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1. Organic phosphorus immobilization in microbial biomass controls how N2-fixing trees affect phosphorus bioavailability in two tropical soils

Author

Kittima Waithaisong, Agnès Robin, Valentin L'Huillery, Josiane Abadie, François-Xavier Sauvage, Patrick Chemardin, Louis Mareschal, Jean-Pierre Bouillet, Jean-Paul Laclau, José Leonardo Moraes Gonçalves, and Claude Plassard

Subjects
Enzyme-reactive Po, Bioassay, Acacia mangium, Eucalyptus, Plant P accumulation, Environmental sciences, GE1-350
Abstract

Eucalyptus is the tree most widely planted in tropical countries to satisfy growing demand for wood products, but high yields require high fertilizer inputs. Introducing N2-fixing trees (NFT), such as Acacia mangium, has been proposed to improve soil fertility and aboveground tree biomass in Eucalyptus plantations. In addition to N inputs, NFT species may increase plant P nutrition through increased rates of organic P (Po) cycling. However, the positive effect of acacia on soil P availability and plant P nutrition was found to vary substantially between sites. The ability of acacia to improve P bioavailability might mainly depend on Po sequestration in microbial biomass, preventing Po mineralization by phosphatases and efficient Po recycling. This hypothesis was tested at two tropical sites, Itatinga (Brazil) and Kissoko (Congo) by measuring inorganic phosphate (Pi), Po and enzyme-labile Po in bicarbonate extracts from the topsoil collected from plots with Eucalyptus, acacias, or native vegetation. We used bicarbonate enzyme-labile Po after soil autoclaving as an indicator of microbial Po, and a Eucalyptus bioassay to measure the actual P bioavailability for Eucalyptus seedlings. At Itatinga, bicarbonate-Pi was very low, while Po was the main P form. Enzyme-labile Po was very weak in intact soils and high in autoclaved soils, indicating high immobilization in microbial biomass. At Kissoko, Po was highly enzyme-labile in both intact and autoclaved soils, especially from acacia plots, suggesting very low Po immobilization in microbial biomass. Growth and P accumulations in Eucalyptus seedlings were low in all soils at Itatinga and were the highest in Eucalyptus plants grown in acacia soils at Kissoko. Our results highlight the potential of acacia trees for improving P bioavailability for other tree species if labile Po enrichment in the soil provided by this N2-fixing tree is not locked into the microbial biomass.

Published
2022
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2. A dansyl-derivatized phytic acid analogue as a fluorescent substrate for phytases: experimental and computational approach

Author

Claude Plassard, Herve Quiquampoix, Patrick Chemardin, Josiane Abadie, Jean-Bernard Behr, Christophe Dussouy, Eric Dubreucq, Véronique Perrier, Institut de Chimie Moléculaire de Reims - UMR 7312 (ICMR), SFR Condorcet, Université de Reims Champagne-Ardenne (URCA)-Université de Picardie Jules Verne (UPJV)-Centre National de la Recherche Scientifique (CNRS)-Université de Reims Champagne-Ardenne (URCA)-Université de Picardie Jules Verne (UPJV)-Centre National de la Recherche Scientifique (CNRS)-SFR CAP Santé (Champagne-Ardenne Picardie Santé), Université de Reims Champagne-Ardenne (URCA)-Université de Picardie Jules Verne (UPJV)-Université de Reims Champagne-Ardenne (URCA)-Université de Picardie Jules Verne (UPJV)-Université de Reims Champagne-Ardenne (URCA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Ingénierie des Agro-polymères et Technologies Émergentes (UMR IATE), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université de Montpellier (UM)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Sciences Pour l'Oenologie (SPO), Université de Montpellier (UM)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Ecologie fonctionnelle et biogéochimie des sols et des agro-écosystèmes (UMR Eco&Sols), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Institut de Recherche pour le Développement (IRD)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), UNLOCKP project, ANR-11-BSV7-0015,UNLOCKP,Mobilisation des réserves de Phytate du sol : quelles sont les clefs nécessaires pour accéder au phosphore de ce trésor ?(2011), Université de Reims Champagne-Ardenne (URCA)-Institut de Chimie du CNRS (INC)-SFR CAP Santé (Champagne-Ardenne Picardie Santé), Université de Reims Champagne-Ardenne (URCA)-Université de Reims Champagne-Ardenne (URCA)-Centre National de la Recherche Scientifique (CNRS)-SFR Condorcet, Université de Reims Champagne-Ardenne (URCA)-Centre National de la Recherche Scientifique (CNRS)-Université de Reims Champagne-Ardenne (URCA)-Centre National de la Recherche Scientifique (CNRS), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Université de Montpellier (UM)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Institut Agro - Montpellier SupAgro, Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), Université de Montpellier (UM)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Institut Agro - Montpellier SupAgro, and Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Institut de Recherche pour le Développement (IRD)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Institut Agro - Montpellier SupAgro

