Torulaspora

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Kenzo Tonomura - One of the best experts on this subject based on the ideXlab platform.

  • purification and characterization ofα glucosidase from Torulaspora pretoriensis yk 1
    Bioscience Biotechnology and Biochemistry, 2014
    Co-Authors: Yuji Oda, Hiroyuki Iwamoto, Keitaro Hiromi, Kenzo Tonomura
    Abstract:

    α-Glucosidase was partially purified 103-fold from a cell-free extract of Torulaspora pretoriensis YK-1 by column chromatography on Toyopearl HW55F, DEAE-Toyopearl 650M, hydroxylapatite and phenyl-Toyopearl 650M. Further purification by preparative polyacrylamide gel electrophoresis (PAGE) gave the homogenous protein, but the specific activity was reduced. The molecular weight of the enzyme was estimated to be 69,000 by SDS-PAGE and 60,000 by gel filtration. Optimum pH and temperature were 6.8 and 35°C, respectively. The enzyme was inhibited strongly by AgNO3, HgCl2, sodium dodecyl sulfate, and N-ethylmaleimide. The Km (mM) for p-nitrophenyl α-D-glucopyranoside, maltose, maltotriose, isomaltose, methyl α-glucoside, and sucrose were 0.15, 150, 45, 17, 18, and 29, and Vmax (μmol/min/mg protein) for those substrates were 87, 0.23, 2.4, 9.0, 12, and 7.4, respectively. The N-terminal amino acid sequence of the enzyme was PEVKNHPETQPKWWKEATVY. The properties of α-glucosidase from T. pretoriensis YK-1 were simil...

  • Reexamination of yeast strains classified as Torulaspora delbrueckii (Lindner)
    International journal of systematic bacteriology, 1997
    Co-Authors: Yuji Oda, Mihe Yabuki, Kenzo Tonomura, Masahito Fukunaga
    Abstract:

    Twenty-eight yeast strains presumed to represent Torulaspora delbrueckii were analyzed by randomly amplified polymorphic DNA-PCR analysis. Four strains (HUT 7161, IFO 1138, IFO 1145, and IFO 1956) that were considerably different from the type strain were further investigated. Morphological and physiological characteristics revealed that strains HUT 7161 and IFO 1145 belong to the genus Debaryomyces rather than the genus Torulaspora, and the former strain may represent Debaryomyces hansenii. Strains IFO 1138 and IFO 1956 were classified as either Saccharomyces castellii or Saccharomyces dairensis by identification keys involving physiological tests. On the basis of analysis of the sequences of two rRNA internal spacer regions, strains IFO 1138 and IFO 1956 were closely related to S. castellii and strains HUT 7161 and IFO 1145 were outside members of the genera Torulaspora, Zygosaccharomyces, and Saccharomyces.

  • Molecular genetic properties of the yeast Torulaspora pretoriensis: characterization of chromosomal DNA and genetic transformation by Saccharomyces cerevisiae-based plasmids.
    Current genetics, 1995
    Co-Authors: Yuji Oda, Kenzo Tonomura
    Abstract:

    Chromosomal DNA banding patterns were obtained for three strains of Torulaspora pretoriensis by contour-clamped homogenous-electric-field gel electrophoresis. Chromosomes were resolved into six or seven bands in the range of 800 to 2000 kb, and a polymorphism of these lengths was observed. By Southern-blot analysis, the three strains were shown to lack the DNA sequences homologous to the URA3, LEU2, TRP1, and HO genes of Saccharomyces cerevisiae. A uracil auxotrophic mutant derived from T. pretoriensis was transformed with three plasmids (YEp24, YRpHI, and YCp50) carrying the URA3 gene of S. cerevisiae by the lithium acetate method.

  • Purification and Characterization of Invertase from Torulaspora pretoriensis YK-1
    Bioscience Biotechnology and Biochemistry, 1994
    Co-Authors: Yuji Oda, Kenzo Tonomura
    Abstract:

    Invertase was purified from Torulaspora pretoriensis YK-1 by acid treatment and column chromatography on DEAE-Toyopearl 650M and phenyl-Toyopearl 650M to homogeneity. The molecular weight of the purified enzyme was estimated to be 130,000 by SDS-polyacrylamide gel electrophoresis and 530,000 by gel filtration. The enzyme contained 50% molecular weight as carbohydrate. Properties of the invertase from T. pretoriensis was similar to external invertase from Saccharomyces cerevisiae.

