P. Galzy

Ecole Nationale Supérieure de Chimie de Montpellier, Montpelhièr, Languedoc-Roussillon, France

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Publications (316)470.93 Total impact

  • P. Galzy · A. Arnaud · F. Vezinhet · A. Chassang ·
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    ABSTRACT: La sporulation est un phénomène de morphogenèse qui comprend au moins trois étapes: la méïose, la différenciation de la paroi de l'asque, la formation des spores. Un certain nombre de facteurs agissant sur la sporulation ont été étudiés: arrêt de la croissance, pH, substrat carboné, oxygène, état physiologique. Les principales étapes morphologiques sont décrites. Des modifications métaboliques ont été mises en évidence: augmentation du Qo2 endogène, variation du Qo2 acétate, augmentation de la teneur en matière sèche et en protéines, accumulation des réserves glucidiques et lipidiques, en particuliers des stérols. L'étude du contrôle génétique de la sporulation est discutée.
    07/2014; 119(sup2):57-69. DOI:10.1080/00378941.1972.10839106
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    ABSTRACT: The exocellular enzyme β-glucosidase of Candida molischiana was studied. This strain is able to ferment soluble cellodextrins. The enzyme was partially purified by ion-exchange chromatography and gel filtration. The molecular weight of this enzyme was 120 000; its optimum pH was between 4 and 4.5 and its optimum temperature was 60 °C. This enzyme was active against different soluble glucosides and was inhibited by p-chloromercuribenzoate, gluconolactone, and glucose. A "glucosyltransferase" activity appeared in the presence of ethanol. The biosynthesis of the enzyme was constitutive but repressed by glucose.
    Biochemistry and Cell Biology 04/2011; 63(11):1160-1166. DOI:10.1139/o85-144 · 2.15 Impact Factor
  • A. Arnaud · Françoise Vezinhet · P. Galzy ·
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    ABSTRACT: Through mutagenesis by nitrous acid a mutant was obtained which differed from the wild strain by two independent characters. The mutant gave smooth colonies on a solid medium containing lactic acid; the wild type yielded rough colonies on the same medium. The smooth colony character was unstable during vegetative growth. The mutant was homothallic. This character was stable during vegetative growth but it was not segregated through meïosis. This mutation inducing homothallism is not controlled by a gene.
    Canadian Journal of Microbiology 02/2011; 17(3):425-428. DOI:10.1139/m71-070 · 1.22 Impact Factor
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    Françoise Vezinhet · A. Arnaud · P. Galzy ·
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    ABSTRACT: During the process of sporulation, the oxidation rate of exogenous carbon source, acetic acid, is high during a period lasting from 1 to 4 h. Then it falls rapidly and the metabolism of acetic acid seems to be deflected. Endogenous oxidation rate rises rapidly at the beginning of the process and reaches its maximum after a 12- to 16-h contact with the sporulation medium. Then it falls regularly.
    Canadian Journal of Microbiology 02/2011; 17(9):1179-1184. DOI:10.1139/m71-188 · 1.22 Impact Factor
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    J. L. Moreau · N. Bernet · A. Arnaud · P. Galzy ·
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    ABSTRACT: Mutants of Brevibacterium sp. R312 were isolated for the production of adipic acid from adiponitrile. One mutant (Ad) with a modified cell wall showed activity against adipamide 3 times greater than the wild type. Another mutant (ACV2) derived from the Ad strain had 30 times more activity on cyano-5-valeric acid, and 7 times more on adipamide, than the wild type. The presence of an amidase acting on amide intermediates in the hydrolysis of dinitriles to organic acids was demonstrated in these mutants.
    Canadian Journal of Microbiology 02/2011; 39(5-5):524-528. DOI:10.1139/m93-074 · 1.22 Impact Factor
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    ABSTRACT: ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.
    ChemInform 04/2010; 22(16). DOI:10.1002/chin.199116080
  • Christel Lambrechts · J. Escudero · P. Galzy ·
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    ABSTRACT: C. LAMBRECHTS, J. ESCUDERO AND P. GALZY. 1995. The esterases of Brevibacterium sp. R312 were found to have an intracellular location. Electrophoresis of lysed cell supernatant fluids revealed seven bands of esterase activity in the presence of α-naphthyl acetate. Eight esterases were separated by anion exchange chromatography. The three main esterases (esterase 4b, 2 and 4a) of Brevibacterium sp. R312 were purified. The molar masses, the pH optima, the temperature optima and heat stabilities were determined. Esterase 2 differed from the two others in sensitivity to inhibitors. Esterase 4b differed from esterases 2 and 4a in its substrate specificity. This enzyme hydrolyses aliphatic and nitrophenyl esters. The spectrum of activity of the two other esterases is narrower. They hydrolysed only naphthyl esters and, in the case of esterase 2, tributyrate and ethyl butyrate.
    Journal of Applied Microbiology 03/2008; 78(2):180 - 188. DOI:10.1111/j.1365-2672.1995.tb02840.x · 2.48 Impact Factor
  • K. Bui · M. Maestracci · A. Thiery · A. Arnaud · P. Galzy ·