Subjects
Models, Molecular, Phytic Acid, Biocompatibility, Phosphate, 01 natural sciences, Biochemistry, Substrate Specificity, Catalysis, chemistry.chemical_compound, Soil, Fertilizer, Artificial substrate, Drug Discovery, PEG ratio, Inositol, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Molecular Biology, Fluorescent Dyes, 6-Phytase, Phytic acid, Inositol-phosphates, Molecular Structure, 010405 organic chemistry, Chemistry, Organic Chemistry, Substrate (chemistry), Combinatorial chemistry, 0104 chemical sciences, 010404 medicinal & biomolecular chemistry, Kinetics, Phosphatidylcholines, Linker, Phytases, Fluorescent tag
Abstract

International audience; A new myo-inositol pentakisphosphate was synthesized, which featured a dansyl group at position C-5. The fluorescent tag was removed from the inositol by a 6-atom spacer to prevent detrimental steric interactions in the catalytic site of phytases. The PEG linker was used in order to enhance hydrophilicity and biocompatibility of the new artificial substrate. Computational studies showed a favorable positioning in the catalytic site of phytases. Enzymatic assays demonstrated that the tethered myo-inositol was processed by two recombinant phytases Phy-A and Phy-C, classified respectively as acid and alkaline phytases, with similar rates of phosphate release compared to their natural substrate.

Published
2021
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3. Wine Thermosensitive Proteins Adsorb First and Better on Bentonite during Fining: Practical Implications and Proposition of Alternative Heat Tests

Author

Philippe Cottereau, Aude Vernhet, Frédéric Charrier, Céline Poncet-Legrand, Eric Meistermann, Patrick Chemardin, Sciences Pour l'Oenologie (SPO), Université de Montpellier (UM)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Institut Français de la Vigne et du Vin (IFV), and French Ministry of Food and Agriculture [Compte d'Affectation Speciale Developpement Agricole et Rural (CasDAR)] 1402

Subjects
hard and soft proteins, Hot Temperature, Food Handling, [SDV]Life Sciences [q-bio], Wine, wine proteins, 01 natural sciences, Fluorescence spectroscopy, bentonite fining, 0404 agricultural biotechnology, Adsorption, Vitis, Practical implications, Plant Proteins, alternative heat tests, haze formation, Chemistry, 010401 analytical chemistry, food and beverages, 04 agricultural and veterinary sciences, General Chemistry, Hydrogen-Ion Concentration, 040401 food science, Accelerated aging, Lower temperature, 0104 chemical sciences, Chemical engineering, Bentonite, General Agricultural and Biological Sciences, [CHIM.OTHE]Chemical Sciences/Other
Abstract

International audience; Bentonite fining is the most popular treatment used to remove proteins in white and rose wines. The usual heat test used to adjust the bentonite dose consists of heating the wine during 30 min at 80 degrees C. At this temperature, all of the proteins are unfolded, and this can lead to an overestimation of the dose. We have shown that proteins adsorb on bentonite in a specific order and, more importantly, that the proteins responsible for haze formation adsorb first. Fluorescence spectroscopy showed that this is due to the structural properties of proteins, which can be classified as hard and soft proteins. Alternative heat tests were performed at a lower temperature (40 degrees C) and showed a better correlation with accelerated aging. These tests were also less dependent upon the wine pH.

