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  • 1
    Electronic Resource
    Electronic Resource
    Incidence of SUC-RTM telomeric repeated genes in brewing and wild wine strains of Saccharomyces (1997)
    Springer
    Current genetics 31 (1997), S. 457-461 
    Details
    ISSN: 1432-0983
    Keywords: Key words Wine yeasts ; Brewing yeasts ; RTM genes ; SUC genes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract When over-expressed, RTM yeast genes confer resistance to the toxicity of molasses. They are found in distiller's and baker's industrial yeasts in multiple copies, scattered on the telomeres and physically linked to the telomeric SUC genes. Because these genes are absent from some laboratory strains, we explored the genomes of other industrial yeasts (brewing strains) and wine wild strains. A collection of 47 wine yeast strains (S. cerevisiae and S. bayanus) and 15 brewing strains, lager, ale and possible ancestors (S. monacensis, S. paradoxus and S. carlsbergensis) were screened for the presence of RTM genes. Only three wine strains and all brewing strains proved to contain RTM sequences in different copy numbers. PCR and chromosome blotting confirm the presence of SUC sequences in tandem with RTM. Moreover, analysis of the entire S. cerevisiae genome sequence shows that three other, non-telomeric, genes related to RTM are scattered on different chromosomes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940050230
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  • 2
    Electronic Resource
    Electronic Resource
    Cloning and sequence analysis of the gene encoding Lactococcus lactis malolactic enzyme: Relationships with malic enzymes (1994)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 116 (1994), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Malolactic enzyme is the key enzyme in the degradation of L-malic acid by lactic acid bacteria. Using degenerated primers designed from the first 20 N-terminal amino acid sequence of lactococcal malolactic enzyme, a 60-bp DNA fragment containing part of the mleS gene was amplified from Lactococcus lactis in a polymerase chain reaction. This specific probe was used to isolate two contiguous fragments covering the gene as a whole. The 1.9-kb region sequenced contains an open reading frame of 1623 bp, coding a putative protein of 540 amino acids. The deduced amino acid sequence reveals that lactococcal putative protein (Mlep) is highly homologous to the malic enzyme of other organisms. Expression of the mleS gene in Escherichia coli results in malolactic activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1994.tb06679.x
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  • 3
    Electronic Resource
    Electronic Resource
    Microbiology of the malolactic fermentation: Molecular aspects (1995)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 126 (1995), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Malolactic fermentation conducted by lactic acid bacteria follows alcoholic fermentation during winemaking, and several positive effects make it indispensable for most wines. Research has focused on the growth and physiology of lactic acid bacteria in wine; resulting in the design of malolactic starter cultures. Future work on these starters will concentrate on aromatic changes as additional criteria for strain selection. Although the main features of the malolactic enzyme and its gene are known, the detailed mechanism of the malolactic reaction remains unclear. Cloning and expression of this activity in enological strains of Saccharomyces cereuisiae might be one of the next most important advances in the control of malic acid degradation in wine.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1995.tb07420.x
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  • 4
    Electronic Resource
    Electronic Resource
    Functional expression in Saccharomyces cerevisiae of the Lactococcus lactis mleS gene encoding the malolactic enzyme (1995)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 125 (1995), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Malolactic fermentation, a crucial step in winemaking, results mostly in degradation by lactic acid bacteria of L-malic acid into L-lactic acid. This direct decarboxylation is catalysed by the malolactic enzyme. Recently we, and others, have cloned the mleS gene of Lactococcus lactis encoding malolactic enzyme. Heterologous expression of mleS in Saccha-romyces cerevisiae was tested to perform simultaneously alcoholic and malolactic fermentations by yeast. mleS gene was cloned in a yeast multicopy vector under a strong promoter. Malolactic activity was present in crude extracts of recombinant yeasts. Malic acid degradation was tested during alcoholic fermentation in synthetic media and must. Yeasts expressing the mleS gene actually produced L-lactate from L-malate; nevertheless malate degradation was far from complete.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1995.tb07332.x
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  • 5
    Electronic Resource
    Electronic Resource
    The tyrosine decarboxylase operon of Lactobacillus brevis IOEB 9809: characterization and conservation in tyramine-producing bacteria (2003)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 229 (2003), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Bacterial genes of tyrosine decarboxylases were recently identified. Here we continued the sequencing of the tyrosine decarboxylase locus of Lactobacillus brevis IOEB 9809 and determined a total of 7979 bp. The sequence contained four complete genes encoding a tyrosyl-tRNA synthetase, the tyrosine decarboxylase, a probable tyrosine permease and a Na+/H+ antiporter. Rapid amplification of cDNA ends (RACE) was employed to determine the 5′-end of mRNAs containing the tyrosine decarboxylase gene. It was located only 34–35 nucleotides upstream of the start codon, suggesting that the preceding tyrosyl-tRNA synthetase gene was transcribed separately. In contrast, reverse transcription-polymerase chain reactions (RT-PCRs) carried out with primers designed to amplify regions spanning gene junctions showed that some mRNAs contained the four genes. Homology searches revealed similar clusters of four genes in the genome sequences of Enterococcus faecalis and Enterococcus faecium. Phylogenetic analyses supported the hypothesis that these genes evolved all together. These data suggest that bacterial tyrosine decarboxylases are encoded in an operon containing four genes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/S0378-1097(03)00787-0