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    ABSTRACT: The effect of different compounds on the enzymic action of the nitrile-hydratase used for the bioconversion of nitriles was studied. An excess of acrylonitrile as a substrate was shown to inhibit the activity of the enzyme. This inhibition occurred only at relatively high substrate concentrations (0.2 mol/l or more). The nitrile bioconversion products (acrylamide, propionamide) and their structural analogues (acrylic acid, thioacetamide) were shown to inhibit the enzyme competitively. The most important inhibition found was that of cyanide (Ki= 0.004 mol/l), a break down product of some nitriles. By using an acetamidase-negative mutant, amides were shown to inhibit biosynthesis of nitrile-hydratase. An identical result was obtained with thioacetamide, a non-substrate compound for acetamidase. This compound repressed the biosynthesis of nitrile-hydratase by both the wild type and the acetamidase-negative mutant to the same extent.
    Journal of Applied Microbiology 03/2008; 57(1):183 - 190. DOI:10.1111/j.1365-2672.1984.tb02373.x · 2.48 Impact Factor
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    ABSTRACT: The β-glucosidase of Hanseniaspora vineae was purified by ion-exchange chromatography and gel filtration. Its molecular weight was 295000 PT 15000, its optimum pH was between 6 and 6–5, and its optimum temperature was 55°C. The enzyme was active against different soluble glucosides with β(1–2), β(1–3), β(1–4), β(1–6) and even aP(1–4) configurations. A glucosyltransferase activity appeared in the presence of ethanol. The enzyme was constitutive but its synthesis was repressed by glucose.
    Journal of Applied Microbiology 03/2008; 66(4):271 - 279. DOI:10.1111/j.1365-2672.1989.tb02479.x · 2.48 Impact Factor
  • D. Vivier · R. Ratomahenina · P. Galzy ·
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    ABSTRACT: Five different Micrococcus spp. were isolated from the surface of Roquefort cheese: M. roseus, M. sedentarius, M. lylae, M. luteus and M. varians. During culture on synthetic medium these bacteria produced acetic acid as the main volatile fatty acid and propanol as the main alcohol. On a complex medium these isolates synthesized additional volatile fatty acids. Studies were made of the effect of pH, of water activity adjusted with sodium chloride or sorbitol, and of temperature on growth rates. All five isolates were inhibited at a pH lower than 5.5 and grew at temperatures from 4° to 44°C; they were halotolerant and multiplied at NaCl concentrations up to 20%, corresponding to a water activity of 0.884.
    Journal of Applied Microbiology 03/2008; 76(6):546 - 552. DOI:10.1111/j.1365-2672.1994.tb01651.x · 2.48 Impact Factor
  • Y. Gueguen · P. Chemardin · A. Arnaud · P. Galzy ·
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    ABSTRACT: A yeast strain isolated in the laboratory was studied and classified as a Zygosaccharomyces bailii. Both intracellular and extracellular β-glucosidases of this yeast were purified by ion-exchange chromatography, gel filtration and hydroxylapatite (only for the intracellular enzyme). The tetrameric structure of the two β-glucosidases was determined following treatment of the purified enzyme with dodecyl sulphate. The intracellular β-glucosidase exhibited optimum activity at 65°C and pH 5.5. The extracellular enzyme exhibited optimum catalytic activity at 55°C and pH 5. The molecular mass of purified intracellular and extracellular β-glucosidases, estimated by gel filtration, was 440 and 360 kDa, respectively. Both enzymes are active against glycosides with (1 → 4)-β, (1 → 6)-β and (1 → 4)- linkage configuration. The intracellular enzyme possesses (1 → 6)--arabinofuranosidase activity and extracellular enzyme (1 → 6)--rhamno-pyranosidase activity. The two β-glucosidases are competitively inhibited by glucose and by D-gluconic-acid-lactone and a slight glucosyl transferase activity is observed in the presence of ethanol. Since the glycosides present in wine and fruit juices represent a potential source of aromatic flavour, the possible use of the yeast β-glucosidases for the liberation of the bound aroma is discussed.
    Journal of Applied Microbiology 03/2008; 78(3):270 - 280. DOI:10.1111/j.1365-2672.1995.tb05026.x · 2.48 Impact Factor
  • C. Venturin · J. Zulaika · H. Boze · G. Moulin · P. Galzy ·
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    ABSTRACT: An alcohol dehydrogenase HUADHII was purified 43.2-fold from Hanseniaspora uvarum K5. The enzyme was trimeric with subunits of mol. wt 42 kDa. The N-terminal amino acid sequence of HUADHII has between 45 and 75% identity with part of the sequence of isoenzymes related to group I from Saccharomyces cerevisiae and Kluyveromyces lactis. C2–C4 alcohols and aldehydes were the preferred substrates. The presence of an’’double bond increased the enzyme activity both for alcohols and aldehydes. It was significantly inhibited by metal-binding agents and thiol reagents. Kinetic studies suggested that HUADHII catalyses the oxidation of ethanol by a random sequential mechanism. It appears that HUADHII, a cytoplasmic fermentative enzyme, is structurally and functionally similar to members of the group I alcohol dehydrogenases.
    Journal of Applied Microbiology 03/2008; 79(1):79 - 86. DOI:10.1111/j.1365-2672.1995.tb03127.x · 2.48 Impact Factor
  • Hélène Boze · Guy Moulin · Pierre Galzy ·