  • Selection of a Novel Baking Strain from the Torulaspora Yeasts
    Bioscience Biotechnology and Biochemistry, 1993
    Co-Authors: Yuji Oda, Kenzo Tonomura
    Abstract:

    Among the yeasts belonging to the genus Torulaspora, T. pretoriensis IFO 10218 was selected as a maltose-fermenting strain that could leaven dough containing 5% glucose as high as commercial baking strains. The freeze-thaw resistance of this strain in the dough was higher than that of Saccharomyces cerevisiae FL 2209 isolated from commercial compressed yeast. Since the cells of IFO 10218 readily sedimented in their suspension, a dispersing mutant, YK-1, was induced. When YK-1 was cultured in the. presence of NaCl, leavening abilities were reduced, unlike FL 2209. α-Glucosidase activity of YK-1 cells grown on maltose increased slightly, resulting in partly improved leavening ability in the dough without addition of sugar. YK-1 was shown to be a candidate applicable to breadmaking by not only usual method but also the frozen-dough method.

Yuji Oda - One of the best experts on this subject based on the ideXlab platform.

  • purification and characterization ofα glucosidase from Torulaspora pretoriensis yk 1
    Bioscience Biotechnology and Biochemistry, 2014
    Co-Authors: Yuji Oda, Hiroyuki Iwamoto, Keitaro Hiromi, Kenzo Tonomura
    Abstract:

    α-Glucosidase was partially purified 103-fold from a cell-free extract of Torulaspora pretoriensis YK-1 by column chromatography on Toyopearl HW55F, DEAE-Toyopearl 650M, hydroxylapatite and phenyl-Toyopearl 650M. Further purification by preparative polyacrylamide gel electrophoresis (PAGE) gave the homogenous protein, but the specific activity was reduced. The molecular weight of the enzyme was estimated to be 69,000 by SDS-PAGE and 60,000 by gel filtration. Optimum pH and temperature were 6.8 and 35°C, respectively. The enzyme was inhibited strongly by AgNO3, HgCl2, sodium dodecyl sulfate, and N-ethylmaleimide. The Km (mM) for p-nitrophenyl α-D-glucopyranoside, maltose, maltotriose, isomaltose, methyl α-glucoside, and sucrose were 0.15, 150, 45, 17, 18, and 29, and Vmax (μmol/min/mg protein) for those substrates were 87, 0.23, 2.4, 9.0, 12, and 7.4, respectively. The N-terminal amino acid sequence of the enzyme was PEVKNHPETQPKWWKEATVY. The properties of α-glucosidase from T. pretoriensis YK-1 were simil...

  • Isolation and characterization of MELt gene from Torulaspora delbrueckii IFO 1255.
    Yeast (Chichester England), 1999
    Co-Authors: Yuji Oda, Masahito Fukunaga
    Abstract:

    Torulaspora delbrueckii IFO 1255 is a melibiose-fermenting strain in Torulaspora species. From the genome of strain IFO 1255, we obtained a 770 bp fragment by PCR with oligonucleotides synthesized based on the MEL genes of Saccharomyces cerevisiae and its related species. The region encompassing the 770 bp fragment was cloned by inverse PCR and sequenced. The nucleotide sequence revealed an open reading frame of 1422 bp encoding a 474 amino acid protein with a molecular weight of 52 360. The similarity of the presumed mature protein to Saccharomyces species and Zygosaccharomyces cidri alpha-galactosidases was 69.7-73.2% and 58.4%, respectively. The phylogenetic relationship between these species is discussed. The sequence is deposited in the DDBJ/EMBL/GenBank database under Accession No. AB027130.

