title: A proteomic approach to studying biogenic amine producing lactic acid bacteria.
abstract: All fermented foods are subject to the risk of biogenic amine contamination. Histamine and tyramine are among the most toxic amines for consumers' health, exerting undesirable effects on the central nervous and vascular systems, but putrescine and cadaverine can also compromise the organoleptic properties of contaminated foods. These compounds are produced by fermenting microbial flora that decarboxylate amino acids to amines. Little is known of the factors which induce biosynthesis of decarboxylating enzymes and/or which modulate their catalytic activity: the accumulation of amines is generally considered to be a mechanism that contrasts an acidic environment and/or that produces metabolic energy through coupling amino acid decarboxylation with electrogenic amino acid/amine antiporters. Two Lactobacillus strains, Lactobacillus sp. 30a (ATCC 33222), and a Lactobacillus sp. strain (w53) isolated from amine-contaminated wine, carrying genetic determinants for histidine decarboxylase (HDC) and ornithine decarboxylase (ODC), were studied and the influence of some environmental and nutritional parameters on amine production and protein biosynthesis was analyzed through a proteomic approach; this is the first report of a proteomic analysis of amine-producing bacteria. HDC and ODC biosynthesis were shown to be closely dependent on the presence of high concentrations of free amino acids in the growth medium and to be modulated by the growth phase. The stationary phase and high amounts of free amino acids also strongly induced the biosynthesis of an oligopeptide transport protein belonging to the proteolytic system of Lactic Acid Bacteria. At least two isoforms of glyceraldehyde-3-phosphate dehydrogenase, with different M(r), pI and expression profiles, were identified from Lactobacillus sp. w53: the biosynthesis of one isoform, in particular, is apparently repressed by high concentrations of free amino acids. Other proteins were identified from the Lactobacillus proteome, affording a global knowledge of protein biosynthesis modulation during biogenic amine production.
authors.affiliation: Dipartimento di Biologia Animale e dell'Uomo, Università di Torino, Turin, Italy. enrica.pessione@unito.it
authors.forename: Enrica
authors.initials: E
authors.lastname: Pessione
authors.forename: Roberto
authors.initials: R
authors.lastname: Mazzoli
authors.forename: Maria Gabriella
authors.initials: MG
authors.lastname: Giuffrida
authors.forename: Cristina
authors.initials: C
authors.lastname: Lamberti
authors.forename: Emilia
authors.initials: E
authors.lastname: Garcia-Moruno
authors.forename: Cristina
authors.initials: C
authors.lastname: Barello
authors.forename: Amedeo
authors.initials: A
authors.lastname: Conti
authors.forename: Carlo
authors.initials: C
authors.lastname: Giunta
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000378:metabolism; D001679:Biogenic Amines / Q000096:biosynthesis*; D003470:Culture Media; D015180:Electrophoresis, Gel, Two-Dimensional; D006640:Histidine Decarboxylase / Q000096:biosynthesis*; D007527:Isoenzymes / Q000096:biosynthesis; D007778:Lactobacillus / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D008969:Molecular Sequence Data; D009955:Ornithine Decarboxylase / Q000096:biosynthesis*; D020543:Proteome / Q000032:analysis; D040901:Proteomics; D014920:Wine / Q000382:microbiology
chemical_list: D000596:Amino Acids; D001679:Biogenic Amines; D003470:Culture Media; D007527:Isoenzymes; D020543:Proteome; D009955:Ornithine Decarboxylase; D006640:Histidine Decarboxylase