    Biotechnology: Enzymes, Biomass, Food and Feed, Volume 9, Second Edition, 03/2008: pages 166 - 220; , ISBN: 9783527620920
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    ABSTRACT: Flavor compounds synthesis by biotechnological processes today plays an increasing role in the food industry. This is the result of scientific advances in biological processes, making use of microorganisms or enzymes as an alternative to chemical synthesis, combined with recent developments in analytical techniques, such as HPLC, gas chromatography (GC), IR, or mass spectrometry. The study of the aromatic potential of some fruits, such as passion fruit, apple, and grapes as well as their fermentation products (juice, wine), has revealed that in addition to a free fraction of volatile terpenols, there exist naturally nonodorous and nonvolatile aroma precursors, which represent an important source of fragant compounds (1–3). An important part of this aromatic pool is composed of terpenylglycosides, whose terpenic residue is β-glucosidically bound to disaccharide glucosides. The sugar moieties have been identified as β-D-glucose, 6-O-α-L-rhamnopyranosyl-β-D-glucopyranose, 6-O-α-L-arabinofuranosyl-β-D-glucopyranose, and 6-O-β-D-apiofuranosyl-β-D-glucopyranose. The aglycon part is frequently formed of terpenols, principally linalool, nerol, and geraniol with in some cases linalool oxides, terpenes diols, and triols (4–6). The presence of a β-glucosidic bond between the terpenic residue and the saccharide has suggested a possible liberation of terpenic molecules by enzymatic catalysis using a β-glucosidase. Such an enzyme has a great potential in the wine and fruit juices industry, since the quantities of bound monoterpenes in most fruit juices and wines are usually relatively high.
    02/2008: pages 323-331;
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    ABSTRACT: Biotransformation of Lmalic acid into Llactic acid was studied in a fluidised bed reactor using cells of Lactobacillus sp. 89 and Leuconostoc oenos ATCC 23278 immobilised in a calcium alginate matrix. The reactor was used in a batch or a continuous manner under a non-oxidising atmosphere. It was shown that 3 mm diameter beads loaded with 6 and 30 mg dry matter per gram of gel were the best operating conditions for Leuconostoc and Lactobacillus respectively. The optimal working conditions were as follows: pH = 3.0–5.0, temperature = 30°C for Lactobacillus and pH = 3.0, temperature = 25°C for Leuconostoc. No inhibition due to lactic acid was observed and the internal diffusional effects were negligible. The short catalyst life that was initially observed with both strains resulted from a depletion in NAD and Mn2+, two basic cofactors for malolactic enzymes. To prevent this detrimental effect, a regeneration process for biocatalyst was proposed.
    Journal of Chemical Technology & Biotechnology 04/2007; 51(1):81 - 95. DOI:10.1002/jctb.280510109 · 2.35 Impact Factor
  • S Demeulle · J P Guiraud · P Galzy ·