  • Reexamination of yeast strains classified as Torulaspora delbrueckii (Lindner)
    International journal of systematic bacteriology, 1997
    Co-Authors: Yuji Oda, Mihe Yabuki, Kenzo Tonomura, Masahito Fukunaga
    Abstract:

    Twenty-eight yeast strains presumed to represent Torulaspora delbrueckii were analyzed by randomly amplified polymorphic DNA-PCR analysis. Four strains (HUT 7161, IFO 1138, IFO 1145, and IFO 1956) that were considerably different from the type strain were further investigated. Morphological and physiological characteristics revealed that strains HUT 7161 and IFO 1145 belong to the genus Debaryomyces rather than the genus Torulaspora, and the former strain may represent Debaryomyces hansenii. Strains IFO 1138 and IFO 1956 were classified as either Saccharomyces castellii or Saccharomyces dairensis by identification keys involving physiological tests. On the basis of analysis of the sequences of two rRNA internal spacer regions, strains IFO 1138 and IFO 1956 were closely related to S. castellii and strains HUT 7161 and IFO 1145 were outside members of the genera Torulaspora, Zygosaccharomyces, and Saccharomyces.

  • Molecular genetic properties of the yeast Torulaspora pretoriensis: characterization of chromosomal DNA and genetic transformation by Saccharomyces cerevisiae-based plasmids.
    Current genetics, 1995
    Co-Authors: Yuji Oda, Kenzo Tonomura
    Abstract:

    Chromosomal DNA banding patterns were obtained for three strains of Torulaspora pretoriensis by contour-clamped homogenous-electric-field gel electrophoresis. Chromosomes were resolved into six or seven bands in the range of 800 to 2000 kb, and a polymorphism of these lengths was observed. By Southern-blot analysis, the three strains were shown to lack the DNA sequences homologous to the URA3, LEU2, TRP1, and HO genes of Saccharomyces cerevisiae. A uracil auxotrophic mutant derived from T. pretoriensis was transformed with three plasmids (YEp24, YRpHI, and YCp50) carrying the URA3 gene of S. cerevisiae by the lithium acetate method.

  • Purification and Characterization of Invertase from Torulaspora pretoriensis YK-1
    Bioscience Biotechnology and Biochemistry, 1994
    Co-Authors: Yuji Oda, Kenzo Tonomura
    Abstract:

    Invertase was purified from Torulaspora pretoriensis YK-1 by acid treatment and column chromatography on DEAE-Toyopearl 650M and phenyl-Toyopearl 650M to homogeneity. The molecular weight of the purified enzyme was estimated to be 130,000 by SDS-polyacrylamide gel electrophoresis and 530,000 by gel filtration. The enzyme contained 50% molecular weight as carbohydrate. Properties of the invertase from T. pretoriensis was similar to external invertase from Saccharomyces cerevisiae.

K. Tonomura - One of the best experts on this subject based on the ideXlab platform.

  • α-Galactosidase from the yeast Torulaspora delbrueckii IFO 1255
    Journal of Applied Bacteriology, 1996
    Co-Authors: Y. Oda, K. Tonomura
    Abstract:

    The yeast Torulaspora delbrueckii IFO 1255 was selected as the strain fermenting melibiose from 35 strains of Torulaspora species. The strain IFO 1255 produced extracellular and cell-associated forms of α-galactosidase when grown on either melibiose or galactose as the sole carbon source. Most of the enzyme was located outside of the cell membrane: the periplasmic space, or cell walls, or both. α-Galactosidase was purified to homogeneity from the cell-free extract of the strain IFO 1255 by acid treatment and column chromatography on DEAE-Toyopearl 650M and Butyl-Toyopearl 650M. The molecular weight of the purified enzyme was estimated to be 88 000 by SDS-polyacrylamide gel electrophoresis and 530 000 by gel filtration. The enzyme contained 50% of its molecular weight as carbohydrate. Optimum pH and temperature were 4.5–5.5 and 55°C, respectively. The enzyme was inhibited strongly by Ag2+, Hg2+ and Cu2+ each at 1 mmol 1-1. The Km (μmol 1-1) for p-, o-, m-nitrophenyl α-D-galactopyranoside, melibiose, raffinose and stachyose were 2.8, 1.3, 2.8, 4.2, 170 and 230, respectively, and Vmax (μmol min-1 mg protein-1) for those substrates were 310, 140, 21, 22, 30 and 44, respectively. The properties of α-galactosidase from T. delbrueckii IFO 1255 were similar to those from the related species, Saccharomyces cerevisiae.