Published
2020
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4. The affinity of white wine proteins for bentonite is dependent on the wine composition and is directly related to their thermal stability / sensitivity

Author

Céline Poncet-Legrand, Eric Meistermann, Frédéric Charrier, Patrick Chemardin, Aude Vernhet, Sciences Pour l'Oenologie (SPO), Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Université Montpellier 1 (UM1)-Université de Montpellier (UM)-Institut National de la Recherche Agronomique (INRA), Institut Français de la Vigne et du Vin (IFV), and Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)

Subjects
fining, haze formation, [SDV]Life Sciences [q-bio], wine matrixOenoivas 2019, protein adsorption, ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2019

6. Some applications coming from a new method to concentrate proteins

Author

Patrick Chemardin, Céline Poncet-Legrand, Stéphanie Roi, Francois Xavier Sauvage, Sciences Pour l'Oenologie (SPO), Institut National de la Recherche Agronomique (INRA)-Université de Montpellier (UM)-Université Montpellier 1 (UM1)-Institut de Recherche pour le Développement (IRD [Nouvelle-Calédonie])-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Université Montpellier 1 (UM1)-Institut de Recherche pour le Développement (IRD [Nouvelle-Calédonie])-Institut National de la Recherche Agronomique (INRA)-Université de Montpellier (UM)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Université Montpellier 1 (UM1)-Institut National de la Recherche Agronomique (INRA)-Université de Montpellier (UM)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), and Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Université Montpellier 1 (UM1)-Université de Montpellier (UM)-Institut National de la Recherche Agronomique (INRA)

Subjects
concentration, protéine, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, protein
Abstract

Some applications coming from a new method to concentrate proteins. Macrowine 2016

Published
2016

7. Complete hydrolysis of myo-inositol hexakisphosphate by a novel phytase from Debaryomyces castellii CBS 2923

Author

Patrick Chemardin, Hélène Boze, Santiago Galvez, G. Moulin, Mélanie Ragon, André Aumelas, Ingénierie des Réactions Biologiques, Bio-productions (IR2B), Institut National de la Recherche Agronomique (INRA)-Université Montpellier 2 - Sciences et Techniques (UM2), Centre de Biochimie Structurale [Montpellier] (CBS), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Institut National de la Santé et de la Recherche Médicale (INSERM), and Université Montpellier 2 - Sciences et Techniques (UM2)-Institut National de la Recherche Agronomique (INRA)

Subjects
Debaryomyces castellii, Phytic Acid, Applied Microbiology and Biotechnology, Phosphates, Substrate Specificity, 03 medical and health sciences, Hydrolysis, chemistry.chemical_compound, Enzyme Stability, HPIC, Inositol, Inositol phosphate, 030304 developmental biology, chemistry.chemical_classification, 6-Phytase, 0303 health sciences, Phytic acid, Chromatography, biology, 030306 microbiology, Chemistry, Hydrophilic interaction chromatography, Phytate degradation, Debaryomyces, Temperature, General Medicine, Hydrogen-Ion Concentration, Enzyme characterization, Phytase, biology.organism_classification, Phosphate, Yeast, NMR, Kinetics, [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology, Biochemistry, Saccharomycetales, Inositol phosphates, Chromatography, Liquid, Biotechnology
Abstract