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    ABSTRACT: Debaryomyces phaffii possesses an inulinase activity which can be induced by growth on beta-fructosidase and particularly on inulin. The enzyme is located in the cell wall but is easily excreted into the culture medium. Maximum activity on inulin is observed at pH 4 and 50 degrees C. The Km on inulin is 1.2 X 10(-2) M. The enzyme breaks down inulin by splitting off terminal fructosyl units and it is active on sucrose and raffinose.
    Zeitschrift für allgemeine Mikrobiologie 01/2007; 21(3):181-9. DOI:10.1002/jobm.19810210303
  • K Oteng-Gyang · G Moulin · P Galzy ·
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    ABSTRACT: The amylolytic system of Schwanniomyces castellii cultured on a yeast extract starch medium consists of 3 enzymes: an alpha-amylase (molecular weight 40,000), glucoamylase I (molecular weight 90,000), and glucoamylase II (molecular weight 45,000). The properties of the enzymes and the action of enzyme inhibitors were determined.
    Zeitschrift für allgemeine Mikrobiologie 01/2007; 21(7):537-44. DOI:10.1002/jobm.19810210707
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    ABSTRACT: Le métabolisme respiratoire de Kluyveromyces fragilis présente des differénces importantes avec celui de Saccharomyces cerevisiae. L'effect glucose qui est très important chez S. cerevisiae (Ephrussi 1966) est inexistant chez les Kluyveromyces. La concentration en glucose n'a pratiquement pas d'influence sur l'activité respiratoire. Le métabolisme fermentaire des Kluyveromyces est moins actif que celui des Saccharomyces. Il est sensible à l'action inhibitrice de l'air. Cependant l'effet Pasteur est moins important que chez S. cerevisiae. Le métabolisme respiratoire est généralement plus actif que le métabolisme fermentaire (Q) Chez les Kluyveromyces.
    Journal of Basic Microbiology 01/2007; 13(3):193-199. DOI:10.1002/jobm.19730130302 · 1.82 Impact Factor
  • Véronique Apaire · J P Guiraud · P Galzy ·
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    ABSTRACT: Several yeast strains can grow with good yield (0.16 to 0.19 mg protein/mg carbohydrate) on nitrogen supplemented Jerusalem artichoke extract. The most promising strain is Lipomyces starkeyi. Including by-products (pulps, proteins of extract), protein production can reach 2 metric tons/ha.
    Zeitschrift für allgemeine Mikrobiologie 01/2007; 23(4):211-8. DOI:10.1002/jobm.3630230402
  • S. Louis-Eugene · R. Ratomahenina · P. Galzy ·

    Journal of Basic Microbiology 01/2007; 24(3):151-159. DOI:10.1002/jobm.19840240306 · 1.82 Impact Factor

Publication Stats

4k Citations
470.93 Total Impact Points


  • 1973-2008
    • Ecole Nationale Supérieure de Chimie de Montpellier
      Montpelhièr, Languedoc-Roussillon, France
  • 1981-2007
    • Université Montpellier 2 Sciences et Techniques
      • Département des Sciences et Technologies des Industries Alimentaires (STIA)
      Montpelhièr, Languedoc-Roussillon, France
    • Ecole Nationale Supérieure d'Arts et Métiers
      Lutetia Parisorum, Île-de-France, France
  • 1971-2007
    • French National Institute for Agricultural Research
      Lutetia Parisorum, Île-de-France, France
  • 1993-1997
    • École Nationale Supérieure Agronomique
      Alger, Alger, Algeria
  • 1991-1992
    • Pierre and Marie Curie University - Paris 6
      • Centre de génétique moléculaire (CGM) - FRE 3144
      Lutetia Parisorum, Île-de-France, France