  • Electrophoretic karyotyping of the yeast genus Torulaspora
    Letters in applied microbiology, 1995
    Co-Authors: Y. Oda, K. Tonomura
    Abstract:

    Karyotypes of yeast strains in the genus Torulaspora were determined by pulse-field gel electrophoresis and compared with those of the related genus Zygosaccharomyces. The DNA bands ranged from 800 to 1600 kb in T. delbrueckii and 800 to 2000 kb in both T. globosa and T. pretoriensis and those numbers were about six in the three species. The chromosomes of Torulaspora strains comprised relatively smaller size of DNAs than Zygosaccharomyces strains.

Maria João Sousa - One of the best experts on this subject based on the ideXlab platform.

  • The Emerging Role of the Yeast Torulaspora delbrueckii in Bread and Wine Production: Using Genetic Manipulation to Study Molecular Basis of Physiological Responses
    Structure and Function of Food Engineering, 2012
    Co-Authors: Andreia Pacheco, Cecilia Leao, Júlia Santos, Susana R. Chaves, Judite Almeida, Maria João Sousa
    Abstract:

    © 2012 Sousa et al., licensee InTech. This is an open access chapter distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The Emerging Role of the Yeast Torulaspora delbrueckii in Bread and Wine Production: Using Genetic Manipulation to Study Molecular Basis of Physiological Responses

  • Improved gene disruption method for Torulaspora delbrueckii
    FEMS yeast research, 2008
    Co-Authors: Andreia Pacheco, Maria Judite Almeida, Maria João Sousa
    Abstract:

    PCR-based disruption cassettes are one of the most commonly used strategies for gene targeting in Saccharomyces cerevisiae. The efficiencies of gene disruption using this conventional method are highly variable among species, and often quite low with nonconventional yeasts. Here we describe an improved strategy to obtain deletion mutants in baker's yeast Torulaspora delbrueckii, one of the most abundant non-Saccharomyces species, present in home-made corn and rye bread dough.

  • Freeze tolerance of the yeast Torulaspora delbrueckii : cellular and biochemical basis
    FEMS microbiology letters, 2004
    Co-Authors: Cecília Alves-araújo, Maria João Sousa, Maria Judite Almeida, Cecilia Leao
    Abstract:

    The freeze stress responses to prolonged storage at −20 °C in Torulaspora delbrueckii PYCC5323 were investigated. In this yeast, no loss of cell viability was observed for at least 120 days during freezing at −20 °C, whereas a loss of 80% was observed in a commercial baker's yeast after 15 days. In the former strain, freeze resistance was dependent on an adaptation process. The primary cell target of freeze stress was the plasma membrane, preservation of its integrity being related with a lower increase of lipid peroxidation and with a higher resistance to H2O2, but not with the intracellular trehalose concentration.

  • Activity of essential oils from Mediterranean Lamiaceae species against food spoilage yeasts.
    Journal of Food Protection, 2003
    Co-Authors: Cecília Alves Araújo, Maria João Sousa, Manuel Fernandes Ferreira, Cecilia Leao
    Abstract:

    The essential oils from aerial parts of Melissa officinalis, Lavandula angustifolia, Salvia officinalis, and Mentha piperita were analyzed by gas chromatography and gas chromatography–mass spectrometry. Their antimicrobial activities were evaluated against five food spoilage yeasts, Torulaspora delbrueckii, Zygosaccharomyces bailii, Pichia membranifaciens, Dekkera anomala, and Yarrowia lipolytica. Saccharomyces cerevisiae was also used as a reference. The oils were preliminarily screened by a disc diffusion technique, with the most active being the oil from M. officinalis. MICs were determined by the broth dilution method, and the main components of the oils were also tested by this method. The essential oil of M. officinalis at 500 μg/ml completely inhibited the growth of all yeast species. The main component of the oil of M. officinalis is citral (neral plus geranial) (58.3%), which showed a marked fungitoxic effect, contributing to its high activity.

Skye P. Meiring - One of the best experts on this subject based on the ideXlab platform.