title: Saccharomyces cerevisiae CCMI 885 secretes peptides that inhibit the growth of some non-Saccharomyces wine-related strains.
abstract: The nature of the toxic compounds produced by Saccharomyces cerevisiae CCMI 885 that induce the early death of Hanseniaspora guilliermondii during mixed fermentations, as well as their ability to inhibit the growth of other non-Saccharomyces wine-related strains, was investigated. The killing effect of mixed supernatants towards H. guilliermondii was inactivated by protease treatments, thus revealing the proteinaceous nature of the toxic compounds. Analysis of the protein pattern of mixed supernatants on Tricine SDS-PAGE showed that this S. cerevisiae strain secretes peptides (<10 kDa), which were detected only when death of H. guilliermondii was already established. Death-inducing supernatants were ultrafiltrated by 10 and 2 kDa membranes, respectively, and the inhibitory effect of those permeates were tested in H. guilliermondii cultures. Results indicated that the (2-10) kDa protein fraction of those supernatants seemed to contain antimicrobial peptides active against H. guilliermondii. Thus, the (2-10) kDa protein fraction was concentrated and its inhibitory effect tested against strains of Kluyveromyces marxianus, Kluyveromyces thermotolerans, Torulaspora delbrueckii and H. guilliermondii. Under the growth conditions used for these tests, the (2-10) kDa protein fraction of S. cerevisiae CCMI 885 supernatants exhibited a fungistatic effect against all the strains and a fungicidal effect against K. marxianus.
authors.affiliation: Unidade de Bioenergia, LNEG, Lisboa, Portugal. helena.albergaria@ineti.pt
authors.forename: Helena
authors.initials: H
authors.lastname: Albergaria
authors.forename: Diana
authors.initials: D
authors.lastname: Francisco
authors.forename: Klaus
authors.initials: K
authors.lastname: Gori
authors.forename: Nils
authors.initials: N
authors.lastname: Arneborg
authors.forename: Francisco
authors.initials: F
authors.lastname: Gírio
mesh_terms: D000935:Antifungal Agents / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism* / Q000494:pharmacology*; D004591:Electrophoresis, Polyacrylamide Gel; D005656:Fungal Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism* / Q000494:pharmacology*; D055321:Hanseniaspora / Q000187:drug effects*; D007716:Kluyveromyces / Q000187:drug effects; D050296:Microbial Viability / Q000187:drug effects; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000378:metabolism; D020543:Proteome / Q000032:analysis; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D055319:Torulaspora / Q000187:drug effects; D014920:Wine / Q000382:microbiology
chemical_list: D000935:Antifungal Agents; D005656:Fungal Proteins; D020543:Proteome; D010447:Peptide Hydrolases