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  • 6
    Electronic Resource
    Electronic Resource
    Molecular analysis of the region encoding the lytic system from Oenococcus oeni temperate bacteriophage φ10MC (1999)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 171 (1999), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Malolactic fermentation by Oenococcus oeni is a crucial step in wine-making. Oe. oeni phages are thought to be responsible for fermentation failures, yet they have received little attention. After a molecular analysis concerning the phage φ10MC integration system, this paper focuses on the lytic system. The attP (phage attachment site)-flanking region has been cloned and sequenced. The 1296-bp lysin gene (Lys) was identified in this region. The deduced amino acid sequence showed classical structural features of phage lysins, and this gene product expressed in Escherichia coli had a lytic activity against Oe. oeni. Downstream of Lys, a second ORF was present (P163). According to its amino acid sequence and the location of its gene, the product could be the φ10MC holin. This study shows that the genomic organization of phage φ10MC attP-flanking regions is very similar to that of other lactic acid bacteriophages.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1999.tb13437.x
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  • 7
    Electronic Resource
    Electronic Resource
    Purification and partial gene sequence of the tyrosine decarboxylase of Lactobacillus brevis IOEB 9809 (2002)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 211 (2002), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Some lactic acid bacteria contain a tyrosine decarboxylase (TDC) which converts tyrosine to tyramine, a biogenic amine frequently encountered in fermented food and wine. Purification and microsequencing of the TDC of Lactobacillus brevis IOEB 9809 allowed us to determine a partial sequence of the TDC gene encoding 264 amino acids of the enzyme. Analysis of this protein sequence revealed typical features of pyridoxal phosphate-dependent amino acid decarboxylases while not any known decarboxylase was closely related to the TDC of L. brevis IOEB 9809. In addition, we could detect other L. brevis strains carrying a TDC gene in a rapid assay based on the polymerase chain reaction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2002.tb11207.x
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  • 8
    Electronic Resource
    Electronic Resource
    Biogenic amines in wines: role of lactic acid bacteria (2001)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 199 (2001), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Biogenic amines have undesirable physiological effects when absorbed at too high a concentration. Several kinds of food and beverages contain biogenic amines. Lactic acid bacteria can decarboxylate amino acids. Since winemaking involves the growth of lactic acid bacteria for malolactic fermentation, biogenic amines may occur. However, not all bacterial strains carry these activities. In the same wine-producing area, some wines may contain very low amounts of biogenic amines while others may have relatively large quantities. It is now possible to detect the presence of undesirable histamine-producing strains by PCR test or DNA probe based on the presence of the gene encoding histidine decarboxylase. Other strains have the ornithine and/or tyrosine decarboxylase. When biogenic amine-producing strains are present, the winemaker is encouraged to inoculate selected malolactic starters to replace the indigenous microflora.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2001.tb10643.x
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  • 9
    Electronic Resource
    Electronic Resource
    Purification and characterization of tyrosine decarboxylase of Lactobacillus brevis IOEB 9809 isolated from wine (2001)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 195 (2001), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Tyrosine decarboxylase (EC 4.1.1.25) (TDC) from the wine Lactobacillus brevis IOEB 9809 was purified by a rapid procedure involving anion exchange chromatography, ultrafiltration and hydrophobic interaction chromatography. The protein comprised two subunits of identical molecular mass (approximately 70 000 Da). Enzyme activity was dependent on exogenously supplied pyridoxal 5′-phosphate and the enzyme was stable at 4°C in the presence of the coenzyme. Optimum pH for the pure enzyme was 5.0. At this pH, TDC exhibited Michaelis–Menten kinetics (Km 0.63 mM, Vmax 998 units) and was highly substrate-specific for l-tyrosine. Other amino acids and L-DOPA are not converted by the protein. Tyramine acted as a mixed non-competitive inhibitor. Significant similarities in some biochemical properties were observed with the corresponding decarboxylase enzyme of Streptococcus faecalis, the sole bacterial TDC described to date.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2001.tb10505.x
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  • 10
    Electronic Resource
    Electronic Resource
    Identification and sequence analysis of the region encoding the site-specific integration system from Leuconostoc œnos (Œnococcus œni) temperate bacteriophage φ10MC (1997)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 147 (1997), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Malolactic fermentation conducted by Leuconostoc œnos is an essential step in winemaking. L. œnos bacteriophages are thought to be responsible for fermentation failures, yet they have received little attention. The integration system of bacteriophage φ10MC in the LOF111 L. œnos strain chromosome was studied and a 1456 bp phage DNA fragment was cloned and sequenced. An open reading frame (int) showing homology with several temperate bacteriophage integrases was located upstream of the phage attachment site (attP). This organisation is comparable to other phage site-specific recombination systems. The same bacterial attachment site (attB) located in a tRNAleu gene was found in all 15 L. œnos strains studied and was involved in φ10MC integration in the bacterial chromosome.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1997.tb10254.x
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