteomics Approach.PMC9370124001560714/2010-6Carvalho HSEvaristo JAMde Carvalho MCSilva CRKoblitz MGBTakeyama MMNogueira FCSFai AECUetanabaro APTda Costa AMfalsePectinases Secretion by <i>Saccharomyces cerevisiae</i>: Optimization in Solid-State Fermentation and Identification by a Shotgun Proteomics Approach.A sequential design strategy was applied to optimize the secretion of pectinases by a <i>Saccharomyces cerevisiae</i> strain, from Brazilian sugarcane liquor vat, on passion fruit residue flour (PFRF), through solid-state fermentation (SSF). A factorial design was performed to determine the influence variables and two rotational central composite designs were executed. The validated experimental result was of 7.1 U mL^-1 using 50% PFRF (<i>w</i>/<i>w</i>), pH 5, 30 °C for 24 h, under static SSF. Polygalacturonase, pectin methyl esterase, pectin-lyase and pectate-lyase activities were 3.5; 0.08; 3.1 and 0.8 U mL^-1, respectively. Shotgun proteomics analysis of the crude extract enabled the identification of two pectin-lyases, one pectate-lyase and a glucosidase. The crud2022-01-01T00:00:00Z2022 Aug2025-04-18T18:06:12.705Z2025-02-19T03:32:09.496ZS-EPMC93701243595693010.3390/molecules27154981