correspondance: boze@supagro.inra.fr; International audience; Debaryomyces castellii phytase was purified to homogeneity in a single step by hydrophobic interaction chromatography. Its molecular mass is 74 kDa with 28.8% glycosylation. Its activity was optimal at 60°C and pH 4.0. The Km value for sodium phytate was 0.532 mM. The enzyme exhibited a low specificity and hydrolyzed many phosphate esters. The phytase fully hydrolyzed myo-inositol hexakisphosphate (or phytic acid, Ins P6) to inositol and inorganic phosphate. The sequence of Ins P6 hydrolysis was determined by combining results from high-performance ionic chromatography and nuclear magnetic resonance. D. castellii phytase is a 3-phytase that sequentially releases phosphate groups through Ins (1,2,4,5,6) P5, Ins (1,2,5,6) P4, Ins (1,2,6) P3, Ins (1,2) P2, Ins (1 or 2) P1, and inositol (notation 3/4/5/6/1 or 2).

Published
2008
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8. NMR structure of rALF-Pm3, an anti-lipopolysaccharide factor from shrimp: Model of the possible lipid A-binding site

Author

Delphine Destoumieux-Garzón, Hélène Boze, André Padilla, Yinshan Yang, André Aumelas, Yannick Gueguen, Françoise Roquet, Patrick Chemardin, Martine Pugnière, Evelyne Bachère, Guy Moulin, Anchalee Tassanakajon, Ningxia Medical College, Algorithms and Scheduling for Distributed Heterogeneous Platforms (GRAAL), Inria Grenoble - Rhône-Alpes, Institut National de Recherche en Informatique et en Automatique (Inria)-Institut National de Recherche en Informatique et en Automatique (Inria)-Laboratoire de l'Informatique du Parallélisme (LIP), École normale supérieure de Lyon (ENS de Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de Recherche en Informatique et en Automatique (Inria)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure de Lyon (ENS de Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Beijing Institute of Technology (BIT), Centre de Biochimie Structurale [Montpellier] (CBS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), School of Physics and Astronomy [Nottingham], University of Nottingham, UK (UON), CSIR National Institute of Oceanography [India] (NIO), Institut de Recherche en Infectiologie de Montpellier (IRIM), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Ecosystèmes lagunaires : organisation biologique et fonctionnement (ECOLAG), Université Montpellier 2 - Sciences et Techniques (UM2)-Institut Français de Recherche pour l'Exploitation de la Mer (IFREMER)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de chimie et biochimie des substances naturelles, Muséum national d'Histoire naturelle (MNHN)-Centre National de la Recherche Scientifique (CNRS), Laboratoire Genome Population & Interactions, Université Montpellier 2 - Sciences et Techniques (UM2)-ORSTOM-Centre National de la Recherche Scientifique (CNRS), École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de Recherche en Informatique et en Automatique (Inria)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre National de la Recherche Scientifique (CNRS)-Muséum national d'Histoire naturelle (MNHN), and PADILLA, André

Subjects
Models, Molecular, LIPID A, STRUCTURE, [SDV.BIO]Life Sciences [q-bio]/Biotechnology, Invertebrate Hormones, LIPOPOLYSACCHARIDE, Crystallography, X-Ray, Biochemistry, Penaeus monodon, Lipid A, Crustacea, Septic shock, SURFACE PLASMON RESONANCE ULTRACENTRIFUGATION, Surface plasmon resonance, [INFO.INFO-BT]Computer Science [cs]/Biotechnology, ANTI-LIPOPOLYSACCHARIDE FACTOR, Tachypleus tridentatus, 0303 health sciences, Anti lipopolysaccharide factor, biology, Chemistry, 030302 biochemistry & molecular biology, digestive, oral, and skin physiology, General Medicine, Ultracentrifuge, Protein Binding, Molecular Sequence Data, Biophysics, Lipopolysaccharide, Pichia pastoris, Biomaterials, 03 medical and health sciences, Animals, Amino Acid Sequence, Binding site, Nuclear Magnetic Resonance, Biomolecular, 030304 developmental biology, Binding Sites, Organic Chemistry, SEPTIC SHOCK, Structure, Surface Plasmon Resonance, biology.organism_classification, NMR, Protein Structure, Tertiary, [SDV.BIO] Life Sciences [q-bio]/Biotechnology, [INFO.INFO-BT] Computer Science [cs]/Biotechnology, POLYSACCHARIDE, Structural Homology, Protein, Limulus, Sequence Alignment, Ultracentrifugation
Abstract

Correspondance auteur: Aumelas A. E-mail: aumelas@cbs.cnrs.fr; International audience; The anti-lipopolysaccharide factor ALF-Pm3 is a 98-residue protein identified in hemocytes from the black tiger shrimp Penaeus monodon. It was expressed in Pichia pastoris from the constitutive glyceraldehyde-3-phosphate dehydrogenase promoter as a folded and N-15 uniformly labeled rALF-Pm3 protein. Its 3D structure was established by NMR and consists of three alpha-helices packed against a four-stranded beta-sheet. The C-34-C-55 disulfide bond was shown to be essential for the structure stability. By using surface plasmon resonance, we demonstrated that rALF-Pm3 binds to LPS, lipid A and to OM(R)-174, a soluble analogue of lipid A. Biophysical studies of rALF-Pm3/LPS and rALF-Pm3/OM(R)-174 complexes indicated rather high molecular sized aggregates, which prevented us to experimentally determine by NMR the binding mode of these lipids to rALF-Pm3. However, on the basis of striking structural similarities to the FhuA/LPS complex, we designed an original model of the possible lipid A-binding site of ALF-Pm3. Such a binding site, located on the ALF-Pm3 beta-sheet and involving seven charged residues, is well conserved in ALF-L from Limulus polyphemus and in ALF-T from Tachypleus tridentatus. In addition, our model is in agreement with experiments showing that beta-hairpin synthetic peptides corresponding to ALF-L beta-sheet bind to LPS. Delineating lipid A-binding site of ALFs will help go further in the de novo design of new antibacterial or LPS-neutralizing drugs

Published
2009
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9. Molecular gene cloning and overexpression of the phytase from Debaryomyces castellii CBS 2923

Author

Mélanie Ragon, Patrick Chemardin, Virginie Neugnot-Roux, Hélène Boze, G. Moulin, Ingénierie des Réactions Biologiques, Bio-productions (IR2B), Université Montpellier 2 - Sciences et Techniques (UM2)-Institut National de la Recherche Agronomique (INRA), and Adisseo France SAS

Subjects
Signal peptide, Debaryomyces castellii, Gene isolation, Molecular Sequence Data, Molecular cloning, Pichia, Pichia pastoris, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Amino Acid Sequence, Cloning, Molecular, Gene, Phylogeny, 6-Phytase, biology, Base Sequence, biology.organism_classification, Phytase, Molecular biology, Yeast, Recombinant Proteins, Alcohol oxidase, Kinetics, Biochemistry, Saccharomycetales, Heterologous expression, Biotechnology
Abstract

The ORF encoding the Debaryomyces castellii CBS 2923 phytase was isolated. The deduced 461-amino-acid sequence corresponded to a 51.2 kDa protein and contained the consensus motif (RHGXRXP) which is conserved among phytases. No signal sequence cleavage site was detected. Nine potential N -glycosylation sites have been predicted. The protein shared 21–69% sequence identities with various phytases of yeast or fungal origin. Heterologous expression of the D. castellii CBS 2923 phytase in the methylotrophic yeast Pichia pastoris was tested under both the P. pastoris inducible alcohol oxidase (AOX1) promoter and the constitutive glyceraldehyde-3-phosphate dehydrogenase (GAP) promoter. Maximum production levels obtained were 476 U ml −1 , with the AOX1 expression system and 16.5 U ml −1 with the GAP one. These productions corresponded to a 320-fold and a 10-fold overexpression of the protein, respectively as compared to the homologous production. The biochemical characteristics of the recombinant phytase were identical to those of the native enzyme.

Published
2008
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